MBHS_AZOCH
ID MBHS_AZOCH Reviewed; 354 AA.
AC P18190;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-NOV-2002, sequence version 3.
DT 03-AUG-2022, entry version 109.
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 Azotobacter chroococcum mcd 1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=355;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2215219; DOI=10.1111/j.1365-2958.1990.tb00672.x;
RA Ford C.M., Garg N., Garg R.P., Tibelius K.H., Yates M.G., Arp D.J.,
RA Seefeldt L.C.;
RT "The identification, characterization, sequencing and mutagenesis of the
RT genes (hupSL) encoding the small and large subunits of the H2-uptake
RT hydrogenase of Azotobacter chroococcum.";
RL Mol. Microbiol. 4:999-1008(1990).
RN [2]
RP SEQUENCE REVISION TO 184.
RA Yates M.G.;
RL Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: An expected iron-sulfur cluster ligand Cys residue was not
CC found at position 231 in this sequence. While a Ser residue may serve
CC as an iron-sulfur cluster ligand, it would be expected to seriously
CC alter the redox behavior of this protein. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA37133.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X52961; CAA37133.1; ALT_FRAME; Genomic_DNA.
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..44
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 45..354
FT /note="Uptake hydrogenase small subunit"
FT /id="PRO_0000013423"
FT BINDING 61
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
SQ SEQUENCE 354 AA; 39132 MW; FB7B2AC69B821533 CRC64;
MSQLETXYDV MRRQGITRRS FLKYCSLTGR PCLGPTFAPQ IAHAMETRPP TPVVWLHGLE
CTCCSESFIR SGDPLVKDVV LSMISLDYDD TLMPPRHQGT VEETMRKYKG EYILAVEGNP
PLNEDGMFCI VGGKPFLDQL KHAAKDAKAV IAWGSCASWG CVQAAKPNPT QAVPIHKVIT
DKPMIKVPGC PPIAEVMTGV ITYMLTFGKL PELDRQGRPK MFYGQRIHDK SYRRPHFDAG
QFVEHWDDEG ARKGYCLYKV GCKGPTSYNA CSTVRWNEGT SFPIQAGHGC IGCSEDGFWD
KGSFYERLTT IPQFGIEKNA DQIGPRGRRG SGAAIAAHAA VTAIKRLQNK GDQA
