seqwords.seq

emboss的linux版本的源代码

ID   ACEA_ECOLI     STANDARD;      PRT;   434 AA.
AC   P05313;
DT   01-NOV-1988 (Rel. 09, Created)
DT   01-NOV-1988 (Rel. 09, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   ISOCITRATE LYASE (EC 4.1.3.1) (ISOCITRASE) (ISOCITRATASE) (ICL).
GN   ACEA OR ICL.
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae;
OC   Escherichia.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12;
RX   MEDLINE; 89083515.
RA   Byrne C.R., Stokes H.W., Ward K.A.;
RT   "Nucleotide sequence of the aceB gene encoding malate synthase A in
RT   Escherichia coli.";
RL   Nucleic Acids Res. 16:10924-10924(1988).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12;
RX   MEDLINE; 88262573.
RA   Rieul C., Bleicher F., Duclos B., Cortay J.-C., Cozzone A.J.;
RT   "Nucleotide sequence of the aceA gene coding for isocitrate lyase in
RT   Escherichia coli.";
RL   Nucleic Acids Res. 16:5689-5689(1988).
RN   [3]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 89008064.
RA   Matsuoka M., McFadden B.A.;
RT   "Isolation, hyperexpression, and sequencing of the aceA gene encoding
RT   isocitrate lyase in Escherichia coli.";
RL   J. Bacteriol. 170:4528-4536(1988).
RN   [4]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12 / MG1655;
RX   MEDLINE; 94089392.
RA   Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J.,
RA   Daniels D.L.;
RT   "Analysis of the Escherichia coli genome. IV. DNA sequence of the
RT   region from 89.2 to 92.8 minutes.";
RL   Nucleic Acids Res. 21:5408-5417(1993).
RN   [5]
RP   SEQUENCE OF 293-434 FROM N.A.
RX   MEDLINE; 88227861.
RA   Klumpp D.J., Plank D.W., Bowdin L.J., Stueland C.S., Chung T.,
RA   Laporte D.C.;
RT   "Nucleotide sequence of aceK, the gene encoding isocitrate
RT   dehydrogenase kinase/phosphatase.";
RL   J. Bacteriol. 170:2763-2769(1988).
RN   [6]
RP   PHOSPHORYLATION.
RX   MEDLINE; 88115398.
RA   Robertson E.F., Hoyt J.C., Reeves H.C.;
RT   "Evidence of histidine phosphorylation in isocitrate lyase from
RT   Escherichia coli.";
RL   J. Biol. Chem. 263:2477-2488(1988).
RN   [7]
RP   CHARACTERIZATION.
RX   MEDLINE; 88269580.
RA   Hoyt J.C., Robertson E.F., Berlyn K.A., Reeves H.C.;
RT   "Escherichia coli isocitrate lyase: properties and comparisons.";
RL   Biochim. Biophys. Acta 966:30-35(1988).
RN   [8]
RP   MUTAGENESIS OF CYS-195.
RC   STRAIN=ML308;
RX   MEDLINE; 95126911.
RA   Robertson A.G., Nimmo H.G.;
RT   "Site-directed mutagenesis of cysteine-195 in isocitrate lyase from
RT   Escherichia coli ML308.";
RL   Biochem. J. 305:239-244(1995).
CC   -!- CATALYTIC ACTIVITY: ISOCITRATE = SUCCINATE + GLYOXYLATE.
CC   -!- COFACTOR: REQUIRES DIVALENT CATIONS.
CC   -!- ENZYME REGULATION: IS ACTIVATED BY PHOSPHORYLATION (ON HISTIDINE)
CC       AND IS INHIBITED BY PEP, 3-PHOSPHOGLYCERATE AND SUCCINATE.
CC   -!- PATHWAY: FIRST STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE
CC       TRICARBOXYLIC ACID CYCLE (IN BACTERIA, PLANTS, AND FUNGI).
CC   -!- SUBUNIT: HOMOTETRAMER.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC.
CC   -!- SIMILARITY: BELONGS TO THE ISOCITRATE LYASE FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to [e-mail]).
CC   --------------------------------------------------------------------------
DR   EMBL; X12431; CAA30974.1; -.
DR   EMBL; X07543; CAA30416.1; -.
DR   EMBL; M20714; AAA24009.1; -.
DR   EMBL; U00006; AAC43109.1; -.
DR   EMBL; AE000474; AAC76985.1; -.
DR   EMBL; M22621; AAC13650.1; -.
DR   PIR; S05692; WZECIC.
DR   SWISS-2DPAGE; P05313; COLI.
DR   ECOGENE; EG10022; ACEA.
DR   INTERPRO; IPR000918; -.
DR   PFAM; PF00463; ICL; 2.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
KW   Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Phosphorylation.
FT   ACT_SITE    195    195       PROBABLE.
FT   MUTAGEN     195    195       C->A: LARGE DECREASE IN ACTIVITY.
FT   MUTAGEN     195    195       C->S: LARGE DECREASE IN ACTIVITY.
FT   CONFLICT    101    117       LAASMYPDQSLYPANSV -> WRPACIRISRSIRQTRC
FT                                (IN REF. 2).
FT   CONFLICT    215    215       A -> P (IN REF. 2).
FT   CONFLICT    293    293       P -> R (IN REF. 5).
FT   CONFLICT    338    338       Q -> E (IN REF. 2).
FT   CONFLICT    419    434       TSSVTALTGSTEESQF -> DVFSHRADRLH
FT                                (IN REF. 3).
SQ   SEQUENCE   434 AA;  47521 MW;  F66449CCD1E168E9 CRC64;
     MKTRTQQIEE LQKEWTQPRW EGITRPYSAE DVVKLRGSVN PECTLAQLGA AKMWRLLHGE
     SKKGYINSLG ALTGGQALQQ AKAGIEAVYL SGWQVAADAN LAASMYPDQS LYPANSVPAV
     VERINNTFRR ADQIQWSAGI EPGDPRYVDY FLPIVADAEA GFGGVLNAFE LMKAMIEAGA
     AAVHFEDQLA SVKKCGHMGG KVLVPTQEAI QKLVAARLAA DVTGVPTLLV ARTDADAADL
     ITSDCDPYDS EFITGERTSE GFFRTHAGIE QAISRGLAYA PYADLVWCET STPDLELARR
     FAQAIHAKYP GKLLAYNCSP SFNWQKNLDD KTIASFQQQL SDMGYKFQFI TLAGIHSMWF
     NMFDLANAYA QGEGMKHYVE KVQQPEFAAA KDGYTFVSHQ QEVGTGYFDK VTTIIQGGTS
     SVTALTGSTE ESQF
//
ID   ALR1_YEAST     STANDARD;      PRT;   859 AA.
AC   Q08269; Q02811;
DT   01-NOV-1997 (Rel. 35, Created)
DT   01-NOV-1997 (Rel. 35, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   ALUMINIUM RESISTANCE PROTEIN 1.
GN   ALR1 OR YOL130W.
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Ascomycota; Saccharomycetes; Saccharomycetales;
OC   Saccharomycetaceae; Saccharomyces.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=S288C / FY1679;
RX   MEDLINE; 97051588.
RA   Casamayor A., Khalid H., Balcells L., Aldea M., Casas C.,
RA   Herrero E., Arino J.;
RT   "Sequence analysis of a 13.4 kbp fragment from the left arm of
RT   chromosome XV reveals a malate dehydrogenase gene, a putative Ser/Thr
RT   protein kinase, the ribosomal L25 gene and four new open reading
RT   frames.";
RL   Yeast 12:1013-1020(1996).
RN   [2]
RP   IDENTIFICATION.
RA   McDiarmid C.W., Gardner R.C.;
RL   Unpublished observations (XXX-1995).
CC   -!- SIMILARITY: STRONG, TO YEAST ALR2. AND ALSO SIMILAR TO MNR2.
CC   -!- SIMILARITY: SOME, TO E.COLI CORA.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to [e-mail]).
CC   --------------------------------------------------------------------------
DR   EMBL; Z74872; CAA99150.1; -.
DR   EMBL; Z74871; CAA99149.1; -.
DR   EMBL; U41293; AAC49462.1; -.
DR   SGD; L0002887; ALR1.
DR   INTERPRO; IPR002523; -.
DR   PFAM; PF01544; CorA; 1.
KW   Transmembrane.
FT   TRANSMEM    744    764       POTENTIAL.
FT   TRANSMEM    773    793       POTENTIAL.
FT   CONFLICT     13     13       N -> Y (IN AAC49462).
SQ   SEQUENCE   859 AA;  95869 MW;  6DA44CA70EFA2693 CRC64;
     MSSSSSSSES SPNLSRSNSL ANTMVSMKTE DHTGLYDHRQ HPDSLPVRHQ PPTLKNKEIA
     KSTKPSIPKE QKSATRYNSH VDVGSVPSRG RMDFEDEGQG MDETVAHHQL RASAILTSNA
     RPSRLAHSMP HQRQLYVESN IHTPPKDVGV KRDYTMSSST ASSGNKSKLS ASSSASPITK
     VRKSSLVSPV LEIPHESKSD THSKLAKPKK RTYSTTSAHS SINPAVLLTK STSQKSDADD
     DTLERKPVRM NTRASFDSDV SQASRDSQET EEDVCFPMPP QLHTRVNGID FDELEEYAQF
     ANAEKSQFLA SLQVPNEQKY SNVSQDIGFT SSTSTSGSSA ALKYTPRVSQ TGEKSESTNE
     TEIHEKKEDE HEKIKPSLHP GISFGKNKVE GEENENIPSN DPAYCSYQGT DFQIPNRFSF
     FCSESDETVH ASDIPSLVSE GQTFYELFRG GEPTWWLDCS CPTDDEMRCI AKAFGIHPLT
     AEDIRMQETR EKVELFKSYY FVCFHTFEND KESEDFLEPI NVYIVVCRSG VLTFHFGPIS
     HCANVRRRVR QLRDYVNVNS DWLCYALIDD ITDSFAPVIQ SIEYEADAIE DSVFMARDMD
     FAAMLQRIGE SRRKTMTLMR LLSGKADVIK MFAKRCQDEA NGIGPALTSQ INIANLQARQ
     DNASHIKNNS STTVPNNYAP TTSQPRGDIA LYLGDIQDHL LTMFQNLLAY EKIFSRSHTN
     YLAQLQVESF NSNNKVTEML GKVTMIGTML VPLNVITGLF GMNVKVPGEN SSIAWWFGIL
     GVLLLLAVLG WFLASYWIKR IDPPATLNEA AESGAKSVIS SFLPKRNKRF NDRSKNINVR
     AGPSNKSVAS LPSRYSRYD
//
ID   GOX_SPIOL      STANDARD;      PRT;   369 AA.
AC   P05414;
DT   01-NOV-1988 (Rel. 09, Created)
DT   01-NOV-1988 (Rel. 09, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   (S)-2-HYDROXY-ACID OXIDASE, PEROXISOMAL (EC 1.1.3.15) (GLYCOLATE
DE   OXIDASE) (GOX) (SHORT CHAIN ALPHA-HYDROXY ACID OXIDASE).
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta;
OC   Magnoliophyta; eudicotyledons; Caryophyllidae; Caryophyllales;
OC   Chenopodiaceae; Spinacia.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 88058933.
RA   Volokita M., Somerville C.R.;
RT   "The primary structure of spinach glycolate oxidase deduced from the
RT   DNA sequence of a cDNA clone.";
RL   J. Biol. Chem. 262:15825-15828(1987).
RN   [2]
RP   SEQUENCE.
RX   MEDLINE; 88225066.
RA   Cederlund E., Lindqvist Y., Soederlund G., Braenden C.-I.,
RA   Joernvall H.;
RT   "Primary structure of glycolate oxidase from spinach.";
RL   Eur. J. Biochem. 173:523-530(1988).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   MEDLINE; 90040713.
RA   Lindqvist Y.;
RT   "Refined structure of spinach glycolate oxidase at 2-A resolution.";
RL   J. Mol. Biol. 209:151-166(1989).
RN   [4]
RP   ACTIVE SITE.
RX   MEDLINE; 89123500.
RA   Lindqvist Y., Braenden C.-I.;
RT   "The active site of spinach glycolate oxidase.";
RL   J. Biol. Chem. 264:3624-3628(1989).
CC   -!- CATALYTIC ACTIVITY: (S)-2-HYDROXY-ACID + O(2) = 2-OXO ACID +
CC       H(2)O(2).
CC   -!- COFACTOR: FMN.
CC   -!- PATHWAY: SECOND REACTION OF THE PHOTORESPIRATORY PATHWAY
CC       (GLYCOLATE PATHWAY).
CC   -!- SUBUNIT: HOMOTETRAMER OR HOMOOCTAMER.
CC   -!- SUBCELLULAR LOCATION: PEROXISOMAL.
CC   -!- SIMILARITY: BELONGS TO THE FMN-DEPENDENT ALPHA-HYDROXY ACID
CC       DEHYDROGENASES FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to [e-mail]).
CC   --------------------------------------------------------------------------
DR   EMBL; J03492; AAA34030.1; -.
DR   PIR; A28496; OXSPH.
DR   PIR; S00621; S00621.
DR   PDB; 1GOX; 15-OCT-89.
DR   PDB; 1AL7; 12-NOV-97.
DR   PDB; 1AL8; 17-SEP-97.
DR   PDB; 1GYL; 31-MAR-95.
DR   INTERPRO; IPR000262; -.
DR   PFAM; PF01070; FMN_dh; 1.
DR   PROSITE; PS00342; MICROBODIES_CTER; 1.
DR   PROSITE; PS00557; FMN_HYDROXY_ACID_DH; 1.
KW   Oxidoreductase; Flavoprotein; FMN; Peroxisome; Glycolate pathway;
KW   Photorespiration; 3D-structure; Acetylation.
FT   MOD_RES       1      1       ACETYLATION.
FT   SIMILAR     159    186       WITH CUCUMBER MALATE SYNTHETASE AND
FT                                SOYBEAN NODULIN 35.
FT   ACT_SITE     24     24       SUBSTRATE BINDING.
FT   ACT_SITE    129    129       SUBSTRATE BINDING.
FT   ACT_SITE    254    254       REMOVES THE SUBSTRATE ALPHA-PROTON AS THE
FT                                FIRST STEP IN CATALYSIS.
FT   ACT_SITE    257    257       SUBSTRATE BINDING.
FT   SITE        367    369       MICROBODY TARGETING SIGNAL (POTENTIAL).
FT   TURN          6      7
FT   HELIX         8     16
FT   HELIX        19     26
FT   TURN         30     31
FT   HELIX        33     44
FT   STRAND       45     47
FT   STRAND       59     59
FT   STRAND       62     64
FT   TURN         65     66
FT   STRAND       67     69
FT   STRAND       73     75
FT   HELIX        81     83
FT   TURN         84     84
FT   TURN         86     87
FT   HELIX        88     98
FT   TURN         99    100
FT   STRAND      103    105
FT   TURN        107    108
FT   HELIX       113    117
FT   TURN        118    119
FT   STRAND      124    128
FT   STRAND      131    131
FT   HELIX       134    146
FT   TURN        147    148
FT   STRAND      151    155
FT   HELIX       165    169
FT   TURN        170    171
FT   TURN        176    177
FT   HELIX       181    183
FT   HELIX       199    205
FT   TURN        206    206
FT   STRAND      207    207
FT   TURN        209    210
FT   HELIX       213    222
FT   STRAND      227    230
FT   HELIX       235    243
FT   TURN        244    245
FT   STRAND      248    251
FT   HELIX       254    256
FT   TURN        257    257
FT   TURN        260    261
FT   HELIX       265    275
FT   TURN        276    278
FT   STRAND      282    285
FT   HELIX       291    300
FT   TURN        301    301
FT   STRAND      304    307
FT   HELIX       309    341
FT   TURN        342    342
FT   STRAND      345    345
FT   TURN        346    348
FT   HELIX       351    353
FT   STRAND      354    356
FT   TURN        357    358
SQ   SEQUENCE   369 AA;  40285 MW;  892F1B3D0C1B48E0 CRC64;
     MEITNVNEYE AIAKQKLPKM VYDYYASGAE DQWTLAENRN AFSRILFRPR ILIDVTNIDM
     TTTILGFKIS MPIMIAPTAM QKMAHPEGEY ATARAASAAG TIMTLSSWAT SSVEEVASTG
     PGIRFFQLYV YKDRNVVAQL VRRAERAGFK AIALTVDTPR LGRREADIKN RFVLPPFLTL
     KNFEGIDLGK MDKANDSGLS SYVAGQIDRS LSWKDVAWLQ TITSLPILVK GVITAEDARL
     AVQHGAAGII VSNHGARQLD YVPATIMALE EVVKAAQGRI PVFLDGGVRR GTDVFKALAL
     GAAGVFIGRP VVFSLAAEGE AGVKKVLQMM RDEFELTMAL SGCRSLKEIS RSHIAADWDG
     PSSRAVARL
//
ID   ICLR_ECOLI     STANDARD;      PRT;   274 AA.
AC   P16528; P76782;
DT   01-AUG-1990 (Rel. 15, Created)
DT   01-AUG-1990 (Rel. 15, Last sequence update)
DT   01-NOV-1997 (Rel. 35, Last annotation update)
DE   ACETATE OPERON REPRESSOR.