ID A0A014MUY4_9BURK Unreviewed; 309 AA. AC A0A014MUY4; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 03-MAY-2023, entry version 39. DE SubName: Full=Formate dehydrogenase-N subunit beta {ECO:0000313|EMBL:EXU81854.1}; GN ORFNames=AX13_00960 {ECO:0000313|EMBL:EXU81854.1}; OS Comamonas aquatica DA1877. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Comamonas. OX NCBI_TaxID=1457173 {ECO:0000313|EMBL:EXU81854.1, ECO:0000313|Proteomes:UP000020766}; RN [1] {ECO:0000313|EMBL:EXU81854.1, ECO:0000313|Proteomes:UP000020766} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DA1877 {ECO:0000313|EMBL:EXU81854.1, RC ECO:0000313|Proteomes:UP000020766}; RA Watson E., Macneil L.T., Ritter A.D., Yilmaz L.S., Rosebrock A.P., RA Caudy A.A., Walhout A.J.; RT "Interspecies Systems Biology Uncovers Metabolites Affecting C. elegans RT Gene Expression and Life History Traits."; RL Submitted (JAN-2014) 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}; 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:EXU81854.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JBOK01000001; EXU81854.1; -; Genomic_DNA. DR RefSeq; WP_042412715.1; NZ_JBOK01000001.1. DR AlphaFoldDB; A0A014MUY4; -. DR STRING; 225991.MA05_09605; -. DR EnsemblBacteria; EXU81854; EXU81854; AX13_00960. DR PATRIC; fig|1457173.3.peg.194; -. DR Proteomes; UP000020766; Unassembled WGS sequence. 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: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 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; PF09163; Form-deh_trans; 1. DR PIRSF; PIRSF036298; FDH_4Fe4S; 1. DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1. DR TIGRFAMs; TIGR01582; FDH-beta; 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 Reference proteome {ECO:0000313|Proteomes:UP000020766}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}; KW Transport {ECO:0000256|ARBA:ARBA00022448}. FT DOMAIN 30..58 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51379" FT DOMAIN 94..126 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51379" FT DOMAIN 127..156 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51379" FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 290..309 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..22 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 39 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR036298-50" FT BINDING 42 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR036298-50" FT BINDING 45 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR036298-50" FT BINDING 49 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" 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 106 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR036298-50" FT BINDING 111 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR036298-50" FT BINDING 115 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 142 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="4" FT /evidence="ECO:0000256|PIRSR:PIRSR036298-50" FT BINDING 146 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="3" 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 166 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR036298-50" FT BINDING 178 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR036298-50" FT BINDING 182 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR036298-50" SQ SEQUENCE 309 AA; 33476 MW; 8D2271D5F6398B34 CRC64; MSSTMSLDIK RRSATTTPAP SAREAHSGEV AKLIDVSKCI GCKACQTACM EWNDLRDEIG TSAAGVYDNP TDLTDQSWTV MRFAEYENEA TGNLEWLIRK DGCMHCEDPG CLKACPSPGA IVQYANGIVD FQQDQCVGCG YCVTGCPFNI PRISKKDHKA YKCTLCSDRV AVGREPACVK TCPTGAIMFG TKKAMHDQAE RRIGDLKQRG YANAGLYDPA AVGGTHVMYV LHHADKPSLY KGLPDDPKIS PMVSLWKGVA KPLAMAALGA AAVGSLFHYI TKGPNDVSKE LEDEMERKDA EALNKENGK //