ID A0A1H6XQ12_9FIRM Unreviewed; 276 AA.
AC A0A1H6XQ12;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Formate dehydrogenase iron-sulfur subunit {ECO:0000313|EMBL:SEJ30276.1};
GN ORFNames=SAMN05660742_105210 {ECO:0000313|EMBL:SEJ30276.1};
OS Propionispira arboris.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Propionispira.
OX NCBI_TaxID=84035 {ECO:0000313|EMBL:SEJ30276.1, ECO:0000313|Proteomes:UP000199662};
RN [1] {ECO:0000313|EMBL:SEJ30276.1, ECO:0000313|Proteomes:UP000199662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2179 {ECO:0000313|EMBL:SEJ30276.1,
RC ECO:0000313|Proteomes:UP000199662};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|PIRSR:PIRSR036298-50};
CC Note=Binds 4 [4Fe-4S] clusters per subunit.
CC {ECO:0000256|PIRSR:PIRSR036298-50};
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DR EMBL; FNZK01000005; SEJ30276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6XQ12; -.
DR STRING; 84035.SAMN05660742_105210; -.
DR Proteomes; UP000199662; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045333; P:cellular respiration; IEA:InterPro.
DR GO; GO:0015944; P:formate oxidation; IEA:InterPro.
DR CDD; cd10562; FDH_b_like; 1.
DR Gene3D; 3.30.70.20; -; 2.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR014603; Formate_DH_Fe-S_su.
DR PANTHER; PTHR43545; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, IRON-SULFUR SUBUNIT; 1.
DR PANTHER; PTHR43545:SF4; FORMATE DEHYDROGENASE-O IRON-SULFUR SUBUNIT; 1.
DR Pfam; PF13247; Fer4_11; 1.
DR PIRSF; PIRSF036298; FDH_4Fe4S; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRSR:PIRSR036298-50};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR036298-50};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR036298-
KW 50};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036298-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000199662};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 4..34
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 64..97
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 98..127
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 13
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT BINDING 16
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT BINDING 19
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT BINDING 23
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT BINDING 75
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT BINDING 78
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT BINDING 83
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT BINDING 87
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT BINDING 107
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT BINDING 110
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT BINDING 113
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT BINDING 117
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT BINDING 131
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT BINDING 134
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT BINDING 152
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT BINDING 156
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
SQ SEQUENCE 276 AA; 30675 MW; C14BB694150E5655 CRC64;
MSRLAYYYDS SKCMGCRGCQ AACKEWNEEE VENTHFEGSY QNPPQLSPDT RMIIKFYENF
EKDTVPQLNM LKYQCFHCGD PACVKVCPSG CLQRTEDGVV IMDKDKCIAC GYCHSACPFT
IPSIGKTVNK CDMCFSRIRE GSESEKTSTP ACVKACLADA LSFGNRDELV QKGKERVTWL
KTRGYENANL YGESILGGLG VLSVLKDKPT KYGLPEEPSM PLEITAWKDI LNPIAPLAFV
GAIGLSAVQH LCALKQIKDE KKKDDTDKDD ADKGEK
//
