ID A0A4P8IRW3_9BURK Unreviewed; 986 AA.
AC A0A4P8IRW3;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:QCP48649.1};
GN ORFNames=FAZ95_05255 {ECO:0000313|EMBL:QCP48649.1};
OS Trinickia violacea.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Trinickia.
OX NCBI_TaxID=2571746 {ECO:0000313|EMBL:QCP48649.1, ECO:0000313|Proteomes:UP000298656};
RN [1] {ECO:0000313|EMBL:QCP48649.1, ECO:0000313|Proteomes:UP000298656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHOD12 {ECO:0000313|EMBL:QCP48649.1,
RC ECO:0000313|Proteomes:UP000298656};
RA Gao Z.-H., Qiu L.-H.;
RT "Burkholderia sp. DHOD12, isolated from subtropical forest soil.";
RL Submitted (MAY-2019) 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}.
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DR EMBL; CP040077; QCP48649.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4P8IRW3; -.
DR OrthoDB; 9815647at2; -.
DR Proteomes; UP000298656; Chromosome 1.
DR GO; GO:0051536; F:iron-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 430..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 986 AA; 109809 MW; 52A8A660C641A783 CRC64;
MEHRARTQNE KLEVKTTTCY MCACRCGIRV HLRDGEVRYI DGNPNHPLNQ GVICAKGSSG
IMKQYSPARL TQPLMRKPGA ERGTAQFEPV SWDVAFATLE KRLGHLRATD PKKFALFTGR
DQMQALTGLF AKQFGTPNYA AHGGFCSVNM AAGMIYTMGG SFWEFGGPDL DSAKLFFMIG
TAEDHHSNPL KIALSKFKRA GGRFIAINPV RTGYAAIADE WVPIRPGTDG ALFMALIREL
IETESYDREF VTRYTNAAEL LDMNAERNTF GLFVQDPESP VGNPLFPQNR MWWDPAAQRA
VVHHAPGVTP ALEGRYALAD GTPVVPSFAL LREQVAECTP EWASEITGIP ADTIRRLAQE
MADTARDHKI TLPIPWTDAW GQTHDTVTGN PIAFHAMRGL AAHSNGFQSI RALSILMSIM
GTIDRPGGFR HKSPYPRAVP PSAKPPNDPD VIQPNTPLAN GPLGWPAAPE DLFVDKDGQP
GRIDKAFSWE YPLAVHGLMH SVITNAWRGD PYPIDTLFIF MANLAWNSSM NTVEVRKMLA
DKHENGEHKI PFIVVCDAFQ SEMTAFADLI LPDTTYLERH DAMSVLDRPI SEYDGPVDSV
RVPVVPPTGE CKPFQEVLIE LGSRLKLPAF TKEDGTRKYR DYPDFVVNFQ TSPNSGVGFL
AGWRGKDGDK ALVGEPNPNQ WEQYAKNNCV FHFTLPESIQ YMRNCNGPYL KWAVENGFRK
FDTPIVIQLY SDVLQKFRLA ARGKTTGRQP PDHLRARIER YFDPLPFYYP PLENAATDTA
RYPLAAITQR PMAMYHSWDS QNAWLRQIHG ENYLFMNPRM AQENGIEDGG WIYVESQWGK
VRCMARYSEA VEPGTVWTWN AIGKAAGAWN LGPDANESKH GFLLNHLITD ELPAQEKNAA
AGARMSNSDP VTGQAAWYDV RVRVYPAEAD ADHTLPQFAP MTALPGSTGA NAVQRVVQAY
FAGRGEFAKR LMQAVKPAAK HHDGEQ
//