ID A0A257EI09_9BURK Unreviewed; 580 AA.
AC A0A257EI09;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:OYU12720.1};
GN ORFNames=CFE38_06990 {ECO:0000313|EMBL:OYU12720.1};
OS Comamonadaceae bacterium PBBC1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=2015580 {ECO:0000313|EMBL:OYU12720.1, ECO:0000313|Proteomes:UP000216161};
RN [1] {ECO:0000313|EMBL:OYU12720.1, ECO:0000313|Proteomes:UP000216161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBBC1 {ECO:0000313|EMBL:OYU12720.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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:OYU12720.1}.
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DR EMBL; NKIP01000004; OYU12720.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257EI09; -.
DR Proteomes; UP000216161; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF152; OXIDASE (CODA), PUTATIVE (AFU_ORTHOLOGUE AFUA_8G04090)-RELATED; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 2.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968}.
FT DOMAIN 148..171
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT BINDING 150
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 290
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 516
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 580 AA; 62662 MW; 00309A06D48E0F58 CRC64;
MTHHIANFEE PNDTLMERLE RALIAGRMNR RHFMRAAAAA GFGAIGLNAL ADELDAIRVN
QNQRSAKLQG AYDYVVVGAG SAACALVGRL ATRKDASILM IEAGDWDTAP SVMDPSVWFT
NLGTERDWGD VAIASPSTNN RAIPEHMGRV VGGGSSINAT IWARPFKNDL EYWAQASGDK
AWGYESALNI YRGMENWQGK PDARYRGKNG PVWCQPAHNP HPVANAMLQA CKVLGYPVLD
DQNGQREEGG IGFALMNQII RDGRRQSMAR SYLYPVLSRP NVTVVVNTHV DRLALSGTKV
TGVHIHRAGV QSVISANTEV ILCSGGINTP KLLMLSGIGD EAQLRQHGIK TVVNAKEVGK
NFQDHLLHGG CIFEPKEHIP HRNSAANAAG FLKSQSSLAA PDVNIVQIEL PYASDVVAKQ
YTPPGTSWAL CAGLVAPKSR GEIKLRSADA KDRPIVDAKF LSHPDDVKAL AFGIEVSRDI
GNSAAMKDFV KREVAPGKKL AGKDMEDFVR NGATTYFHQS GTCRMGKDSE AVVDAQLRVN
GIQGLRIADS SIMPRIASVA TMATCALIGE RMADILTARS
//
