ID A0A074X9J6_AURPU Unreviewed; 448 AA.
AC A0A074X9J6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:KEQ82043.1};
GN ORFNames=M438DRAFT_67880 {ECO:0000313|EMBL:KEQ82043.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ82043.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ82043.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ82043.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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; KL584989; KEQ82043.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074X9J6; -.
DR STRING; 1043002.A0A074X9J6; -.
DR HOGENOM; CLU_016922_10_0_1; -.
DR OrthoDB; 345661at2759; -.
DR Proteomes; UP000030706; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; PTHR11986; AMINOTRANSFERASE CLASS III; 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 ECO:0000313|EMBL:KEQ82043.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000030706};
KW Transferase {ECO:0000313|EMBL:KEQ82043.1}.
SQ SEQUENCE 448 AA; 48235 MW; 55B7B4E46683911E CRC64;
MSVTKLAEFG AKHVARGIGR LSNHVLESGA GSYVTTTEGR KMLDFTSGIG VTNLGHCHPT
VTKAAQEQVG KLVHGQVNIA FQKPYLELVE SLLPMMPHKS LDTFFFWNSG SEAVEAAVKL
ARHATKKQNI IVMQGSYHGR TFGTMAMTRS KTIYGENYAP LMPGVFSVPF PYCKQCSIAL
NADGKFGFDK CCMDPVLQLE LLLKRETAPS DTAAIFVEPV LGEGGYVPPP AGYLAALRKI
CDKHNILLVA DEVQCGFGRT GKMFAVEHWD VRPDILIMAK GIANGFPLSG IVSRKELMDK
QQPGSMGGTY AGNAVSCAAG VAVAKAFKEE KILDNVNARG GELKGALQAA KEDPKTGKLI
YDVRGLGLML ALECTPGKGY ASKIQAKCME KDMLVLTTSI YDTLRFIPPL NITKEDMAKG
IQIITDAIKE VAAGEDPQET ATKGQAPE
//
