MBHL_RUBGE
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 03-AUG-2022, entry version 85.
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; Proteobacteria; Betaproteobacteria; Burkholderiales; 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=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; X52522; CAA36755.1; -; Genomic_DNA.
DR PIR; S09251; S09251.
DR AlphaFoldDB; P17632; -.
DR SMR; P17632; -.
DR PRIDE; P17632; -.
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..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
