ID W1QKC2_OGAPD Unreviewed; 428 AA.
AC W1QKC2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Salicylate hydroxylase (Salicylate 1-monooxygenase) {ECO:0000313|EMBL:ESX02317.1};
GN ORFNames=HPODL_05066 {ECO:0000313|EMBL:ESX02317.1};
OS Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL
OS Y-7560 / DL-1) (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=871575 {ECO:0000313|EMBL:ESX02317.1, ECO:0000313|Proteomes:UP000008673};
RN [1] {ECO:0000313|EMBL:ESX02317.1, ECO:0000313|Proteomes:UP000008673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC {ECO:0000313|Proteomes:UP000008673};
RX PubMed=24279325; DOI=10.1186/1471-2164-14-837;
RA Ravin N.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V., Schneider J.,
RA Mardanova E.S., Smekalova E.M., Zvereva M.I., Dontsova O.A., Mardanov A.V.,
RA Skryabin K.G.;
RT "Genome sequence and analysis of methylotrophic yeast Hansenula polymorpha
RT DL1.";
RL BMC Genomics 14:837-837(2013).
RN [2] {ECO:0000313|Proteomes:UP000008673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC {ECO:0000313|Proteomes:UP000008673};
RA Ravin N.V., Mardanov A.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V.,
RA Zvereva M.I., Smekalova E.M., Dontsova O.A., Skryabin K.G.;
RT "Genome sequence of the methylotrophic yeast Hansenula polymorpha DL1.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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:ESX02317.1}.
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DR EMBL; AEOI02000004; ESX02317.1; -; Genomic_DNA.
DR RefSeq; XP_013936903.1; XM_014081428.1.
DR AlphaFoldDB; W1QKC2; -.
DR STRING; 871575.W1QKC2; -.
DR GeneID; 25774489; -.
DR KEGG; opa:HPODL_05066; -.
DR eggNOG; ENOG502RSIP; Eukaryota.
DR HOGENOM; CLU_009665_6_4_1; -.
DR OMA; WLNEHDA; -.
DR OrthoDB; 1786978at2759; -.
DR Proteomes; UP000008673; Chromosome II.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR PANTHER; PTHR13789:SF309; PUTATIVE (AFU_ORTHOLOGUE AFUA_6G14510)-RELATED; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Monooxygenase {ECO:0000313|EMBL:ESX02317.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008673}.
FT DOMAIN 9..333
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 428 AA; 48456 MW; 26D393DFF81ED000 CRC64;
MTDVTKPLEI AIVGGGIVGA FAAATLSRLP NSRVTLYEKS EGPREAGAWI ALTEAALLTL
SRIANIEEVQ EFVYRGKPAP LARRHWKTGE VLKYDTSSFP RPDNFVQART HRVPLHNFVL
KHVPEGVIKY NHAAVKVDVD SSGAILHFEN QDPVRADLVV AADGIYSRIR RQFRVNEKLE
YKGIVAYRYV FDEKLLKDVD GVLDDTSAWM GRDGTWVFLG KVGLGKYGFV ALIPEPPNVA
SDLTWNRSAG QWGISHLLEF FQEWDPLITK IIKVLPDILA FPLERAPWLQ DLIIGDRIAF
AGDAAHPTSG VYAVGSSMGF DDIWALYRAL SETSTKSTNG DPDEQTKYNL PLSLFLFNET
RKHFLQRVER QTFIDGEVKK KYLNLAKDDS DWQRRLLNTL GGLDWVKEHN VELEYQKVRD
EHFLKIYT
//
