ID A0A1X1RWX1_MYCCE Unreviewed; 770 AA.
AC A0A1X1RWX1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:ORV19588.1};
GN ORFNames=AWB95_01255 {ECO:0000313|EMBL:ORV19588.1};
OS Mycobacterium celatum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=28045 {ECO:0000313|EMBL:ORV19588.1, ECO:0000313|Proteomes:UP000193907};
RN [1] {ECO:0000313|EMBL:ORV19588.1, ECO:0000313|Proteomes:UP000193907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44243 {ECO:0000313|EMBL:ORV19588.1,
RC ECO:0000313|Proteomes:UP000193907};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-2016) 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}.
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:ORV19588.1}.
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DR EMBL; LQOM01000006; ORV19588.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1RWX1; -.
DR STRING; 28045.AWB95_01255; -.
DR Proteomes; UP000193907; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR CDD; cd02787; MopB_CT_ydeP; 1.
DR CDD; cd02767; MopB_ydeP; 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; IPR037951; MopB_CT_YdeP.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR010046; Mopterin_OxRdtse_a_bac.
DR InterPro; IPR041953; YdeP_MopB.
DR NCBIfam; TIGR01701; Fdhalpha-like; 1.
DR PANTHER; PTHR43105:SF4; PROTEIN YDEP; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR PIRSF; PIRSF000144; CbbBc; 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:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 127..503
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 770 AA; 84657 MW; FD9790F422FFBD34 CRC64;
MLGQGTPESA APGCGPGEGR PKKRDYHHPA AGWGAAMSVS KVLLQRRELL EGPQVIVRMN
HENGGFDCPG CAWPDDRKGL RLDICENGIK HSTWEMDPKR VGPDFFAAHS VTELLTWSDF
ALEDAGRLTQ PMVYDPQSDH YVPIEWERAF ALIGETLRGL DSPNQASFYT SGRLGNEATF
LYQWFVREFG TNNFPDCSNM CQEASGVALL TTLGTGKGTV DLVDWEESDC LIIMGVNAAT
NAPRMLTALV EAHRRGAAIV HINPLIEAAA TRTIVPHEML DMALFRATDI STMNIQPRTG
GDFALIRGVA KALLETAKDD PAAIDELFIE RYTRGFAQYK AACEAVSWPE IEHQSGVPVD
QIRGLADVYR NARASIIAWC LGVSQHAHGP DAVREIVNLL LLRGNIGREG AGPCPIRGHS
NVQGNRTCGV DHHPSEEFLD RIAAACEIDV PREHGLDVVA TINAMHRGDV KVFFGMGGNF
ALAAPDTAYT FEALRQCELT VHVSTKLNRS HLVHGRRALI LPCVARTEID RQASGIQSIT
VEDSMSMVHL SVGMKEPASP HLLSEPAIVA GIAEATLPNS KTPWRELVAD YDLIRNRMAK
GLYGFEDFNR RVRQPLGFRI RQPARELVFL TDSGKAEFSA AELPNVVPPE GQLILGTMRS
HDQFNTTVYS DDDRYRGVKN LRTLLFMNTI DMAEMGISEF DYIDITSIAK DGTRRSVYGY
RAVGYDIPRG CAAGYMPELN VLCPIGNFNA ESGQPVMKHV PIEVTRSAAR
//