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
//