ID V5DY58_9GAMM Unreviewed; 517 AA.
AC V5DY58;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=2-oxopropyl-CoM reductase, carboxylating {ECO:0000313|EMBL:ESS72256.1};
DE EC=1.8.1.5 {ECO:0000313|EMBL:ESS72256.1};
GN Name=xecC {ECO:0000313|EMBL:ESS72256.1};
GN ORFNames=MGMO_63c00040 {ECO:0000313|EMBL:ESS72256.1};
OS Methyloglobulus morosus KoM1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methyloglobulus.
OX NCBI_TaxID=1116472 {ECO:0000313|EMBL:ESS72256.1, ECO:0000313|Proteomes:UP000017842};
RN [1] {ECO:0000313|EMBL:ESS72256.1, ECO:0000313|Proteomes:UP000017842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KoM1 {ECO:0000313|EMBL:ESS72256.1,
RC ECO:0000313|Proteomes:UP000017842};
RX PubMed=24356841;
RA Poehlein A., Deutzmann J.S., Daniel R., Simeonova D.D.;
RT "Draft Genome Sequence of the Methanotrophic Gammaproteobacterium
RT Methyloglobulus morosus DSM 22980 Strain KoM1.";
RL Genome Announc. 1:e01078-13(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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:ESS72256.1}.
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DR EMBL; AYLO01000061; ESS72256.1; -; Genomic_DNA.
DR RefSeq; WP_023494712.1; NZ_AYLO01000061.1.
DR AlphaFoldDB; V5DY58; -.
DR STRING; 1116472.MGMO_63c00040; -.
DR PATRIC; fig|1116472.3.peg.1950; -.
DR eggNOG; COG1249; Bacteria.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000017842; Unassembled WGS sequence.
DR GO; GO:0050628; F:2-oxopropyl-CoM reductase (carboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR22912:SF217; DIHYDROLIPOYL DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000313|EMBL:ESS72256.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017842}.
FT DOMAIN 41..364
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 384..499
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 517 AA; 57369 MW; 0F74A59BC7FE62CB CRC64;
MDVWGDCLTI EKWQHFVAET LESGNSTPVF NINPNDTREF DAIFLGGGAA GRFGAAYLRA
LGGRVLILDR WPFLGGSCPH QACVPHHLFS DCAAQLMLER TFSGKLWFQN LNDKIVSIKD
IVELFRTGRT GPHAVMNFQS KEQLGLEFVL NAEFEIIDAH TVQVGDRKFH VKNLVLALGA
KPFVPDIPGA TLKGVFTSQT LVENLDFEPG NTIVVIGGGK SAIEYGCFFN ATGRRTIVVA
RNQVMPMLKD AESRAYAILM MEEQGMEFFE NAEVMEIQGD AQGKVRSVSI KTSDGIIDID
TDFVFMGLGE QANSEIIAQK LGLETSDKGF IKVNRHMQTS VPHVYAVGDV TGPPMEMFKA
RKEGVCAAKN IMGQASEYKT ADYPDFMHTH YEACWLGLSE EEARQRYANV KIMKLPPDNP
NGLDVGLPAG DRMMLYLMAK PRMSGFQKLI LDGDTRKILG ATHIGYGAKD GFQYLNYLVK
KGLTIDDLAD MDELFISPSY FIQLCRLRAG DPHFNDM
//
