ID   A0A248VNX8_9BURK        Unreviewed;       974 AA.
AC   A0A248VNX8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:ASW00734.1};
GN   ORFNames=CJU94_21010 {ECO:0000313|EMBL:ASW00734.1};
OS   Paraburkholderia aromaticivorans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=2026199 {ECO:0000313|EMBL:ASW00734.1, ECO:0000313|Proteomes:UP000215158};
RN   [1] {ECO:0000313|Proteomes:UP000215158}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BN5 {ECO:0000313|Proteomes:UP000215158};
RA   Lee Y.;
RT   "Identification and genetic characteristics of simultaneous BTEX- and
RT   naphthalene-degrading Paraburkholderia sp. BN5 isolated from petroleum-
RT   contaminated soil.";
RL   Submitted (AUG-2017) 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; CP022990; ASW00734.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A248VNX8; -.
DR   KEGG; parb:CJU94_21010; -.
DR   OrthoDB; 9815647at2; -.
DR   Proteomes; UP000215158; Chromosome 2.
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; cd02763; MopB_2; 1.
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          431..461
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   974 AA;  108294 MW;  350F7A1B52A630F8 CRC64;
     MEHHARTQNE RLDVKTTTCY MCACRCGIRV HLRDGEVRYI DGNPEHPLNQ GVICAKGASG
     IMKQYSPARL TRPLMRKPGA ERGSAQFEPV SWEHAFDVLE QRLGAIRATD PKKFALFTGR
     DQMQALTGLF AKQFGTPNYA AHGGFCSANM AAGMIYTIGG SFWEFGGPDL DSAKLFFMIG
     TAEDHHSNPL KIALSKFKRA GGRFIAINPI RTGYAAIADE WVPIKPGTDG ALFMAFLHEL
     IAADAWDHEF VRRYTNAAEL VDLDEASDNF GLFVRDPERP VGNPLFPQNH LWWDASAARA
     VPHHAPGVTP ALEGRYTLDD GTPVTPSFAL LRERVADCTP EWAAAITGIS ADTIRRLAGE
     MIQTSREHRI TLPIRWTDAW GETHETVTGN PVAFHAMRGL AAHSNGFQSI RALAVLMSLL
     GTIDRPGGFR HKSPFPRAVP PSAKPPNSPD AVKPNTPLAT GPLGWPAAPE DLFIDDQGGP
     VRIDKAFSWE YPLAVHGVMH SVITNAWRGD PYPIDTLMIF MANMAWNSSM NTMKVREMLA
     DKHENGEYKI PFLVVCDAFQ SEMTAFADLI LPDTTYLERH DAMSMLDRPI SEFDGPVDSV
     RVPVVPPTGE CKPFQEVLIE LASRLKFPAF TTAGGARRFR DYPDFVVNFT TSPDSGVGFL
     SGWRGKDGDK ALVGEPNPRQ WEQYAKNNCV FHYRLPETLQ YMRNCNGPYL EWAVKNGFRK
     FGEPILIQLY SDVMQKFRLA AQGRTSGRQP PDHLRARVET YFDPLPFWYA PLESAATDLA
     RFPLAAVTQR PMAMYHSWDS QNAWLRQIHG ENYLYMNPLM AAEHGIADGS WIYAESQWGR
     VRCMARFSET VEPGTVWTWN AIGKAAGAWS LGPGANESQR GFLLNHLITD ELPGRDDEVA
     SRMSNSDPVT GQAAWYDVRV RIYPAEAHAR HTLPQFAAMP AVPGENGVIS RIVQTYFAGR
     GEFAARLRGA TGRK
//