ID A0A0P0MEN9_9BURK Unreviewed; 987 AA.
AC A0A0P0MEN9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Formate dehydrogenase H {ECO:0000313|EMBL:ALK91243.1};
DE EC=1.1.99.33 {ECO:0000313|EMBL:ALK91243.1};
GN Name=fdhF_1 {ECO:0000313|EMBL:ALK91243.1};
GN ORFNames=L103DPR2_00837 {ECO:0000313|EMBL:ALK91243.1};
OS Limnohabitans sp. 103DPR2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Limnohabitans.
OX NCBI_TaxID=1678129 {ECO:0000313|EMBL:ALK91243.1, ECO:0000313|Proteomes:UP000063254};
RN [1] {ECO:0000313|EMBL:ALK91243.1, ECO:0000313|Proteomes:UP000063254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=103DPR2 {ECO:0000313|EMBL:ALK91243.1,
RC ECO:0000313|Proteomes:UP000063254};
RA Ahn J.-H., Kim S.B.;
RT "Limnohabitans sp. 2 strains.";
RL Submitted (JUN-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 -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP011834; ALK91243.1; -; Genomic_DNA.
DR RefSeq; WP_055359887.1; NZ_CP011834.1.
DR AlphaFoldDB; A0A0P0MEN9; -.
DR STRING; 1678129.L103DPR2_00837; -.
DR KEGG; lim:L103DPR2_00837; -.
DR PATRIC; fig|1678129.3.peg.829; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000063254; 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:ALK91243.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000063254};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 76..132
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 987 AA; 109619 MW; 5D61FEE1C7EB2E5C CRC64;
MLLTKKNSGT SGASASPFVH SLRRGLTQAL PTLDRRTFLR RSGLGVGVGL AASQLSLVKK
AQAGTQGGSI IGAGKVEVKR TVCTHCSVGC AVDAVVENGV WVRQEPVFDS PINLGAHCAK
GAALREHGHG EYRLRYPMKL VNGKYERISW DLALKEISER MMELRKASGP DSVYFIGSSK
HNNEQAYLMR KFVSFWGTNN TDHQARICHS TTVAGVANTW GYGAMTNSYN DMQNSKCALY
IGSNAAEAHP VSMLHMLHAK ENGCKMIVVD PRFTRTAAKA DEYVRIRSGT DIPFLFGIVY
HIFKNGWEDK KYINDRVYGM EAVKADIMAK WTPDKVEEAC GVKEEQVFKV AKMLHENNPS
TIVWCMGQTQ HTIGNAMVRA SCILQLALGN IGKSGGGTNI FRGHDNVQGA TDVGPNPDSL
PGYYGLAEGS WKHFAKAWDV DFEWIKGRYA SPAMMGKNGI TVSRWIDGVL EKNELIDQDS
NLRGVFYWGH APNSQTRGLE MKRAMDKLDL LVVVDPYPSA TAAMAAMPGK PEDLNPNRAV
YLLPAATQFE TSGSCTASNR SLQWRDKVID PLWESRSDHM IMYQLADKLG FGKELVKNYK
MQKVKGMDEP VPEDILREIN KCVWTIGYTG QSPERLKAHM RNMHLFDVKT LKSKGGKDKE
TGYDFGDDYF GLPWPCYGTP ELKHPGSPNL YDTSKHVMEG GGNFRANFGV EREGKSLLAE
DGSHSKGADI TTGYPELDHV LLKKLGWWGE LTEAEAKAAE GKNWKTDSSG GMIRVFMKNH
GCHPFGNAKA RAVVWNFPDP IPQHREPLYG TRADMMAKYP THDDKKAFWR LPTLYKTIQD
KNIADKVHEK FPLIMTSGRL VEYEGGGEET RSNPWLAELQ QEMFVEINPQ TASKRGIRNG
ERAWVKTPTG ARLNVQALVT ERVAPDTVFL PFHFSGRWQG ADMLAHYPNG AAPIVRGEAV
NTATTYGYDS VTMMQETKTT VCDVEKA
//
