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MBHL_SHIFL
ID   MBHL_SHIFL              Reviewed;         597 AA.
AC   P0ACD9; P19927; P78056;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=SF0974, S1041;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: This is one of three E.coli hydrogenases synthesized in
CC       response to different physiological conditions. HYD1 is believed to
CC       have a role in hydrogen cycling during fermentative growth (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + H2 = AH2; Xref=Rhea:RHEA:12116, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:18276; EC=1.12.99.6;
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000250};
CC       Note=Binds 1 nickel ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Heterodimer of a large and a small subunit. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC       family. {ECO:0000305}.
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DR   EMBL; AE005674; AAN42602.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP16488.1; -; Genomic_DNA.
DR   RefSeq; NP_706895.1; NC_004337.2.
DR   RefSeq; WP_000107384.1; NZ_WPGW01000043.1.
DR   AlphaFoldDB; P0ACD9; -.
DR   SMR; P0ACD9; -.
DR   STRING; 198214.SF0974; -.
DR   EnsemblBacteria; AAN42602; AAN42602; SF0974.
DR   EnsemblBacteria; AAP16488; AAP16488; S1041.
DR   GeneID; 1023947; -.
DR   GeneID; 66670751; -.
DR   KEGG; sfl:SF0974; -.
DR   KEGG; sfx:S1041; -.
DR   PATRIC; fig|198214.7.peg.1133; -.
DR   HOGENOM; CLU_030087_0_0_6; -.
DR   OMA; EEVTHSW; -.
DR   OrthoDB; 1967820at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
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:UniProtKB-EC.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   GO; GO:0022904; P:respiratory electron transport chain; IEA:UniProt.
DR   Gene3D; 1.10.645.10; -; 1.
DR   InterPro; IPR001501; Ni-dep_hyd_lsu.
DR   InterPro; IPR018194; Ni-dep_hyd_lsu_Ni_BS.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   Pfam; PF00374; NiFeSe_Hases; 1.
DR   SUPFAM; SSF56762; SSF56762; 1.
DR   PROSITE; PS00507; NI_HGENASE_L_1; 1.
DR   PROSITE; PS00508; NI_HGENASE_L_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Metal-binding; Nickel; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..597
FT                   /note="Hydrogenase-1 large chain"
FT                   /id="PRO_0000199713"
FT   BINDING         76
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         79
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         576
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         579
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
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
 
 
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