seqwords.seq

emboss的linux版本的源代码

GN   ICLR.
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae;
OC   Escherichia.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 90236928.
RA   Sunnarborg A., Klumpp D.J., Chung T., Laporte D.C.;
RT   "Regulation of the glyoxylate bypass operon: cloning and
RT   characterization of iclR.";
RL   J. Bacteriol. 172:2642-2649(1990).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12;
RX   MEDLINE; 91138983.
RA   Negre D., Cortay J.-C., Old I.G., Galinier A., Richaud C.,
RA   Saint-Girons I., Cozzone A.J.;
RT   "Overproduction and characterization of the iclR gene product of
RT   Escherichia coli K-12 and comparison with that of Salmonella
RT   typhimurium LT2.";
RL   Gene 97:29-37(1991).
RN   [3]
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   [4]
RP   SEQUENCE OF 262-274 FROM N.A.
RX   MEDLINE; 91138981.
RA   Galinier A., Bleicher F., Negre D., Perriere G., Duclos B.,
RA   Cozzone A.J., Cortay J.-C.;
RT   "Primary structure of the intergenic region between aceK and iclR in
RT   the Escherichia coli chromosome.";
RL   Gene 97:149-150(1991).
CC   -!- FUNCTION: REGULATION OF THE GLYOXYLATE BYPASS OPERON (ACEBAK),
CC       WHICH ENCODES ISOCITRATE LYASE, MALATE SYNTHASE AS WELL AS
CC       ISOCITRATE DEHYDROGENASE KINASE/PHOSPHORYLASE.
CC   -!- SIMILARITY: BELONGS TO THE ICLR FAMILY OF TRANSCRIPTIONAL
CC       REGULATORS.
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; M31761; AAA24008.1; -.
DR   EMBL; M63914; AAA50561.1; ALT_INIT.
DR   EMBL; U00006; AAC43112.1; ALT_INIT.
DR   EMBL; AE000475; AAC76988.1; ALT_INIT.
DR   EMBL; M63497; AAA73003.1; -.
DR   PIR; A35267; RPECIR.
DR   PIR; JQ0871; JQ0871.
DR   ECOGENE; EG10491; ICLR.
DR   INTERPRO; IPR000285; -.
DR   PFAM; PF01614; IclR; 1.
DR   PROSITE; PS01051; HTH_ICLR_FAMILY; 1.
KW   Transcription regulation; Glyoxylate bypass; DNA-binding;
KW   Repressor.
FT   DNA_BIND     46     65       H-T-H MOTIF (POTENTIAL).
SQ   SEQUENCE   274 AA;  29739 MW;  7C8A7E9FD2841D0C CRC64;
     MVAPIPAKRG RKPAVATAPA TGQVQSLTRG LKLLEWIAES NGSVALTELA QQAGLPNSTT
     HRLLTTMQQQ GFVRQVGELG HWAIGAHAFM VGSSFLQSRN LLAIVHPILR NLMEESGETV
     NMAVLDQSDH EAIIIDQVQC THLMRMSAPI GGKLPMHASG AGKAFLAQLS EEQVTKLLHR
     KGLHAYTHAT LVSPVHLKED LAQTRKRGYS FDDEEHALGL RCLAACIFDE HREPFAAISI
     SGPISRITDD RVTEFGAMVI KAAKEVTLAY GGMR
//
ID   MDH_ECOLI      STANDARD;      PRT;   312 AA.
AC   P06994; Q59343; Q59344; Q59345; Q59346; Q59347; Q59348; Q60133;
AC   Q60150; O30401; O30402; O30403;
DT   01-APR-1988 (Rel. 07, Created)
DT   01-NOV-1995 (Rel. 32, Last sequence update)
DT   30-MAY-2000 (Rel. 39, Last annotation update)
DE   MALATE DEHYDROGENASE (EC 1.1.1.37).
GN   MDH.
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae;
OC   Escherichia.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 87259981.
RA   McAlister-Henn L., Blaber M., Bradshaw R.A., Nisco S.J.;
RT   "Complete nucleotide sequence of the Escherichia coli gene encoding
RT   malate dehydrogenase.";
RL   Nucleic Acids Res. 15:4993-4993(1987).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 88105815.
RA   Vogel R.F., Entian K.-D., Mecke D.;
RT   "Cloning and sequence of the mdh structural gene of Escherichia coli
RT   coding for malate dehydrogenase.";
RL   Arch. Microbiol. 149:36-42(1987).
RN   [3]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12 / MG1655;
RX   MEDLINE; 97426617.
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [4]
RP   SEQUENCE OF 1-40 FROM N.A.
RX   MEDLINE; 85288979.
RA   Sutherland P., McAlister-Henn L.;
RT   "Isolation and expression of the Escherichia coli gene encoding
RT   malate dehydrogenase.";
RL   J. Bacteriol. 163:1074-1079(1985).
RN   [5]
RP   SEQUENCE OF 1-36.
RX   MEDLINE; 82047078.
RA   Fernley R.T., Lentz S.R., Bradshaw R.A.;
RT   "Malate dehydrogenase: isolation from E. coli and comparison with the
RT   eukaryotic mitochondrial and cytoplasmic forms.";
RL   Biosci. Rep. 1:497-507(1981).
RN   [6]
RP   SEQUENCE OF 1-16.
RX   MEDLINE; 93281685.
RA   Henzel W.J., Billeci T.M., Stults J.T., Wong S.C., Grimley C.,
RA   Watanabe C.;
RT   "Identifying proteins from two-dimensional gels by molecular mass
RT   searching of peptide fragments in protein sequence databases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:5011-5015(1993).
RN   [7]
RP   SEQUENCE OF 1-26.
RC   STRAIN=K12 / EMG2;
RX   MEDLINE; 97443975.
RA   Link A.J., Robison K., Church G.M.;
RT   "Comparing the predicted and observed properties of proteins encoded
RT   in the genome of Escherichia coli K-12.";
RL   Electrophoresis 18:1259-1313(1997).
RN   [8]
RP   SEQUENCE OF 1-26.
RA   Charnock C.;
RL   Submitted (JAN-1996) to the SWISS-PROT data bank.
RN   [9]
RP   SEQUENCE OF 1-11.
RC   STRAIN=K12 / W3110;
RA   Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.;
RL   Submitted (FEB-1996) to the SWISS-PROT data bank.
RN   [10]
RP   SEQUENCE OF 1-13.
RX   MEDLINE; 96283620.
RA   Nystroem T., Larsson C., Gustafsson L.;
RT   "Bacterial defense against aging: role of the Escherichia coli ArcA
RT   regulator in gene expression, readjusted energy flux and survival
RT   during stasis.";
RL   EMBO J. 15:3219-3228(1996).
RN   [11]
RP   SEQUENCE OF 12-299 FROM N.A.
RC   STRAIN=VARIOUS STRAINS;
RX   MEDLINE; 94151313.
RA   Boyd E.F., Nelson K., Wang F.S., Whittam T.S., Selander R.K.;
RT   "Molecular genetic basis of allelic polymorphism in malate
RT   dehydrogenase (mdh) in natural populations of Escherichia coli and
RT   Salmonella enterica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:1280-1284(1994).
RN   [12]
RP   SEQUENCE OF 12-299 FROM N.A.
RC   STRAIN=VARIOUS STRAINS;
RX   MEDLINE; 97342740.
RA   Pupo G.M., Karaolis D.K., Lan R., Reeves P.R.;
RT   "Evolutionary relationships among pathogenic and nonpathogenic
RT   Escherichia coli strains inferred from multilocus enzyme
RT   electrophoresis and mdh sequence studies.";
RL   Infect. Immun. 65:2685-2692(1997).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS).
RX   MEDLINE; 92373767.
RA   Hall M.D., Levitt D.G., Banaszak L.J.;
RT   "Crystal structure of Escherichia coli malate dehydrogenase. A
RT   complex of the apoenzyme and citrate at 1.87-A resolution.";
RL   J. Mol. Biol. 226:867-882(1992).
CC   -!- CATALYTIC ACTIVITY: L-MALATE + NAD(+) = OXALOACETATE + NADH.
CC   -!- SUBUNIT: HOMODIMER.
CC   -!- SIMILARITY: BELONGS TO THE LDH FAMILY. MDH SUBFAMILY.
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; M10417; AAA24147.1; -.
DR   EMBL; M24777; AAA16107.1; -.
DR   EMBL; U18997; AAA58038.1; -.
DR   EMBL; AE000403; AAC76268.1; -.
DR   EMBL; Y00129; CAA68326.1; -.
DR   EMBL; U04742; AAC43730.1; -.
DR   EMBL; U04743; AAC43731.1; -.
DR   EMBL; U04744; AAC43732.1; -.
DR   EMBL; U04745; AAC43733.1; -.
DR   EMBL; U04746; AAC43734.1; -.
DR   EMBL; U04747; AAC43735.1; -.
DR   EMBL; U04748; AAC43736.1; -.
DR   EMBL; U04749; AAC43737.1; -.
DR   EMBL; U04750; AAC43738.1; -.
DR   EMBL; U04751; AAC43739.1; -.
DR   EMBL; U04752; AAC43740.1; -.
DR   EMBL; U04753; AAC43741.1; -.
DR   EMBL; U04754; AAC43742.1; -.
DR   EMBL; U04755; AAC43743.1; -.
DR   EMBL; U04756; AAC43744.1; -.
DR   EMBL; U04757; AAC43745.1; -.
DR   EMBL; U04758; AAC43746.1; -.
DR   EMBL; U04759; AAC43747.1; -.
DR   EMBL; U04760; AAC43748.1; -.
DR   EMBL; U04770; AAC43758.1; -.
DR   EMBL; AF004170; AAB87003.1; -.
DR   EMBL; AF004171; AAB87004.1; -.
DR   EMBL; AF004172; AAB87005.1; -.
DR   EMBL; AF004173; AAB87006.1; -.
DR   EMBL; AF004174; AAB87007.1; -.
DR   EMBL; AF004175; AAB87008.1; -.
DR   EMBL; AF004176; AAB87009.1; -.
DR   EMBL; AF004177; AAB87010.1; -.
DR   EMBL; AF004179; AAB87012.1; -.
DR   EMBL; AF004180; AAB87013.1; -.
DR   EMBL; AF004182; AAB87015.1; -.
DR   EMBL; AF004183; AAB87016.1; -.
DR   EMBL; AF004184; AAB87017.1; -.
DR   EMBL; AF004186; AAB87019.1; -.
DR   EMBL; AF004187; AAB87020.1; -.
DR   EMBL; AF004188; AAB87021.1; -.
DR   EMBL; AF004190; AAB87023.1; -.
DR   EMBL; AF004191; AAB87024.1; -.
DR   EMBL; AF004195; AAB87028.1; -.
DR   EMBL; AF004196; AAB87029.1; -.
DR   EMBL; AF004199; AAB87032.1; -.
DR   EMBL; AF004200; AAB87033.1; -.
DR   EMBL; AF004201; AAB87034.1; -.
DR   EMBL; AF004202; AAB87035.1; -.
DR   EMBL; AF004203; AAB87036.1; -.
DR   EMBL; AF004204; AAB87037.1; -.
DR   EMBL; AF004205; AAB87038.1; -.
DR   EMBL; AF004206; AAB87039.1; -.
DR   EMBL; AF004207; AAB87040.1; -.
DR   EMBL; AF004208; AAB87041.1; -.
DR   EMBL; AF004209; AAB87042.1; -.
DR   PIR; A26525; DEECM.
DR   PDB; 2CMD; 31-OCT-93.
DR   PDB; 1CME; 31-JAN-94.
DR   PDB; 1EMD; 31-OCT-93.
DR   SWISS-2DPAGE; P06994; COLI.
DR   ECO2DBASE; F030.2; 6TH EDITION.
DR   ECOGENE; EG10576; MDH.
DR   INTERPRO; IPR001236; -.
DR   INTERPRO; IPR001252; -.
DR   PFAM; PF00056; ldh; 1.
DR   PROSITE; PS00068; MDH; 1.
KW   Oxidoreductase; Tricarboxylic acid cycle; NAD; 3D-structure.
FT   ACT_SITE    150    150       PROTON-RELAY.
FT   BINDING     153    153       SUBSTRATE CARBOXYL GROUP.
FT   ACT_SITE    177    177       PROTON-RELAY.
FT   VARIANT      71     71       D -> N (IN STRAINS EC47, EC49 AND EC50).
FT   VARIANT     106    106       A -> S (IN STRAIN ECOR27).
FT   VARIANT     218    218       A -> R (IN STRAINS A8190, E2666-74,
FT                                E830587, E851819, E3406, EC10, EC14,
FT                                EC32, EC35, EC38, EC40, EC44, EC46, EC47,
FT                                EC49, EC50, EC52, EC58, E64 AND EC70).
FT   VARIANT     232    232       A -> T (IN STRAIN ECOR37).
FT   VARIANT     289    289       Q -> K (IN STRAINS EC35, EC38, EC40,
FT                                EC44, EC46 AND EC47).
FT   VARIANT     290    290       N -> S (IN STRAINS E2666-74, ECOR27 AND
FT                                ECOR45).
FT   VARIANT     291    291       A -> S (IN STRAIN EC35).
FT   VARIANT     294    294       G -> A (IN STRAIN ECOR45).
FT   VARIANT     297    297       D -> N (IN STRAIN E830587).
FT   CONFLICT     37     37       P -> S (IN REF. 4).
FT   CONFLICT     70     70       A -> R (IN REF. 2).
FT   CONFLICT     80     80       A -> R (IN REF. 1 AND 2).
FT   CONFLICT    116    116       I -> N (IN REF. 2).
FT   CONFLICT    144    144       F -> L (IN REF. 1).
FT   CONFLICT    305    312       LGEEFVNK -> WAKSSLISN (IN REF. 2).
FT   CONFLICT    307    307       E -> Q (IN REF. 1).
FT   STRAND        2      6
FT   TURN          7      9
FT   HELIX        11     23
FT   TURN         26     27
FT   STRAND       28     33
FT   TURN         37     38
FT   HELIX        39     47
FT   TURN         48     48
FT   STRAND       53     58
FT   HELIX        64     67
FT   TURN         68     69
FT   STRAND       72     75
FT   TURN         83     84
FT   HELIX        87    108
FT   TURN        110    111
FT   STRAND      113    116
FT   HELIX       121    134
FT   TURN        135    136
FT   TURN        140    141
FT   STRAND      143    145
FT   HELIX       148    162
FT   TURN        163    163
FT   HELIX       166    168
FT   STRAND      173    175
FT   TURN        179    181
FT   STRAND      182    184
FT   HELIX       186    188
FT   TURN        190    191
FT   HELIX       196    217
FT   TURN        218    219
FT   HELIX       225    242
FT   TURN        243    244
FT   STRAND      248    255
FT   STRAND      263    271
FT   TURN        272    273
FT   STRAND      274    278
FT   HELIX       286    311
SQ   SEQUENCE   312 AA;  32337 MW;  17741A3B5AD068BA CRC64;
     MKVAVLGAAG GIGQALALLL KTQLPSGSEL SLYDIAPVTP GVAVDLSHIP TAVKIKGFSG
     EDATPALEGA DVVLISAGVA RKPGMDRSDL FNVNAGIVKN LVQQVAKTCP KACIGIITNP
     VNTTVAIAAE VLKKAGVYDK NKLFGVTTLD IIRSNTFVAE LKGKQPGEVE VPVIGGHSGV
     TILPLLSQVP GVSFTEQEVA DLTKRIQNAG TEVVEAKAGG GSATLSMGQA AARFGLSLVR
     ALQGEQGVVE CAYVEGDGQY ARFFSQPLLL GKNGVEERKS IGTLSAFEQN ALEGMLDTLK
     KDIALGEEFV NK
//