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Database: UniProt
Entry: A3P7I1_BURP0
LinkDB: A3P7I1_BURP0
Original site: A3P7I1_BURP0 
ID   A3P7I1_BURP0            Unreviewed;       304 AA.
AC   A3P7I1;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 98.
DE   SubName: Full=Formate dehydrogenase, beta subunit {ECO:0000313|EMBL:ABN94980.1};
DE            EC=1.2.1.2 {ECO:0000313|EMBL:ABN94980.1};
GN   Name=fdoH {ECO:0000313|EMBL:ABN94980.1};
GN   OrderedLocusNames=BURPS1106A_A2258 {ECO:0000313|EMBL:ABN94980.1};
OS   Burkholderia pseudomallei (strain 1106a).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=357348 {ECO:0000313|EMBL:ABN94980.1, ECO:0000313|Proteomes:UP000006738};
RN   [1] {ECO:0000313|Proteomes:UP000006738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1106a {ECO:0000313|Proteomes:UP000006738};
RA   DeShazer D., Woods D.E., Nierman W.C.;
RL   Submitted (FEB-2007) 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; CP000573; ABN94980.1; -; Genomic_DNA.
DR   RefSeq; WP_004188093.1; NC_009078.1.
DR   AlphaFoldDB; A3P7I1; -.
DR   GeneID; 56598019; -.
DR   KEGG; bpl:BURPS1106A_A2258; -.
DR   HOGENOM; CLU_043374_0_3_4; -.
DR   OMA; KACQSAC; -.
DR   Proteomes; UP000006738; Chromosome II.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045333; P:cellular respiration; IEA:InterPro.
DR   GO; GO:0015944; P:formate oxidation; IEA:InterPro.
DR   CDD; cd10558; FDH-N; 1.
DR   Gene3D; 3.30.70.20; -; 2.
DR   Gene3D; 1.20.5.480; Single helix bin; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR006470; Formate_DH_bsu_Proteobacteria.
DR   InterPro; IPR038384; Formate_DH_C_sf.
DR   InterPro; IPR014603; Formate_DH_Fe-S_su.
DR   InterPro; IPR015246; Formate_DH_TM.
DR   NCBIfam; TIGR01582; FDH-beta; 1.
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   Pfam; PF12800; Fer4_4; 1.
DR   Pfam; PF09163; Form-deh_trans; 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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR036298-50};
KW   Oxidoreductase {ECO:0000313|EMBL:ABN94980.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          29..57
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          91..123
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          124..153
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         38
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         41
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         44
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         48
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         100
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         103
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         108
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         112
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         133
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         136
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         139
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         143
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         160
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         163
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         175
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         179
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
SQ   SEQUENCE   304 AA;  33026 MW;  9242EA9FCCC0E258 CRC64;
     MALQSLDIKR VSATTTPPPT AREPVTGSVA KLIDVSKCIG CKACQTACME WNDLRDEVGT
     NVGVYDNPAD LTEHSWTVMR FAEYENPAGD LEWLIRKDGC MHCEDPGCLK ACPSPGAIVQ
     YNNGIVDFHE EHCIGCGYCV TGCPFNIPRI SKQDNRAYKC TLCSDRVAVG QEPACVKTCP
     TGAIVFGTKE DMKQHAAERV ADLKGRGFEN AGLYDPQGVG GTHVMYVLHH ADKPSLYHGL
     PDNPSISPMV KLWKGLAKPL AVAGIALSAL VGFFHYTRVG PNDVTDDEEA AARDEARRIQ
     EDAK
//
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