ID A0A099P6Y3_PICKU Unreviewed; 526 AA.
AC A0A099P6Y3;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=JL09_g951 {ECO:0000313|EMBL:KGK39977.1};
OS Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=4909 {ECO:0000313|EMBL:KGK39977.1, ECO:0000313|Proteomes:UP000029867};
RN [1] {ECO:0000313|Proteomes:UP000029867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SD108 {ECO:0000313|Proteomes:UP000029867};
RX PubMed=25159171; DOI=10.1186/s12934-014-0121-4;
RA Xiao H., Shao Z., Jiang Y., Dole S., Zhao H.;
RT "Exploiting Issatchenkia orientalis SD108 for succinic acid production.";
RL Microb. Cell Fact. 13:121-121(2014).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
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:KGK39977.1}.
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DR EMBL; JQFK01000005; KGK39977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099P6Y3; -.
DR VEuPathDB; FungiDB:C5L36_0A01180; -.
DR eggNOG; KOG1232; Eukaryota.
DR HOGENOM; CLU_017779_4_1_1; -.
DR Proteomes; UP000029867; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2190; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
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; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF02913; FAD-oxidase_C; 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 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 83..262
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 526 AA; 57982 MW; 2DDA7F22D1E063F5 CRC64;
MFALASISRL GRASASARAR ASAVLSIRGF ALTAEKYPSV KRGDYAKLTD EDLGKFHSIL
NPNQIITDAA DLAAFNQDWM KKYAGQSQLV LKPKTTQQVS QILKYCNERK LAVVPQGGNT
GLVGGSVPVF DEIVISMAGM NQIRSFDENS GTLKVDAGVI LENADNYLAE RGYIFPLDLG
AKGSCFVGGN VATNAGGLRL LRFGSLHGSV LGLEVVLADG TIVDSMHSLR KDNTGFDLKQ
LFIGSEGTLG IITGVSILCP ARPKAVNIAF LGLESYEHVI QCFKEARSDL GEILSAFEFM
DRDSQLVASK FLKTTHPLCQ EDEVAEASVP EYPFYVLLET SGSNKDHDDE KLEKFLEKVM
ENEVVVDGTV SQDEAQLKTL WTWREGIAEA SQQFGGVYKY DVSLPLDSLY KLVEETQERL
KSFSLASTED ESKPVYEAIG YGHIGDGNLH LNVAVREYNK EVEKALEPFV YEFIEKHNGS
ISAEHGLGFQ KKNYIGYSKS EVEIKMMKEL KNHYDPNGIL NPYKYI
//
