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 27-MAR-2024, entry version 109.
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; Pseudomonadota; 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 PaxDb; 198214-SF0974; -.
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 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 Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1.
DR InterPro; IPR001501; Ni-dep_hyd_lsu.
DR InterPro; IPR018194; Ni-dep_hyd_lsu_Ni_BS.
DR InterPro; IPR029014; NiFe-Hase_large.
DR PANTHER; PTHR42958:SF3; HYDROGENASE-1 LARGE CHAIN; 1.
DR PANTHER; PTHR42958; HYDROGENASE-2 LARGE CHAIN; 1.
DR Pfam; PF00374; NiFeSe_Hases; 1.
DR SUPFAM; SSF56762; HydB/Nqo4-like; 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
//
