ID   MBHL_BRADU              Reviewed;         596 AA.
AC   P12636;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 123.
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; OrderedLocusNames=bll6941;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3054886; DOI=10.1073/pnas.85.22.8395;
RA   Sayavedra-Soto L.A., Powell G.K., Evans H.J., Morris R.O.;
RT   "Nucleotide sequence of the genetic loci encoding subunits of
RT   Bradyrhizobium japonicum uptake hydrogenase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:8395-8399(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 589-596.
RX   PubMed=8163174; DOI=10.1016/0378-1119(94)90126-0;
RA   Fu C., Maier R.J.;
RT   "Sequence and characterization of three genes within the hydrogenase gene
RT   cluster of Bradyrhizobium japonicum.";
RL   Gene 141:47-52(1994).
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; J04114; AAA26219.1; -; Genomic_DNA.
DR   EMBL; BA000040; BAC52206.1; -; Genomic_DNA.
DR   EMBL; L24446; AAD13471.1; -; Genomic_DNA.
DR   PIR; B31341; HQZJUL.
DR   RefSeq; NP_773581.1; NC_004463.1.
DR   RefSeq; WP_011089679.1; NZ_CP011360.1.
DR   AlphaFoldDB; P12636; -.
DR   SMR; P12636; -.
DR   STRING; 224911.27355222; -.
DR   EnsemblBacteria; BAC52206; BAC52206; BAC52206.
DR   GeneID; 64026697; -.
DR   KEGG; bja:bll6941; -.
DR   PATRIC; fig|224911.44.peg.6975; -.
DR   eggNOG; COG0374; Bacteria.
DR   HOGENOM; CLU_030087_0_0_5; -.
DR   InParanoid; P12636; -.
DR   OMA; EEVTHSW; -.
DR   PhylomeDB; P12636; -.
DR   Proteomes; UP000002526; 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; -; 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..596
FT                   /note="Uptake hydrogenase large subunit"
FT                   /id="PRO_0000199710"
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"
SQ   SEQUENCE   596 AA;  65923 MW;  0409EE8972F036B7 CRC64;
     MGIQTPNGFN LDNSGKRIVV DPVTRIEGHM RVEVNVDADN VIRNAVSTGT MWRGIEVILK
     NRDPRDAWAF TERICGVCTG THALTSVRAV ENALGITIPE NANSIRNLMQ LALQVHDHVV
     HFYHLHALDW VDVVSALSAD PRATSTLAQS ISNWPLSSPG YFKDLQTRLK KFVESGQLGP
     FKNGYWGSKA YKLPPEANLM AVAHYLEALD FQKEIVKIHT IFGGKNPHPN WLVGGVPCPI
     NVDGTGAVGA INMERLNLIS SIIDRLIEFN EMVYLPDVAA IGSFYKDWLY GGGLSGQSVL
     AYGDVPEHAN DYSAKSLKLP RGAIINGNLS EVFPVDHANP DEIQEFVVHS WYKYPDETKG
     LHPWDGVTEP NYVLGPNAKG TKTAIEQLDE GGKYSWIKAP RWKGHAMEVG PLARWVVGYA
     QNKSEFKDPV DKFLRDLNLP TSALFSTLGR TAARALESVW AGRQMRYFQD KLVANIKAGD
     SSTANVDKWK PESWPKEAKG VGFTEAPRGA LAHWIKIKDT KIDNYQCVVP TTWNGSPRDP
     KGNIGAFEAS LMNTPMVNPE QPLEILRTIH SFDPCLACST HVMSPDGQEL AKVKVR