GenomeNet

Database: UniProt
Entry: A0A081CPA1_PSEA2
LinkDB: A0A081CPA1_PSEA2
Original site: A0A081CPA1_PSEA2 
ID   A0A081CPA1_PSEA2        Unreviewed;       780 AA.
AC   A0A081CPA1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=GMC oxidoreductase {ECO:0000313|EMBL:GAK68497.1};
GN   ORFNames=PAN0_115c6757 {ECO:0000313|EMBL:GAK68497.1};
OS   Pseudozyma antarctica (Yeast) (Candida antarctica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX   NCBI_TaxID=84753 {ECO:0000313|EMBL:GAK68497.1};
RN   [1] {ECO:0000313|EMBL:GAK68497.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 10317 {ECO:0000313|EMBL:GAK68497.1};
RA   Morita T., Saika A., Koike H.;
RT   "Draft genome sequence of the yeast Pseudozyma antarctica JCM 10317 known
RT   as a producer of lipase B which used in a wide range of industrial
RT   applications.";
RL   Submitted (JUL-2014) 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, ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; DF830182; GAK68497.1; -; Genomic_DNA.
DR   RefSeq; XP_014653303.1; XM_014797817.1.
DR   AlphaFoldDB; A0A081CPA1; -.
DR   GeneID; 26307543; -.
DR   HOGENOM; CLU_002865_6_0_1; -.
DR   OrthoDB; 858083at2759; -.
DR   Proteomes; UP000053758; 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   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 4.10.450.10; Glucose Oxidase, domain 2; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR027424; Glucose_Oxidase_domain_2.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11552:SF218; GMC_OXRDTASE_N DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
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.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053758}.
FT   DOMAIN          211..234
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          714..755
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   780 AA;  80798 MW;  B6A829DDC5E69D1A CRC64;
     MHSVSSGVGS EVRRHDLLVH PPASPRQTAS PKQASGAGRN AKKLWCAQPV FAHAAASIYP
     AKLPNLDSRP PSSLARSASP SHSLLWNVGG MKLVLLLSLA AACAAVPSPV DYLLFRRSVT
     TDAGALSGNT YDYVIVGGGL AGLVVANRLS ANPNISVAVI EAGASGYADA AKFSVPAANL
     YDSSVGTQYD WQWQTTPQSG LAGRSAPWPR GKVLGGSSAI NGLYYVRPSD TEQNAWSNLI
     ADDAWNWDNM FAAMKKSESF TAPNDATTRT VNVGYNAASH GTDGPLHVSY PLRTYPEVGA
     FIESATSVGI PASQDPNAGN NTGVFLATSN INPANATRSF SRTAYLDPVA ARPNLSVLTG
     HTVTRVVFNS TQGDEAVASG VQFAASRGAA VSTVYARKEV VLCGGAVNDP QILQLSGIGD
     AALLQRVGVE QVVDLAGVGY HLQDHLSTGV VFSPSSDATM PPTRITGDAA TDSYVNSAIA
     YVRGSTLFSD PQWTSLIDQM RQNRAASIAA YDAPSAVKAG YNATYTTQVE TLFPTSVGPI
     ELLFALSFGG VQVQAALQHP LSRGSITVTS TDAFTPPRID PGYLSNDVDM VILRQGFKLA
     RRVGSTSPLA DFTSAETAPG VGVETDAQWD EWIRRTVGTE YHPSSTCSML PRELGGVVDA
     KLKVYGTRNL RVIDAAVPPV SFSAHLMSVT YGLAEIGAEM VLQDYAAGMK SNTTQAATGG
     SRGSSGSSGS SGSSGSTGST GSRGAAGSSA SGATSAATRP TLTTAHAAAA MIAIIALALL
//
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