GenomeNet

Database: UniProt
Entry: E0TBM8_PARBH
LinkDB: E0TBM8_PARBH
Original site: E0TBM8_PARBH 
ID   E0TBM8_PARBH            Unreviewed;       555 AA.
AC   E0TBM8;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Putative cholesterol oxidase {ECO:0000313|EMBL:ADM08403.1};
GN   OrderedLocusNames=PB2503_01622 {ECO:0000313|EMBL:ADM08403.1};
OS   Parvularcula bermudensis (strain ATCC BAA-594 / HTCC2503 / KCTC 12087).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Parvularculales;
OC   Parvularculaceae; Parvularcula.
OX   NCBI_TaxID=314260 {ECO:0000313|EMBL:ADM08403.1, ECO:0000313|Proteomes:UP000001302};
RN   [1] {ECO:0000313|Proteomes:UP000001302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-594 / HTCC2503 / KCTC 12087
RC   {ECO:0000313|Proteomes:UP000001302};
RA   Kang D.-M., Oh H.-M., Cho J.-C.;
RT   "Genome sequence of Parvularcula bermudensis HTCC2503.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADM08403.1, ECO:0000313|Proteomes:UP000001302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-594 / HTCC2503 / KCTC 12087
RC   {ECO:0000313|Proteomes:UP000001302};
RX   PubMed=21037002; DOI=10.1128/JB.01205-10;
RA   Oh H.M., Kang I., Vergin K.L., Kang D., Rhee K.H., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2503T of Parvularcula bermudensis,
RT   the type species of the order "Parvularculales" in the class
RT   Alphaproteobacteria.";
RL   J. Bacteriol. 193:305-306(2011).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002156; ADM08403.1; -; Genomic_DNA.
DR   AlphaFoldDB; E0TBM8; -.
DR   STRING; 314260.PB2503_01622; -.
DR   KEGG; pbr:PB2503_01622; -.
DR   eggNOG; COG2303; Bacteria.
DR   HOGENOM; CLU_040036_0_0_5; -.
DR   Proteomes; UP000001302; Chromosome.
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   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR47470; CHOLESTEROL OXIDASE; 1.
DR   PANTHER; PTHR47470:SF1; FAD-DEPENDENT OXIDOREDUCTASE 2 FAD BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001302}.
FT   DOMAIN          475..542
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   555 AA;  59800 MW;  63DA12A2746A2FED CRC64;
     MGQNYSNNKQ NIQKAAKQTK SGVSTGRRDL LKVGLASALS TSVLSAPAIA RPFRQRERHR
     AVIIGTGFGG AVTALRLAQA GIDVTLLERG IRWPSGPNGD TFPDFEGASK DPRTTWLSNA
     PAFQPIGQGG VLPDKVLEKL FFKPFTGLQE RVVGNGLDII CGAGVGGGSL TYQGVTMQPS
     EAQFVADLPG LDYGKFDRDY YRRVEAMLRL APIPDDLLYH PTYKAALQWH DRIAAAGETP
     YRTRMPIDWS FAQAELRGEM KPVYTTGDLV FGVNNGGKFS LDKTYIAAAE ATGRVSLKVL
     HNVTDIHRDR WGRWLVDVDI IDTGGEVMQR KRLVTDALFL GAGSAGTTRL LMKAKAKDQI
     ADLPDDVGGQ WGNNGDRIFV WRPSDVSPGP QQGGPTAIAL QDWDNPGGPL TLMQGPVPAK
     VDVGVSTLVG FGPVSPGGYF TYDERKDDAV LNWDQAVDRE LTQRITAKMQ EVVGPDDLLF
     DTTTAETTTW HPLGGAIMGK VCDLAGRVMG QTGLYVVDGA LIAGSTGACN PSMTIAALAE
     HCIETVLKED LGRVF
//
DBGET integrated database retrieval system