ID A2SEZ2_METPP Unreviewed; 988 AA.
AC A2SEZ2;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Formate dehydrogenase large subunit {ECO:0000313|EMBL:ABM94131.1};
DE EC=1.2.1.2 {ECO:0000313|EMBL:ABM94131.1};
GN OrderedLocusNames=Mpe_A1170 {ECO:0000313|EMBL:ABM94131.1};
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM94131.1, ECO:0000313|Proteomes:UP000000366};
RN [1] {ECO:0000313|EMBL:ABM94131.1, ECO:0000313|Proteomes:UP000000366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC {ECO:0000313|Proteomes:UP000000366};
RX PubMed=17158667; DOI=10.1128/JB.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
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 -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP000555; ABM94131.1; -; Genomic_DNA.
DR RefSeq; WP_011828768.1; NC_008825.1.
DR AlphaFoldDB; A2SEZ2; -.
DR STRING; 420662.Mpe_A1170; -.
DR KEGG; mpt:Mpe_A1170; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_1_1_4; -.
DR Proteomes; UP000000366; Chromosome.
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; 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; 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; 2.
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; 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 ECO:0000313|EMBL:ABM94131.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000366};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 77..133
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 988 AA; 109386 MW; 24860B07163A21C7 CRC64;
MLLTRKSPDA GSGSPASSLV SSLSRGLSRA IPTMDRRSFL RRSGLGVGAG LAAGQLTLVR
KAQASDASKA EAGPGKVEVR RTVCGHCSVG CAVDAVVHNG VWVRQEPVFD SPINLGAHCA
KGAALREHGR GEYRLRYPMK LVNGKYERIS WDTALDEISA RMLELRKQSG PDSVFVVGSS
KHNNEQAYLL RKWMSLWGSN NCDHQARICH STTVAGVANT WGYGAMTNSY NDMQNARMAL
YIGSNAAEAH PVSMLHMLHA KETGCKMIVV DPRFTRTAAR ADEHVRIRSG SDIPFLFGVL
HHIFKNGWED KQYINDRVYG MDKVREDVLA NWTPDKVQEA CGVDEATVFR VAKTMADNRP
GTIVWCMGQT QHTIGNAMVR ASCILQLALG NIGKSGGGAN IFRGHDNVQG ATDVGPNPDS
LPGYYGLAEG SFKHFAKTWG VDFEWIKKQY APGMMTKPGM TVSRWVDGVL EKNELIDQDS
NLRGLFFWGH APNSQTRGLE MKKAMDKLDL LVVVDPFPSA TAAMAAMPGK PEDQNPNRAV
YLLPATTQFE TSGSCTASNR SIQWREQVIE PLWESRNDHM IMYQLAQKLG FDKELTKNYK
LVAGKGGMME PEPESILREI NKSVWTIGYT GQSPERLKVH MRNMHVFDVK TLRAKGGTDK
ETGYSLDGDY FGLPWPCYGT PEMKHPGSPN LYDTSKHVMD GGGNFRANFG VEKDGVNLLA
EDGSFSKGAD LTTGYPEFDH VLLKKLGWWD ELSEPEKAAA EGKNWKTDSS GGIIRVAMKN
HGCHPFGNAK ARAVVWNFPD AIPKHREPLY STRPDLVAKY PTHDDKKAFW RLPTLFKTVQ
DKNKDIGKDF PLIMSSGRLV EYEGGGEETR SNPYLAELQQ EMFVEINPAT ANDRGIRNGE
TVWVRTPTGA RLTVKALVTE RVDRETVWLP FHFSGRWQGV DLAPYYPQGA MPVIRGEAIN
TATTYGYDSV TMMQETKTTV CQVERASV
//
