ID A0A0J5WRL9_BURCE Unreviewed; 978 AA. AC A0A0J5WRL9; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 29-MAY-2024, entry version 33. DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:KML57284.1}; GN ORFNames=VL15_14510 {ECO:0000313|EMBL:KML57284.1}; OS Burkholderia cepacia (Pseudomonas cepacia). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=292 {ECO:0000313|EMBL:KML57284.1, ECO:0000313|Proteomes:UP000036338}; RN [1] {ECO:0000313|EMBL:KML57284.1, ECO:0000313|Proteomes:UP000036338} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LK29 {ECO:0000313|EMBL:KML57284.1, RC ECO:0000313|Proteomes:UP000036338}; RA Chan X.Y.; RT "Draft genome of Burkholderia cepacia LK29."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|ARBA:ARBA00001966}; CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}. 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:KML57284.1}. 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; LDWR01000023; KML57284.1; -; Genomic_DNA. DR RefSeq; WP_048246326.1; NZ_LDWR01000023.1. DR AlphaFoldDB; A0A0J5WRL9; -. DR PATRIC; fig|292.27.peg.2813; -. DR Proteomes; UP000036338; 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:0043546; F:molybdopterin cofactor binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR CDD; cd02783; MopB_CT_2; 1. DR Gene3D; 2.40.40.20; -; 1. DR Gene3D; 3.30.200.210; -; 1. DR Gene3D; 3.40.50.740; -; 1. DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1. DR InterPro; IPR009010; Asp_de-COase-like_dom_sf. DR InterPro; IPR006657; MoPterin_dinucl-bd_dom. DR InterPro; IPR006656; Mopterin_OxRdtase. DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom. DR PANTHER; PTHR43598:SF5; DMSO REDUCTASE CHAIN A; 1. DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1. DR Pfam; PF04879; Molybdop_Fe4S4; 1. DR Pfam; PF00384; Molybdopterin; 1. DR Pfam; PF01568; Molydop_binding; 1. DR SMART; SM00926; Molybdop_Fe4S4; 1. DR SUPFAM; SSF50692; ADC-like; 1. DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1. DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485}; KW Iron {ECO:0000256|ARBA:ARBA00023004}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}. FT DOMAIN 12..68 FT /note="4Fe-4S Mo/W bis-MGD-type" FT /evidence="ECO:0000259|PROSITE:PS51669" FT REGION 434..460 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 438..452 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 978 AA; 108619 MW; F39EFC7230F0C8D7 CRC64; MEHRARERDE QAEIKTTTCY MCACRCGIRV HLRDGEVRYI DGNPEHPLNQ GVICAKGSSG IMKQYSPARL TQPLMRKAGA ERGDAQFEPV SWAVAFDVLE KRLAHLRATD PKRFALFTGR DQMQALTGLF AKQFGTPNYA AHGGFCSANM AAGMIYTIGG SFWEFGGPDL DNAKLFFMIG TAEDHHSNPL KIALGKFKRA GGRFIAINPV RTGYAAIADE WIPIRPGTDG ALFMALMHEL IARNAFDVEF VSRFTNAAEL VDQRDGADTF GLFVRDAAAP EVNALYPQNR MWWDTKTNRA VLHHTEGAEP ALDGRYTLDD GTPVAPSFTL LREQVAGCTP EWAADITGIA ADTIRRVARE METVARDHAI ELPVRWTDSW GKEHATVKGV PIAFHAMRGL AAHSNGFQTI RALAVLMSLL GTIDRPGGFR HKTPYPRAVP PSAKPPNDPA QVKPNTPLAT GPLGWPAGPE DLFIHPDGTP ARLDKAFSWE YPLAVHGLMH SVITNAWRGD PYPIDTLLIF MANMAWNSSM NTTEVRKMLV DKRDDGEYRI PFLVVCDAFA SEMTAFADLI LPDTTYLERH DVMSVLDRPI SEFDGPVDSV RVPVVPPTGE CKPFQEVLIE LASRLKFPAF TTVDGQRKYR DYPDFVINFQ TAPESGTGFL IGWRGKNGDK AVVGEPNPDQ WQRYAENNCV YHHRLPEPLQ YMRNCNGPYM QWAVDNGMRK FGVPIMIQLY SDVMQKFRLA AQGRTSGRQP PDHLRERIAR YFDPLPFWHR SLESGLTDAN RYPLAAITQR PMAMYHSWDS QNAWLRQIHG ENHLFVNPVT AAAQQIGDGA WIYVESPWGK VRCRARYSEA VEPGTVWTWN AIGKAAGAWN LGPEAGESQR GFLLNHVITD ELPDAARAGA RMSNSDPVTG QAGWYDVQVR IYPAEADAAT TLPQFAPMPP LPGTPRVLQR VQAYFAGTGA FAARLRRATA AGSQSDDS //