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HYCG_ECOLI
ID   HYCG_ECOLI              Reviewed;         255 AA.
AC   P16433; Q2MAB0; Q46881;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 166.
DE   RecName: Full=Formate hydrogenlyase subunit 7;
DE            Short=FHL subunit 7;
DE   AltName: Full=Hydrogenase-3 component G;
GN   Name=hycG; Synonyms=hevG; OrderedLocusNames=b2719, JW2689;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=2187144; DOI=10.1111/j.1365-2958.1990.tb00590.x;
RA   Boehm R., Sauter M., Boeck A.;
RT   "Nucleotide sequence and expression of an operon in Escherichia coli coding
RT   for formate hydrogenlyase components.";
RL   Mol. Microbiol. 4:231-243(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
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., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC   -!- SUBUNIT: FHL comprises of a formate dehydrogenase, unidentified
CC       electron carriers and a hydrogenase (isoenzyme 3). In this non-energy
CC       conserving pathway molecular hydrogen and carbodioxide from formate are
CC       released.
CC   -!- INTERACTION:
CC       P16433; P07658: fdhF; NbExp=3; IntAct=EBI-541977, EBI-1121603;
CC       P16433; P45464: lpoA; NbExp=2; IntAct=EBI-541977, EBI-557795;
CC       P16433; P30750: metN; NbExp=6; IntAct=EBI-541977, EBI-541886;
CC       P16433; P0A9F1: mntR; NbExp=4; IntAct=EBI-541977, EBI-541895;
CC   -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; X17506; CAA35552.1; -; Genomic_DNA.
DR   EMBL; U29579; AAA69229.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75761.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76796.1; -; Genomic_DNA.
DR   PIR; S08625; S08625.
DR   RefSeq; NP_417199.1; NC_000913.3.
DR   RefSeq; WP_000067392.1; NZ_LN832404.1.
DR   AlphaFoldDB; P16433; -.
DR   SMR; P16433; -.
DR   BioGRID; 4262939; 20.
DR   BioGRID; 851523; 3.
DR   ComplexPortal; CPX-317; Formate hydrogenlyase-H/Hydrogenase-3 complex.
DR   DIP; DIP-9977N; -.
DR   IntAct; P16433; 10.
DR   MINT; P16433; -.
DR   STRING; 511145.b2719; -.
DR   TCDB; 3.D.1.9.2; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR   PaxDb; P16433; -.
DR   PRIDE; P16433; -.
DR   EnsemblBacteria; AAC75761; AAC75761; b2719.
DR   EnsemblBacteria; BAE76796; BAE76796; BAE76796.
DR   GeneID; 58389194; -.
DR   GeneID; 947191; -.
DR   KEGG; ecj:JW2689; -.
DR   KEGG; eco:b2719; -.
DR   PATRIC; fig|1411691.4.peg.4022; -.
DR   EchoBASE; EB0475; -.
DR   eggNOG; COG3260; Bacteria.
DR   HOGENOM; CLU_088839_0_0_6; -.
DR   InParanoid; P16433; -.
DR   OMA; AYGACGC; -.
DR   PhylomeDB; P16433; -.
DR   BioCyc; EcoCyc:HYCG-MON; -.
DR   BioCyc; MetaCyc:HYCG-MON; -.
DR   PRO; PR:P16433; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0009326; C:formate dehydrogenase complex; IPI:ComplexPortal.
DR   GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   GO; GO:0019645; P:anaerobic electron transport chain; IDA:ComplexPortal.
DR   GO; GO:0009061; P:anaerobic respiration; IDA:ComplexPortal.
DR   GO; GO:0015944; P:formate oxidation; IDA:ComplexPortal.
DR   GO; GO:0006007; P:glucose catabolic process; IDA:ComplexPortal.
DR   InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR   InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su.
DR   Pfam; PF01058; Oxidored_q6; 1.
DR   PROSITE; PS01150; COMPLEX1_20K; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..255
FT                   /note="Formate hydrogenlyase subunit 7"
FT                   /id="PRO_0000118780"
FT   BINDING         45
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         51
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         115
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         145
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        57
FT                   /note="A -> G (in Ref. 1; CAA35552)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   255 AA;  27999 MW;  B24FBAE3C44F3A10 CRC64;
     MSNLLGPRDA NGIPVPMTVD ESIASMKASL LKKIKRSAYV YRVDCGGCNG CEIEIFATLS
     PLFDAERFGI KVVPSPRHAD ILLFTGAVTR AMRSPALRAW QSAPDPKICI SYGACGNSGG
     IFHDLYCVWG GTDKIVPVDV YIPGCPPTPA ATLYGFAMAL GLLEQKIHAR GPGELDEQPA
     EILHGDMVQP LRVKVDREAR RLAGYRYGRQ IADDYLTQLG QGEEQVARWL EAENDPRLNE
     IVSHLNHVVE EARIR
 
 
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