ID A0A248VYJ7_9BURK Unreviewed; 331 AA.
AC A0A248VYJ7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=hydrogenase (acceptor) {ECO:0000256|ARBA:ARBA00012082};
DE EC=1.12.99.6 {ECO:0000256|ARBA:ARBA00012082};
GN ORFNames=CJU94_38550 {ECO:0000313|EMBL:ASW04109.1};
OS Paraburkholderia aromaticivorans.
OG Plasmid pbn2 {ECO:0000313|Proteomes:UP000215158}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=2026199 {ECO:0000313|EMBL:ASW04109.1, ECO:0000313|Proteomes:UP000215158};
RN [1] {ECO:0000313|Proteomes:UP000215158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BN5 {ECO:0000313|Proteomes:UP000215158};
RC PLASMID=pbn2 {ECO:0000313|Proteomes:UP000215158};
RA Lee Y.;
RT "Identification and genetic characteristics of simultaneous BTEX- and
RT naphthalene-degrading Paraburkholderia sp. BN5 isolated from petroleum-
RT contaminated soil.";
RL Submitted (AUG-2017) 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}.
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DR EMBL; CP022992; ASW04109.1; -; Genomic_DNA.
DR RefSeq; WP_035483938.1; NZ_CP022992.1.
DR AlphaFoldDB; A0A248VYJ7; -.
DR KEGG; parb:CJU94_38550; -.
DR OrthoDB; 9766729at2; -.
DR Proteomes; UP000215158; Plasmid pbn2.
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: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 PANTHER; PTHR30013:SF5; HYDROGENASE SMALL SUBUNIT; 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 SUPFAM; SSF56770; HydA/Nqo6-like; 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 Plasmid {ECO:0000313|EMBL:ASW04109.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 11..175
FT /note="NADH:ubiquinone oxidoreductase-like 20kDa subunit"
FT /evidence="ECO:0000259|Pfam:PF01058"
FT DOMAIN 198..273
FT /note="Cytochrome-c3 hydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14720"
FT BINDING 11
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 14
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 114
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 162
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 201
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 204
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 224
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 231
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 240
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 258
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 261
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
SQ SEQUENCE 331 AA; 34933 MW; 748754301E4E12F6 CRC64;
MNVLWLQSGG CGGCSMSLLC ADTVDFYGAL DGAGVSLLWH PSVSLESGTE LLQVLDRCVS
GEIPLDVLCI EGSMLRGPNG TGRFHLLAGT DVPMIDWVRR LAAVAHHTVA IGTCAAFGGV
TAGGSNPTDA CGLQYDGDEP GGLLGVEFRG RGGLPVINVA GCPTHPGWVI DTLMLLSAGL
LDRNGLDTLG RPRFYADYLV HHGCTRNEYY EFKASAEKPS DLGCMMENMG CKGTQAHADC
NTRLWNGAGS CTRGGYACIS CTEPGFEEPG HPFHETPKVA GIPIGLPTDM PKAWFVALAS
LSKSATPKRV KMNATSDHAV IAPAVRKSRL R
//
