ID A0A0M2CTW5_9MICC Unreviewed; 909 AA.
AC A0A0M2CTW5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:EYT52219.1};
GN ORFNames=H488_0110155 {ECO:0000313|EMBL:EYT52219.1};
OS Kocuria sp. UCD-OTCP.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=1292021 {ECO:0000313|EMBL:EYT52219.1, ECO:0000313|Proteomes:UP000033173};
RN [1] {ECO:0000313|EMBL:EYT52219.1, ECO:0000313|Proteomes:UP000033173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-OTCP {ECO:0000313|EMBL:EYT52219.1,
RC ECO:0000313|Proteomes:UP000033173};
RX PubMed=23661474;
RA Coil D.A., Doctor J.I., Lang J.M., Darling A.E., Eisen J.A.;
RT "Draft Genome Sequence of Kocuria sp. Strain UCD-OTCP (Phylum
RT Actinobacteria).";
RL Genome Announc. 1:E00172-13(2013).
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}.
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:EYT52219.1}.
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DR EMBL; AOSQ01000019; EYT52219.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2CTW5; -.
DR HOGENOM; CLU_000422_1_2_11; -.
DR Proteomes; UP000033173; Unassembled WGS sequence.
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 Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR048158; Formate_DH_Act.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR NCBIfam; NF041513; formate_DH_Act; 1.
DR PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR Pfam; PF00384; Molybdopterin; 2.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00022485};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 2..397
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 440..484
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 729..833
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
FT REGION 125..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 909 AA; 100092 MW; 8A15F7BACBE3A1EA CRC64;
MANADCIVIQ GSNMAECHPV GYQWVTEAKA RGARVIHVDP RFTRTSAVAD KHVPIRAGSD
IVLLGALVNH VLTHDLWFEE YVRAYTNAAT LVNEDYRDAE DLDGLFSGFD PETGQYDMST
WAYAENEGGA GDHDGRVDAP AGDPDHGAEE GAEAVDEAAG QQLGSGGAPM EHARMQRDET
LQDPRTVFQI LKRHYARYTP EMVQEVCGVS PEDFAYLARS ITENSGRERT TCFAYAVGWT
QHSLGAQYIR TASILQLLLG NMGRPGGGIM ALRGHASIQG STDIPTLFNL LPGYLPMPVA
GTHDTFDDYL AAIASKKQKG YWAEADAYTT SLLKAWWGDA ATADNDWAYD YLPRLTGAHG
TFQTLTKMLD DEVEGYFLLG QNPAVGSSNG RMQRMAMSHL KWLVVRDLNL IESATWWKDG
PEIASGELRT EDIETEVFFL PAATHVEKSG TFTQTQRLLQ WRHQAVAPPG ECQSELQFFF
ELGRRIRERL AGSGDERDRP LLDLTWDYPV DEHGEPDPEA VLAEINGRHL TGPDAGKPLS
SYTEMRADGS TSGGCWIYTG VYADGVNRAA ARRPGEEQGP AALEWGWAWP ANRRLLYNRA
SADPEGRPWS ERKKLVWWDE EQDQWVGDDV PDFPLHLAPG TRPDPDSGGA AALAGDDPFI
MQADGKGWLY APKGVLDGPL PTHYEPQESP VANALYTQQR NPSRVLFARQ DNLTAPSAGE
PGADVYPYVF TTYRLTEHHT AGGMSRWLPY LSELQPEMFC EVSPELAAEC GLEPYGWATI
VSPRAAIEVR VLVTERMTPL VVRGHTVHQI GLPYHWGVGD DAVVSGDSAN DLLGLTLEPN
VQIQDSKVGS CHIRPGRRPR GPELLDLVLE YQQRAGATVE TGNTRIDVPG TDRSTDPGTD
PTTDPMREH
//
