ID   F4WJG7_ACREC            Unreviewed;       430 AA.
AC   F4WJG7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Aspartate aminotransferase {ECO:0000256|RuleBase:RU000480};
DE            EC=2.6.1.1 {ECO:0000256|RuleBase:RU000480};
GN   ORFNames=G5I_05846 {ECO:0000313|EMBL:EGI65745.1};
OS   Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS   echinatior).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Acromyrmex.
OX   NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN   [1] {ECO:0000313|EMBL:EGI65745.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Nygaard S., Zhang G.;
RT   "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT   adaptations to social evolution and fungus farming.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000984,
CC         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; GL888182; EGI65745.1; -; Genomic_DNA.
DR   RefSeq; XP_011054104.1; XM_011055802.1.
DR   AlphaFoldDB; F4WJG7; -.
DR   STRING; 103372.F4WJG7; -.
DR   EnsemblMetazoa; XM_011055802.1; XP_011054104.1; LOC105145903.
DR   GeneID; 105145903; -.
DR   KEGG; aec:105145903; -.
DR   eggNOG; KOG1411; Eukaryota.
DR   InParanoid; F4WJG7; -.
DR   OrthoDB; 1123851at2759; -.
DR   Proteomes; UP000007755; Unassembled WGS sequence.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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:SF22; ASPARTATE AMINOTRANSFERASE, MITOCHONDRIAL; 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   ECO:0000313|EMBL:EGI65745.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW   Transferase {ECO:0000256|RuleBase:RU000480, ECO:0000313|EMBL:EGI65745.1}.
FT   DOMAIN          58..424
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   430 AA;  48018 MW;  EF9BF7AE3F2624E8 CRC64;
     MAHTTRLLVT TGNFLKSACN PFTMAARSSS SWWSHVEMGP PDAILGVTEA YKRDQNPKKI
     NLGAGAYRDD NGKPYVLPSV RKAEEKIRIK EMDKEYSTIA GNIEFCQHSI NLALGDENEV
     VPNGLNATVQ GISGTGSLFI GAQFLSHYFP GNKEIYLPTP SWGNHTPLFK LAGLTVKSYR
     YYDPKTCGLD FKGVMEDLSN IPEKSIILLH ACAHNPTGVD PKPEQWGELS TLIKKKNLFP
     FFDMAYQGFA SGDLTRDAYA VRLFIKEGHK IALAQSYAKN MGLYGERIGA FSLVTSNKDE
     AVRTLSQLKI LIRPMYSNPP IYGARIANEI LGDPELRKQW LYDVKGMADR IISVRAKLRD
     NLKKNGSTRD WSHITDQIGM FCYTGLKPNE VEKLTKDFSI YLTKDGRISM AGVTSKNVEY
     LAHAMHEVTK
//