ID A0A1A6AFW4_9TREE Unreviewed; 442 AA.
AC A0A1A6AFW4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=2,2-dialkylglycine decarboxylase (Pyruvate) {ECO:0008006|Google:ProtNLM};
GN ORFNames=I303_00736 {ECO:0000313|EMBL:OBR88918.1};
OS Kwoniella dejecticola CBS 10117.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296121 {ECO:0000313|EMBL:OBR88918.1, ECO:0000313|Proteomes:UP000078595};
RN [1] {ECO:0000313|EMBL:OBR88918.1, ECO:0000313|Proteomes:UP000078595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10117 {ECO:0000313|EMBL:OBR88918.1,
RC ECO:0000313|Proteomes:UP000078595};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus dejecticola CBS10117.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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DR EMBL; KI894027; OBR88918.1; -; Genomic_DNA.
DR RefSeq; XP_018266760.1; XM_018404106.1.
DR AlphaFoldDB; A0A1A6AFW4; -.
DR STRING; 1296121.A0A1A6AFW4; -.
DR GeneID; 28964435; -.
DR VEuPathDB; FungiDB:I303_00736; -.
DR OrthoDB; 345661at2759; -.
DR Proteomes; UP000078595; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000078595};
KW Transferase {ECO:0000256|ARBA:ARBA00022576}.
SQ SEQUENCE 442 AA; 47832 MW; 820F4E6F955625DD CRC64;
MPAPTFDAQQ FWSDADSHLI RYSGGGDFVK RVIVKAQGCT MIDSEGNEII DWTSGQMSSM
LGHGNQEIVQ VVNDSMSTLD HLFSGFVSKP VVEAAKFLSS LLPPQLSKVQ FLNTGAESNE
CALRMAKLYT GKHEVVSFSS SWHGMTQAAA AATYSAGRKG YGPNSPGQFV LPTPSPHRSR
FRKEDGSYDW EAELNFGFEL IDCQSTGNLA AAIVEPILSS GGVIELPAGY MKALKAHCER
RGMLLIIDEA QTGVGRTGDM FAFEHEGVVP DILTLSKTLG CGLPVAATIT SAQIEQDVFE
KGFLFYTTHV SDPLCAAVAL KAMEIVTRDQ LHLRAKELGK KVKNGLLDLQ KKYKCIGEVR
GRGLLLGVEI ISGPDSPHSA QVLGAAISDR CMDLGLSMNI VRLAHMGGVF RIAPPLTISE
ELVEKALDLM DEAFRTTKGT TW
//
