MBHL_CITFR
ID MBHL_CITFR Reviewed; 597 AA.
AC Q46046;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 76.
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;
OS Citrobacter freundii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX NCBI_TaxID=546;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Yano K., Ikebukuro K., Tomiyama M., Karube I.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
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.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC family. {ECO:0000305}.
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DR EMBL; D28594; BAA05930.1; -; Genomic_DNA.
DR AlphaFoldDB; Q46046; -.
DR SMR; Q46046; -.
DR STRING; 1333848.CFNIH1_11595; -.
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.
FT CHAIN 1..597
FT /note="Hydrogenase-1 large chain"
FT /id="PRO_0000199711"
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; 66391 MW; F9CCABD815D017F4 CRC64;
MSNSYQTQGY TVNNAGRRLV VDPITRIEGH MRCEVNIDEQ NIITNAVSCG TMFRGLEIIL
QGRDPRDAWA FVERICGVCT GVHALASVYA IEDAIGIKVP DNANIIRNIM LATLWCHDHL
VHFYQLAGMD WIDVLNALKA DPRATSQLAQ SLSAWPMSSP GYFFDVQNRL KKFVDGGQLG
IFRNGYWGHP QYKLSPEANL MGFAHYLEAL DFQREIIKIH TVFGGKNPHP NWIVGGMPCA
INIDQSGAVG AVDMERLNLV QSIITRTADF INNVMVPDAL AIGQFNKPWS QIGTGLSDKC
VLSYGAFPDI ANDFSAKSLL MPGGAVINGD FNNVMPVDLA DQQQIQEFVD HAWYRYPDDQ
LGRHPFEGIT EPWYNPGDVK GSDTDIQQLN EQERYSWIKA PRWRGHAMEV GPLARTLIAY
HKGDAATIES VDRMMSALKL PLSGMQSTLG RILCRAHEAQ WAVSKLQYFF DKLMTNLKNG
NLATANTEKW EPASWPQQCR GIGFTEAPRG ALGHWASIRD QKIDVYQCVV PTTWNASPRD
PEGQIGAYEA ALMGTQMAIP DQPLEILRTL HSFDPCLACS THVLGDDGSE LIAVQVR