ID A0A1J5CHF9_9BURK Unreviewed; 358 AA.
AC A0A1J5CHF9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 22.
DE RecName: Full=hydrogenase (acceptor) {ECO:0000256|ARBA:ARBA00012082};
DE EC=1.12.99.6 {ECO:0000256|ARBA:ARBA00012082};
GN ORFNames=AUK50_04290 {ECO:0000313|EMBL:OIP19602.1};
OS Comamonadaceae bacterium CG2_30_57_122.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1805089 {ECO:0000313|EMBL:OIP19602.1, ECO:0000313|Proteomes:UP000182154};
RN [1] {ECO:0000313|EMBL:OIP19602.1, ECO:0000313|Proteomes:UP000182154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_57_122 {ECO:0000313|EMBL:OIP19602.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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:OIP19602.1}.
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DR EMBL; MNXW01000096; OIP19602.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5CHF9; -.
DR Proteomes; UP000182154; 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: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 InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR00391; hydA; 1.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR30013:SF6; HYDROGENASE-1 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, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..42
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 43..358
FT /note="hydrogenase (acceptor)"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012475845"
FT DOMAIN 59..204
FT /note="NADH:ubiquinone oxidoreductase-like 20kDa subunit"
FT /evidence="ECO:0000259|Pfam:PF01058"
FT DOMAIN 224..305
FT /note="Cytochrome-c3 hydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14720"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 62
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 157
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 191
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 229
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 232
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 257
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 263
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 272
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 291
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 294
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
SQ SEQUENCE 358 AA; 39051 MW; EE77847E24B77397 CRC64;
METFYEVMRR QGISRRSLLK YCSLTATSLG LAPSFVPQMA HAMETKPRTP VLWLHGLECT
CCSESFIRSA HPLAKDVVLS MLSLDYDDTL MAAAGHQAEA ILEEIMTKYK GQYILAVEGN
PPLNEDGMFC IQSGKPFIEK LKRVAKDAKA VIAWGSCASW GCVQAAKPNP TQATPIHKVI
TDKPIIKVPG CPPIAEVMTG VITYMLTFDK IPELDRQGRP KMFYSQRIHD KCYRRPHFDA
GQFVEAFDDE SARKGYCLYK VGCKGPTTYN ACSTVMWNEG TSFPIKAGHG CIGCSEDGFW
DKGSFYDRLT TIHQFGVEGT ADKIGGTAAA VVGAAVVAHA AVSAISRAAA AKDKTTKA
//
