ID   Q753W1_EREGS            Unreviewed;       419 AA.
AC   Q753W1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   RecName: Full=Aspartate aminotransferase {ECO:0000256|RuleBase:RU000480};
DE            EC=2.6.1.1 {ECO:0000256|RuleBase:RU000480};
GN   ORFNames=AGOS_AFR211C {ECO:0000313|EMBL:AAS53582.1};
OS   Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL
OS   Y-1056) (Yeast) (Ashbya gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS53582.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS53582.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC         Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC         Evidence={ECO:0000256|RuleBase:RU000480};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC       ECO:0000256|RuleBase:RU000480}.
CC   -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
CC       chloroplastic isozymes. {ECO:0000256|RuleBase:RU000480}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR   EMBL; AE016819; AAS53582.1; -; Genomic_DNA.
DR   RefSeq; NP_985758.1; NM_211112.1.
DR   AlphaFoldDB; Q753W1; -.
DR   STRING; 284811.Q753W1; -.
DR   EnsemblFungi; AAS53582; AAS53582; AGOS_AFR211C.
DR   GeneID; 4622019; -.
DR   KEGG; ago:AGOS_AFR211C; -.
DR   eggNOG; KOG1412; Eukaryota.
DR   HOGENOM; CLU_032440_1_2_1; -.
DR   InParanoid; Q753W1; -.
DR   OMA; SWAIRYF; -.
DR   OrthoDB; 1123851at2759; -.
DR   Proteomes; UP000000591; Chromosome VI.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005777; C:peroxisome; IEA:EnsemblFungi.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006532; P:aspartate biosynthetic process; IBA:GO_Central.
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; IPR000796; Asp_trans.
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; PTHR11879; ASPARTATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11879:SF55; GLUTAMATE OXALOACETATE TRANSAMINASE 1, ISOFORM B; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00799; TRANSAMINASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|RuleBase:RU000480};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Transferase {ECO:0000256|RuleBase:RU000480}.
FT   DOMAIN          32..407
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   419 AA;  45673 MW;  F802CA54DEB59822 CRC64;
     MSLTAFNQLE ILPPDALFDV KKRLTQDTRS FKVDLGLGAY RDENGKPWVL PCVREAEKQL
     MADPGYNHEY LGIAGLEEFR AAAARVLLGE DSEALAEGRV VSVQSISGTG ALHVAAKLLA
     KTVPDATVYM SDPTWGNHFA VFETQGLRTA TYPYWDAATR SLDMEGVLGA LGAAPRGSVF
     VLHACAHNPT GLDPNEEQWV QILDAVAARE HTVLFDSAYQ GFASGSLARD AYALRAGLRR
     LAEVTPVLVC QSFAKNIGMY GERVGALHVV LPRQPAESLA HVKAAVLSQL SHITRSELSN
     PPAYGAKIVT KVLTTPELAA QWKKDMITMS SRIARMRRVL RDRLVELGTP GNWDHIVQQC
     GMFSYTGLTK EMVARMEKDF AIYMVSSGRI SIAGLNDSNV GHVANAIDNA VRHFSTPKL
//