MBHS_RHOCA
ID MBHS_RHOCA Reviewed; 358 AA.
AC P15283;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Uptake hydrogenase small subunit;
DE EC=1.12.99.6;
DE AltName: Full=Hydrogenlyase;
DE AltName: Full=Membrane-bound hydrogenase small subunit;
DE Flags: Precursor;
GN Name=hupA; Synonyms=hupS;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
RC STRAIN=ATCC 33303 / B10;
RX PubMed=8497190; DOI=10.1111/j.1365-2958.1993.tb01199.x;
RA Colbeau A., Richaud P., Toussaint B., Caballero F.J., Elster C.,
RA Delphin C., Smith R.L., Chabert J., Vignais P.M.;
RT "Organization of the genes necessary for hydrogenase expression in
RT Rhodobacter capsulatus. Sequence analysis and identification of two hyp
RT regulatory mutants.";
RL Mol. Microbiol. 8:15-29(1993).
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=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000250};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 2 [4Fe-4S] clusters. {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 small subunit
CC family. {ECO:0000305}.
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DR EMBL; X13520; CAA31869.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M37261; AAA69668.1; ALT_TERM; Genomic_DNA.
DR PIR; S08316; S08316.
DR AlphaFoldDB; P15283; -.
DR SMR; P15283; -.
DR GO; GO:0009375; C:ferredoxin hydrogenase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR GO; GO:0033748; F:hydrogenase (acceptor) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.700; -; 1.
DR Gene3D; 4.10.480.10; -; 1.
DR InterPro; IPR027394; Cytochrome-c3_hydrogenase_C.
DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR InterPro; IPR037148; NiFe-Hase_small_C_sf.
DR InterPro; IPR037024; NiFe_Hase_small_N_sf.
DR InterPro; IPR001821; NiFe_hydrogenase_ssu.
DR PANTHER; PTHR30013; PTHR30013; 1.
DR Pfam; PF14720; NiFe_hyd_SSU_C; 1.
DR Pfam; PF01058; Oxidored_q6; 1.
DR PIRSF; PIRSF000310; NiFe_hyd_ssu; 1.
DR TIGRFAMs; TIGR00391; hydA; 1.
PE 3: Inferred from homology;
KW 3Fe-4S; 4Fe-4S; Cell membrane; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Oxidoreductase; Signal.
FT SIGNAL 1..45
FT CHAIN 46..358
FT /note="Uptake hydrogenase small subunit"
FT /id="PRO_0000013435"
FT BINDING 62
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
SQ SEQUENCE 358 AA; 39403 MW; D08C1887F1376237 CRC64;
MSDIETFYDV MRRQGITRRS FMKSVRSPQH VLGLGPSFVP KIGEAMETKP RTPVVWVHGL
ECTCCSESFI RSAHPLAKDV VLSMISLDYD DTLMAAAGHA AEAAFEETIA KYKGNYILAV
EGNPPLNEDG MFCITGGKPF VEKLRHAAEG AKAIISWGAC ASYGCVQAAA PNPTQATPVH
KVITDKPIIK VPGCPPIAEV MTGVITYMLT FDRMPELDRQ GRPAMFYSQR IHDKCYRRPH
FDAGQFVEHW DDENARKGYC LYKMGCKGPT TYNACSTVPL ERRRHFPIQS GHGCIGCSED
GFWDQGSFYD RLTTIKQFGI EATADQIGWT ATGLVGAAVA AHAAVSVLKR AQKKNEEA
