ID Q2T0X3_BURTA Unreviewed; 645 AA.
AC Q2T0X3;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Cholesterol oxidase {ECO:0000313|EMBL:ABC36409.1};
GN OrderedLocusNames=BTH_I0619 {ECO:0000313|EMBL:ABC36409.1};
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 /
OS CIP 106301 / E264).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848 {ECO:0000313|EMBL:ABC36409.1, ECO:0000313|Proteomes:UP000001930};
RN [1] {ECO:0000313|EMBL:ABC36409.1, ECO:0000313|Proteomes:UP000001930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264
RC {ECO:0000313|Proteomes:UP000001930};
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP000086; ABC36409.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2T0X3; -.
DR KEGG; bte:BTH_I0619; -.
DR HOGENOM; CLU_456985_0_0_4; -.
DR BRENDA; 1.1.3.6; 8156.
DR Proteomes; UP000001930; Chromosome I.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016899; F:oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.10; FAD-linked oxidases, C-terminal domain; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR015213; Cholesterol_OX_subst-bd.
DR InterPro; IPR016170; Cytok_DH_C_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR010031; FAD_lactone_oxidase-like.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR43762; L-GULONOLACTONE OXIDASE; 1.
DR PANTHER; PTHR43762:SF1; L-GULONOLACTONE OXIDASE; 1.
DR Pfam; PF09129; Chol_subst-bind; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827}.
FT DOMAIN 129..321
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 645 AA; 70287 MW; 2BA2C410E3A9E27D CRC64;
MTHARCHLSS NDFRSAGHNL LQNNHALRTT STRLKRETHF DSLKSFTPTL RNPSTFEKPM
KKILGDPASR VRRRAFLGDI ARLAGAGVVA GWTPIRPIPA HAQPAGAAPP NFPADIPLHK
QAFRNWSGEI AVADLWTAVP ATPADVVAIV NWAASNGYRA RPLGHMHNWS PLTVAGNGAS
ERTILVDTTT HLTAVSVDAS ATPARVVAQA GVSLDTLLAT LEQHGLGMAA APAPGDITLG
GALAIGAHGT ALPAADETRT PGHTYGSLSN AVLALTAVVH DASSGRYALR TFDRTDPDIG
PFLAHVGRAF VVEATLQVGA NQRLQCESFV DIPASELFAP AGSRGRTVES FVRRSGRIEA
IWFPFTDYPW LKVWTVRPTR PSGARVVDQP YNYPFSDSIS QHVSDLVSRI VLNGEIQLAP
LFGKTQYTIT YLGLTNIFGP RTNLWGWSRS VLHYVRPTTL RVTANGYAVL TRRENVQRAI
NEFVGAYRQR IADYRAAGRY PVNGPVEIRV TGVDTPADVG PGAVPPSLSA IRPRPDHPDW
NAAIWFDILT IPGTPDANRF YREIEQWMLS NYSGDYATVR PEWSKGWGYA DTAAWSDGAM
LGTTIPDLFR LGLSPADNWD AALRTLERYD PRRVFSSPLL DRLMG
//
