ID A0A0Q8RIU6_9BURK Unreviewed; 986 AA.
AC A0A0Q8RIU6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:KRB94041.1};
GN ORFNames=ASE07_00380 {ECO:0000313|EMBL:KRB94041.1};
OS Noviherbaspirillum sp. Root189.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Noviherbaspirillum.
OX NCBI_TaxID=1736487 {ECO:0000313|EMBL:KRB94041.1, ECO:0000313|Proteomes:UP000051303};
RN [1] {ECO:0000313|EMBL:KRB94041.1, ECO:0000313|Proteomes:UP000051303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root189 {ECO:0000313|EMBL:KRB94041.1,
RC ECO:0000313|Proteomes:UP000051303};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB94041.1, ECO:0000313|Proteomes:UP000051303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root189 {ECO:0000313|EMBL:KRB94041.1,
RC ECO:0000313|Proteomes:UP000051303};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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:KRB94041.1}.
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DR EMBL; LMHZ01000001; KRB94041.1; -; Genomic_DNA.
DR RefSeq; WP_057288815.1; NZ_LMHZ01000001.1.
DR AlphaFoldDB; A0A0Q8RIU6; -.
DR STRING; 1736487.ASE07_00380; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000051303; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
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; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 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 InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 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 PIRSF; PIRSF036643; FDH_alpha; 3.
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.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS51318; TAT; 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 Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000051303};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 73..129
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 986 AA; 109299 MW; 9A7C91B6A765634E CRC64;
MLLTRKGQSG QRSPNRFTSS LSESLSRALP TMDRRTFLKR SGIGIGAGIA ASQLNLIQKA
RAADGDKAAG GKIEVKRTVC THCSVGCAVD AVVENGVWVR QEPVFDSPIN LGAHCAKGAA
LREHGHGEYR LKYPMKLVNG KYQRITWDQA LNEISARMLD IRKASGPDSV FFVGSSKHNN
EQSALLRKFV SFFGTNNTDH QARICHSTTV AGVANTWGYG AMTNSYNDMQ NAKAVMYIGS
NAAEAHPVSM LHMLHAKETG TKMIVVDPRF TRTAAKADQY IRIRSGSDIP YLYGMLYHIF
KNGWEDKQYI NDRVYGMEKV KEEVMKWTPD KVEEACGVPE AEVFKAAETM AKNRPSSLVW
CMGQTQHSIG NAMVRASCLV QLALGNVGVA GGGANIFRGH DNVQGATDVG PNPDSLPGYY
GLATGSWKHW AAVWGVDYEW IKKQFVSQAM MEKSGTTVSR WVDAVMEKNE LIDQDNNVKA
MLFWGHAPNS QTRGLDMKKA LDKLDLLVVI DPYPSATAAM AAMKVDGQEL NPNRAVYLLP
AATQFETSGS VTASNRSLQW REKVIEPLFE SRTDHMIMYQ LAEKLGFGKE LVAKIKLVPG
KGGMMEPEPE DMLREINRGT WTIGYTGQSP ERLKAHMRNM HLFDVKTLRC KAGKDAATGY
DMTGDYFGLP WPCYGTPELK HPGTHILYNT NQHLMDGGGC FRANFGVERE GVNLLAEDGS
HSAGSDITTG YPEFDHVLLK KLGWWDDLTD AEKKAAEGKN WKTDLSGGIQ RVCMKVHGVH
PFGNAKARAV VWNFPDPVPL HREPLYGTRA DLVAKYPTHD DKKGFWRLPT LYKSVQQKNV
ETKLYEKFPI ILTSGRLVEY EGGGEETRSN PWLAELQQDN FVEINPKAAA DRGIRNGEYV
IVSTPTGARL KVKALVTPRV GPDTAFIPFH FSGWWQGKDM LEYYPEGAAP VVRGEAVNTA
TTYGYDSVTM MQETKTTICN IERFTA
//
