MBHL_RHOCA
ID MBHL_RHOCA Reviewed; 597 AA.
AC P15284;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, 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 Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33303 / B10;
RX PubMed=3067084; DOI=10.1007/bf00340186;
RA Leclerc M., Colbeau A., Cauvin B., Vignais P.M.;
RT "Cloning and sequencing of the genes encoding the large and the small
RT subunits of the H2 uptake hydrogenase (hup) of Rhodobacter capsulatus.";
RL Mol. Gen. Genet. 214:97-107(1988).
RN [2]
RP ERRATUM OF PUBMED:3067084, AND SEQUENCE REVISION.
RA Leclerc M., Colbeau A., Cauvin B., Vignais P.M.;
RL Mol. Gen. Genet. 215:368-368(1989).
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; X13520; CAA31870.1; -; Genomic_DNA.
DR PIR; S08317; S08317.
DR AlphaFoldDB; P15284; -.
DR SMR; P15284; -.
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..597
FT /note="Uptake hydrogenase large subunit"
FT /id="PRO_0000199716"
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 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; 66046 MW; C038E25E05EFB9C8 CRC64;
MTTQTPNGFT LDNAGKRIVV DPVTRIEGHM RCEVNVNDQG IITNAVSTGT MWRGLEVILK
GRDPRDAWAF TERICGVCTG THALTSVRAV ESALGITIPD NANSIRNMMQ LNLQIHDHIV
HFYHLHALDW VNPVNALRAD PKATSELQQM VSPSHPLSSP GYFRDVQNRL KKFVESGQLG
LFKNGYWDNP AYKLPPEADL MATTHYLEAL DLQKEVVKVH TIFGGKNPHP NWLVGGVPCP
INVDGVGAVG AINMERLNLV SSIIDRCTEF TRNVYLPDLK AIGGFYKEWL YGGGLSGQSV
LSYGDIPENP NDFSAGQLHL PRGAIINGNL NEVHDVDTTD PEQVQEFVDH SWYDYGEPGM
GLHPWDGRTE PKFELGPNLK GTRTNIENID EGAKYSWIKA PRWRGNAMEV GPLAATSSVT
RKGHEDIKNQ VEGLLRDMNL PVSALFSTLG RTAARALEAE YCCRLQKHFF DKLVTNIKNG
DSSTANVEKW DPSTWPKEAK GVGMTEAPRG ALGHWVKIKD GRIENYQCVV PTTWNGSPRD
SKGNIGAFEA SLLNTKMERP EEPVEILRTL HSFDPCLACS THVMSAEGAP LTTVKVR