MBHS_RHILV
ID MBHS_RHILV Reviewed; 360 AA.
AC P18637;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 116.
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 Rhizobium leguminosarum bv. viciae.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=387;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B10;
RX PubMed=2402452; DOI=10.1093/nar/18.17.5285;
RA Schneider C.G., Schmitt H.J., Schild C., Tichy H.V., Lotz W.;
RT "DNA sequence encoding the two structural genes for the uptake hydrogenase
RT of Rhizobium leguminosarum bv. viciae B10.";
RL Nucleic Acids Res. 18:5285-5285(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=128c53;
RX PubMed=2103457; DOI=10.1007/bf00036924;
RA Hidalgo E., Leyva A., Ruiz-Argueso T.;
RT "Nucleotide sequence of the hydrogenase structural genes from Rhizobium
RT leguminosarum.";
RL Plant Mol. Biol. 15:367-370(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=[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 -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase small subunit
CC family. {ECO:0000305}.
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DR EMBL; Z36981; CAA85430.1; -; Genomic_DNA.
DR EMBL; X52974; CAA37148.1; -; Genomic_DNA.
DR PIR; S11968; S11968.
DR RefSeq; WP_018517045.1; NZ_WIEJ01000010.1.
DR AlphaFoldDB; P18637; -.
DR SMR; P18637; -.
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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 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..46
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 47..360
FT /note="Uptake hydrogenase small subunit"
FT /id="PRO_0000013434"
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"
FT CONFLICT 160
FT /note="C -> S (in Ref. 1; CAA85430)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="R -> P (in Ref. 1; CAA85430)"
FT /evidence="ECO:0000305"
FT CONFLICT 228..230
FT /note="SQR -> AQP (in Ref. 1; CAA85430)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 39149 MW; 85304E046F3DAAAF CRC64;
MATAETFYDV IRRQGITRRS FTKFCSLTAA SLGFGPGAAT AMAEALETKE RVPVIWMHGL
ECTCCSESFI RSAHPLVKDV VLSMISLDYD DTIMAAAGHQ AESILAETKE KYKGKYILAV
EGNPPLNEGG MFCIDGGKPF VEKLKWMAED AMAIIAWGAC ASWGCVQAAK PNPTQATPID
KVILDKPIIK VPGCPPIAEV MTGVVTFITT FGKLPELDRQ GRPKMFYSQR IHDKCYRRPH
FDAGQFVEEW DDEGARKGYC LYKMGCKGPT TYNACSTVRW NGGVSFPIQS GHGCIGCSED
GFWDNGSFYD RLTNIHQFGI EANADKVGMT AAGVVGGAIA AHAAVTAVKR LTTKREKADA
