ID   MBHL_RHILV              Reviewed;         596 AA.
AC   P18636;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Uptake hydrogenase large subunit;
DE            EC=1.12.99.6;
DE   AltName: Full=Hydrogenlyase;
DE   AltName: Full=Membrane-bound hydrogenase large subunit;
GN   Name=hupB; Synonyms=hupL;
OS   Rhizobium leguminosarum bv. viciae.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=387;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B10;
RX   PubMed=2402452; DOI=10.1093/nar/18.17.5285;
RA   Schneider C.G., Schmitt H.J., Schild C., Tichy H.V., Lotz W.;
RT   "DNA sequence encoding the two structural genes for the uptake hydrogenase
RT   of Rhizobium leguminosarum bv. viciae B10.";
RL   Nucleic Acids Res. 18:5285-5285(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=128c53;
RX   PubMed=2103457; DOI=10.1007/bf00036924;
RA   Hidalgo E., Leyva A., Ruiz-Argueso T.;
RT   "Nucleotide sequence of the hydrogenase structural genes from Rhizobium
RT   leguminosarum.";
RL   Plant Mol. Biol. 15:367-370(1990).
CC   -!- FUNCTION: This enzyme recycles the H(2) produced by nitrogenase to
CC       increase the production of ATP and to protect nitrogenase against
CC       inhibition or damage by O(2) under carbon- or phosphate-limited
CC       conditions.
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; Z36981; CAA85431.1; -; Genomic_DNA.
DR   EMBL; X52974; CAA37149.1; -; Genomic_DNA.
DR   PIR; S11969; S11969.
DR   RefSeq; WP_018517046.1; NZ_WIEJ01000010.1.
DR   AlphaFoldDB; P18636; -.
DR   SMR; P18636; -.
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; -; 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..596
FT                   /note="Uptake hydrogenase large subunit"
FT                   /id="PRO_0000199715"
FT   BINDING         75
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         78
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         575
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         578
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        510
FT                   /note="R -> A (in Ref. 2; CAA37149)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   596 AA;  66193 MW;  474EA9B9FD2CBF68 CRC64;
     MTIQTPNGFT LDNSGKRIVV DPVTRIEGHM RVEVNVDENN IIRNAVSTGT MWRGIEVILK
     NRDPRDAWAF TERICGVCTG THALTSVRAV ENALGITIPD NANSIRNLMQ LALQVHDHVV
     HFYHLHALDW VDVVSALSAD PKATSALAQS ISDWPLSSPG YFKDIQTRLK KFVESGQLGP
     FKNGYWGNAS YKLPPEANLM AVAHYLEALD FQKEIVKIHT IFGGKNPHPN WLVGGVPCPI
     NVDGTGAVGA INMERLNMVT SIIDQLIEFN DKVYVPDIMA IGSFYKDWLY GGGLSGKNVL
     AYGDVPEHAN DYSEASLKLP RGAIINGNLA EVFPVDHADP EQIQEFVTHS WYKYPDESKG
     LHPWDGITEP HYELGPNAKG TKTNIEQLDE GAKYSWIKAP RWRGNAMEVG PLARWVIGYA
     QNKAEFKDPV DKVLKDLGLP VTALFSTLGR TAARALESQW AGYQMRYFQN KLIANIKAGD
     SNTAFVDKWK PETWPKEVKG VGFTEAPRGR LAHWIRIKDG KIDNYQCVVP TTWNGSPRDP
     TGNIGAFEAS LMDTPMSNPT QPLEILRTIH SFDPCLACST HVMSPDGQEM ARVQVR