ID A0A0J1GTZ9_9GAMM Unreviewed; 381 AA.
AC A0A0J1GTZ9;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=hydrogenase (acceptor) {ECO:0000256|ARBA:ARBA00012082};
DE EC=1.12.99.6 {ECO:0000256|ARBA:ARBA00012082};
GN ORFNames=ABT56_20765 {ECO:0000313|EMBL:KLV03185.1};
OS Photobacterium aquae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=1195763 {ECO:0000313|EMBL:KLV03185.1, ECO:0000313|Proteomes:UP000036097};
RN [1] {ECO:0000313|EMBL:KLV03185.1, ECO:0000313|Proteomes:UP000036097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12159 {ECO:0000313|EMBL:KLV03185.1,
RC ECO:0000313|Proteomes:UP000036097};
RA Machado H., Gram L.;
RT "Photobacterium galathea sp. nov.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00000386};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000256|ARBA:ARBA00001927};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC {ECO:0000256|ARBA:ARBA00011771}.
CC -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase small subunit
CC family. {ECO:0000256|ARBA:ARBA00006605}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KLV03185.1}.
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DR EMBL; LDOT01000039; KLV03185.1; -; Genomic_DNA.
DR RefSeq; WP_047880834.1; NZ_LDOT01000039.1.
DR AlphaFoldDB; A0A0J1GTZ9; -.
DR STRING; 1195763.ABT56_20765; -.
DR PATRIC; fig|1195763.3.peg.4454; -.
DR OrthoDB; 9766729at2; -.
DR Proteomes; UP000036097; Unassembled WGS sequence.
DR GO; GO:0009375; C:ferredoxin hydrogenase complex; IEA:InterPro.
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; 4.10.480.10; Cytochrome-c3 hydrogenase, C-terminal domain; 1.
DR Gene3D; 3.40.50.700; NADH:ubiquinone oxidoreductase-like, 20kDa subunit; 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 NCBIfam; TIGR00391; hydA; 1.
DR PANTHER; PTHR30013:SF7; HYDROGENASE-2 SMALL CHAIN; 1.
DR PANTHER; PTHR30013; NIFE / NIFESE HYDROGENASE SMALL SUBUNIT FAMILY MEMBER; 1.
DR Pfam; PF14720; NiFe_hyd_SSU_C; 1.
DR Pfam; PF01058; Oxidored_q6; 1.
DR PIRSF; PIRSF000310; NiFe_hyd_ssu; 1.
DR PRINTS; PR00614; NIHGNASESMLL.
DR SUPFAM; SSF56770; HydA/Nqo6-like; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW 3Fe-4S {ECO:0000256|ARBA:ARBA00023291, ECO:0000256|PIRSR:PIRSR000310-1};
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRSR:PIRSR000310-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000310-1};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR000310-
KW 1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000310-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 84..230
FT /note="NADH:ubiquinone oxidoreductase-like 20kDa subunit"
FT /evidence="ECO:0000259|Pfam:PF01058"
FT DOMAIN 250..332
FT /note="Cytochrome-c3 hydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14720"
FT BINDING 84
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 87
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 184
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 217
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 255
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 258
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 283
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 289
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 298
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 317
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 320
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
SQ SEQUENCE 381 AA; 40849 MW; 77A55AA708AC983E CRC64;
MDTHAALYEL GKARLEQLRQ LPSNKQQPLQ ERLAENGISR REFLVWSATM TAALALPMPF
SSLVAEAAEL ADRVPLIWLH MAECTGCSES LIRSSTPDVS TLIFDHVSLE YQETLMAAAG
WQAEENLDAA MRNYKGQYLL AVEGAVPTAN GGAFLTLGCK GRTGLEMVQE AAAGAAAIIS
VGTCASFGGV QAAKPNPTGA KGVHAVVDRP VINLGGCPPS SSNIVGTLMY FIMFGKLPAL
DTFNRPKWAY GARVHDNCER RGHFDAGEFV EEFGDVSAEN GYCLYKMGCK GPYTYNNCPQ
VRFNNHTSWP VLAGHGCIGC SEPDFWDDMA DFEKPLGRQL LHGLDATADT IGAVTLGLTA
VGIGAHAVGS FFAGTYNDED N
//
