ID D4B5T4_ARTBC Unreviewed; 459 AA.
AC D4B5T4;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Aminotransferase, classes I and II family {ECO:0000313|EMBL:EFE29270.1};
GN ORFNames=ARB_03841 {ECO:0000313|EMBL:EFE29270.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE29270.1, ECO:0000313|Proteomes:UP000008866};
RN [1] {ECO:0000313|Proteomes:UP000008866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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:EFE29270.1}.
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DR EMBL; ABSU01000050; EFE29270.1; -; Genomic_DNA.
DR RefSeq; XP_003009915.1; XM_003009869.1.
DR AlphaFoldDB; D4B5T4; -.
DR STRING; 663331.D4B5T4; -.
DR GeneID; 9525260; -.
DR KEGG; abe:ARB_03841; -.
DR eggNOG; KOG0256; Eukaryota.
DR HOGENOM; CLU_017584_1_2_1; -.
DR OMA; EYATGCN; -.
DR OrthoDB; 1328656at2759; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43795; BIFUNCTIONAL ASPARTATE AMINOTRANSFERASE AND GLUTAMATE/ASPARTATE-PREPHENATE AMINOTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR43795:SF63; PUTATIVE (AFU_ORTHOLOGUE AFUA_4G00630)-RELATED; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00753; ACCSYNTHASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:EFE29270.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000008866};
KW Transferase {ECO:0000313|EMBL:EFE29270.1}.
FT DOMAIN 85..437
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 459 AA; 50842 MW; AC91A79F20C7EAFE CRC64;
MSSGDSSASV RPATVSNRAA KVSKETAANK MWDVFTDLYD AATNENGFVN VGVAENFLMH
GTLLDYIRTH ADLPPHYLTY NDGGDGSRRL KTAASRFLNR HLKPVVPLKP EHLMVTNGVS
AAIEHLAWAF TDPGEGILLG RPHYGAFLPD MTSRPEAEVV PVSFDDLDPF EVRCVTKYER
ALLDFEARTG KRVRALMLCH PHNPLGRCYP RETIIELMKF CQRYQIHLIS DEIYALSVWE
NTVDTAPGTP PPVKFVSALS IPTQGLIDAN LLHALWGMSK DFGANGLRVG VIISQSNPEL
LAAIKGPTLY SYVSGLSDHV ASSILENEGF TDRYIAVNQR KLSESYAFVA RAMQDHDIEY
AAGCNASFFV WVNLGKAYLR NKQIPMPADL TRTVMDELIS KRVFLADGTA FGSEKPGWFR
IVFSHPRPFL DKALGRIMAA IGEPYKYASK PECSARAKL
//
