ID F3P4S3_9ACTO Unreviewed; 531 AA.
AC F3P4S3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Conserved domain protein {ECO:0000313|EMBL:EGF58362.1};
GN ORFNames=HMPREF9056_00022 {ECO:0000313|EMBL:EGF58362.1};
OS Actinomyces sp. oral taxon 170 str. F0386.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=762963 {ECO:0000313|EMBL:EGF58362.1, ECO:0000313|Proteomes:UP000004404};
RN [1] {ECO:0000313|EMBL:EGF58362.1, ECO:0000313|Proteomes:UP000004404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0386 {ECO:0000313|EMBL:EGF58362.1,
RC ECO:0000313|Proteomes:UP000004404};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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:EGF58362.1}.
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DR EMBL; AFBL01000002; EGF58362.1; -; Genomic_DNA.
DR AlphaFoldDB; F3P4S3; -.
DR STRING; 762963.HMPREF9056_00022; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_023699_0_0_11; -.
DR Proteomes; UP000004404; Unassembled WGS sequence.
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; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
FT DOMAIN 461..519
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 531 AA; 57305 MW; F7FE7813F698175D CRC64;
MRTVMTESIS RLIAPSFRDT DLANSVWDVI IVGGGLVGLS LACSLVTECP SLSCLIVEAG
PEATCNGAHI RSIGDDAERQ SATRLSQGPL RGVSISRAAS AAAHNLPVSE RANSLTRRAG
LHEVARGNGA IRLQGATALG GMGLYWLGAC PDPSPSELPT FIPYTEMRSA LAEARCILSV
QNDQFLDSRF TDYVQNKLAD TAPFAGVKRM PMAAVRSSDT RAVTNSVEVP LRKIERQVPR
RFLIRTETSC LEVKPPDTNV IRLVKLKDNQ TGRTYYENTR FVVLACDAIR SAQLLYASGV
RLDALGAYFN EHTQISLIAP IEMPVGTPRA DLIGGPLGAD LSPHESIPAG VTWLPYGVCD
LPYNGMITRI DKKESLLSMS DTAALASIHL YLPELLSAEN RISFSEKRTD WLGLPAPMLS
ENSEASEPDL REEVMRSSLN IARILGASWL PESPKVLPRG SSLHYQGTVR MGERNNGKSV
CDSVGEVWGE PNLFVAGNGV IPTATASNPT LYSVALAMRS ADAILRRLGL H
//