ID   MBHL_ECOLI              Reviewed;         597 AA.
AC   P0ACD8; P19927; P78056;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   16-JUN-2009, entry version 32.
DE   RecName: Full=Hydrogenase-1 large chain;
DE            Short=HYD1;
DE            EC=1.12.99.6;
DE   AltName: Full=Membrane-bound hydrogenase 1 large subunit;
DE   AltName: Full=NiFe hydrogenase;
GN   Name=hyaB; OrderedLocusNames=b0973, JW0955;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
RX   MEDLINE=90202716; PubMed=2180913;
RA   Menon N.K., Robbins J., Peck H.D. Jr., Chatelus C.Y., Choi E.-S.,
RA   Przybyla A.E.;
RT   "Cloning and sequencing of a putative Escherichia coli [NiFe]
RT   hydrogenase-1 operon containing six open reading frames.";
RL   J. Bacteriol. 172:1969-1977(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; 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.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(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
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 276-597.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   MEDLINE=97061202; PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
RA   Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA   Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA   Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA   Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA   Yano M., Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
CC   -!- FUNCTION: This is one of three E.coli hydrogenases synthesized in
CC       response to different physiological conditions. HYD1 is believed
CC       to have a role in hydrogen cycling during fermentative growth.
CC   -!- CATALYTIC ACTIVITY: H(2) + A = AH(2).
CC   -!- COFACTOR: Binds 1 nickel ion per subunit (By similarity).
CC   -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC   -!- INTERACTION:
CC       P28912:yhhI; NbExp=1; IntAct=EBI-851493, EBI-1115282;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large
CC       subunit family.
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DR   EMBL; M34825; AAA23998.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74058.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35738.2; -; Genomic_DNA.
DR   PIR; C64838; HQECL.
DR   RefSeq; AP_001602.1; -.
DR   RefSeq; NP_415492.1; -.
DR   HSSP; P18188; 1FRF.
DR   IntAct; P0ACD8; 7.
DR   GeneID; 945580; -.
DR   GenomeReviews; AP009048_GR; JW0955.
DR   GenomeReviews; U00096_GR; b0973.
DR   KEGG; ecj:JW0955; -.
DR   KEGG; eco:b0973; -.
DR   EchoBASE; EB0464; -.
DR   EcoGene; EG10469; hyaB.
DR   HOGENOM; P0ACD8; -.
DR   OMA; P0ACD8; CLACATH.
DR   BioCyc; EcoCyc:HYAB-MON; -.
DR   BioCyc; MetaCyc:HYAB-MON; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR   GO; GO:0033748; F:hydrogenase (acceptor) activity; IEA:EC.
DR   GO; GO:0016151; F:nickel ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001501; Ni-dep_hyd_lsu.
DR   InterPro; IPR018194; Ni-dep_hyd_lsu_Ni_BS.
DR   Pfam; PF00374; NiFeSe_Hases; 1.
DR   PROSITE; PS00507; NI_HGENASE_L_1; 1.
DR   PROSITE; PS00508; NI_HGENASE_L_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Complete proteome; Direct protein sequencing; Membrane;
KW   Metal-binding; Nickel; Oxidoreductase.
FT   CHAIN         1    597       Hydrogenase-1 large chain.
FT                                /FTId=PRO_0000199712.
FT   METAL        76     76       Nickel (Potential).
FT   METAL        79     79       Nickel (Potential).
FT   METAL       576    576       Nickel (Potential).
FT   METAL       579    579       Nickel (Potential).
FT   CONFLICT     52     52       M -> I (in Ref. 1; AAA23998).
FT   CONFLICT     69     69       W -> R (in Ref. 1; AAA23998).
SQ   SEQUENCE   597 AA;  66253 MW;  659DD7EDE16D6342 CRC64;
     MSTQYETQGY TINNAGRRLV VDPITRIEGH MRCEVNINDQ NVITNAVSCG TMFRGLEIIL
     QGRDPRDAWA FVERICGVCT GVHALASVYA IEDAIGIKVP DNANIIRNIM LATLWCHDHL
     VHFYQLAGMD WIDVLDALKA DPRKTSELAQ SLSSWPKSSP GYFFDVQNRL KKFVEGGQLG
     IFRNGYWGHP QYKLPPEANL MGFAHYLEAL DFQREIVKIH AVFGGKNPHP NWIVGGMPCA
     INIDESGAVG AVNMERLNLV QSIITRTADF INNVMIPDAL AIGQFNKPWS EIGTGLSDKC
     VLSYGAFPDI ANDFGEKSLL MPGGAVINGD FNNVLPVDLV DPQQVQEFVD HAWYRYPNDQ
     VGRHPFDGIT DPWYNPGDVK GSDTNIQQLN EQERYSWIKA PRWRGNAMEV GPLARTLIAY
     HKGDAATVES VDRMMSALNL PLSGIQSTLG RILCRAHEAQ WAAGKLQYFF DKLMTNLKNG
     NLATASTEKW EPATWPTECR GVGFTEAPRG ALGHWAAIRD GKIDLYQCVV PTTWNASPRD
     PKGQIGAYEA ALMNTKMAIP EQPLEILRTL HSFDPCLACS THVLGDDGSE LISVQVR
//