ID   MBHL_RUBGE              Reviewed;         618 AA.
AC   P17632;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   04-NOV-2026, entry version 94.
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   Rubrivivax gelatinosus (Rhodocyclus gelatinosus) (Rhodopseudomonas
OS   gelatinosa).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Sphaerotilaceae; Rubrivivax.
OX   NCBI_TaxID=28068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2325631; DOI=10.1007/bf00280367;
RA   Uffen R.L., Colbeau A., Richaud P., Vignais P.M.;
RT   "Cloning and sequencing the genes encoding uptake-hydrogenase subunits of
RT   Rhodocyclus gelatinosus.";
RL   Mol. Gen. Genet. 221:49-58(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=H2 + A = 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X52522; CAA36755.1; -; Genomic_DNA.
DR   PIR; S09251; S09251.
DR   AlphaFoldDB; P17632; -.
DR   SMR; P17632; -.
DR   OMA; AAEFMFD; -.
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   FunFam; 1.10.645.10:FF:000002; Hydrogenase 2 large subunit; 1.
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   InterPro; IPR050867; NiFe/NiFeSe_hydrgnase_LSU.
DR   PANTHER; PTHR42958; HYDROGENASE-2 LARGE CHAIN; 1.
DR   PANTHER; PTHR42958:SF2; UPTAKE HYDROGENASE LARGE SUBUNIT; 1.
DR   Pfam; PF27537; HoxH; 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.
FT   CHAIN           1..618
FT                   /note="Uptake hydrogenase large subunit"
FT                   /id="PRO_0000199717"
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         597
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         600
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   618 AA;  68527 MW;  87B02F0338AE7BD3 CRC64;
     MGAIETQGFK LDDSGRRIVV DPVTRIEGHM RCEVNVDANN VIRNAVSTGT MWRGLEVILK
     GRDPRDAWAF VERICGVCTG CHALTSVRAV EDALGIRIPK NAHLIREMMA KTLQVHDHAV
     HFYHLHALDW VDVVSALKAD PKKTSELQHL VSPSHPLSSP GYFPRRGRTG LKKFVESGQL
     GPFMNGYWGS KAYVLPPEAN LMAVTHYLEA LDLQKEWVKV HAIFGGKNPH PNYLVGGVPC
     AINLDGNGAA GRINMERLNF VKARIDEMIE FNKNVYLPDV LAIGTIYKQA GWLHGGGLSA
     LNVADYGTYD KVAYDHATHQ LPGGVILDGN WDEIHAIDPR DPEQVQEFVA HSWYQYADES
     KGLHPWDGVT EPKFELGART KGTRTAIEHI DESAKYSWIK SPRWRGHAVE VGPLSRYILG
     YAHALKGNKY CQRVKEQVDF AAEAINHAIP KALGLPETQY TLKQLLPTTI GRTLARCLEG
     QYCGEMMLAD YHELVANIRA GDTATANVEK WDPATWPKEA KGVGTVAAPR GMLGHWIRIK
     DGKIENYQCV VPTTWNGSPR DAKGQIGAFE ASLLGTPMVN PEQPVEILRT LHSFDPCLAC
     STHVMSEDGR ELTTVKVR
//