AATC_CAEEL
ID AATC_CAEEL Reviewed; 408 AA.
AC Q22067;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Aspartate aminotransferase, cytoplasmic {ECO:0000305};
DE EC=2.6.1.1 {ECO:0000269|PubMed:29649217};
DE AltName: Full=Glutamate oxaloacetate transaminase 1.2;
DE AltName: Full=Transaminase A;
GN Name=got-1.2 {ECO:0000312|WormBase:T01C8.5};
GN Synonyms=got-1 {ECO:0000303|PubMed:29649217};
GN ORFNames=T01C8.5 {ECO:0000312|WormBase:T01C8.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF CYS-184.
RX PubMed=29649217; DOI=10.1371/journal.pgen.1007303;
RA Chitturi J., Hung W., Rahman A.M.A., Wu M., Lim M.A., Calarco J., Baran R.,
RA Huang X., Dennis J.W., Zhen M.;
RT "The UBR-1 ubiquitin ligase regulates glutamate metabolism to generate
RT coordinated motor pattern in Caenorhabditis elegans.";
RL PLoS Genet. 14:E1007303-E1007303(2018).
CC -!- FUNCTION: Biosynthesis of L-glutamate from L-aspartate
CC (PubMed:29649217). Important regulator of levels of glutamate, the
CC major excitatory neurotransmitter of the central nervous system
CC (PubMed:29649217). {ECO:0000269|PubMed:29649217}.
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:0000269|PubMed:29649217};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29649217}.
CC -!- TISSUE SPECIFICITY: Expressed in all somatic tissues including the
CC nervous system. {ECO:0000269|PubMed:29649217}.
CC -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
CC chloroplastic isozymes.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; BX284606; CCD68837.1; -; Genomic_DNA.
DR PIR; T29857; T29857.
DR RefSeq; NP_510709.1; NM_078308.5.
DR AlphaFoldDB; Q22067; -.
DR SMR; Q22067; -.
DR BioGRID; 46609; 13.
DR STRING; 6239.T01C8.5.1; -.
DR EPD; Q22067; -.
DR PaxDb; Q22067; -.
DR PeptideAtlas; Q22067; -.
DR EnsemblMetazoa; T01C8.5.1; T01C8.5.1; WBGene00020146.
DR GeneID; 181726; -.
DR KEGG; cel:CELE_T01C8.5; -.
DR UCSC; T01C8.5; c. elegans.
DR CTD; 181726; -.
DR WormBase; T01C8.5; CE07462; WBGene00020146; got-1.2.
DR eggNOG; KOG1412; Eukaryota.
DR GeneTree; ENSGT00950000183082; -.
DR HOGENOM; CLU_032440_1_2_1; -.
DR InParanoid; Q22067; -.
DR OMA; WDQNKRQ; -.
DR OrthoDB; 1104596at2759; -.
DR PhylomeDB; Q22067; -.
DR Reactome; R-CEL-70263; Gluconeogenesis.
DR Reactome; R-CEL-8963693; Aspartate and asparagine metabolism.
DR PRO; PR:Q22067; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00020146; Expressed in larva and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR GO; GO:0006532; P:aspartate biosynthetic process; IBA:GO_Central.
DR GO; GO:0006531; P:aspartate metabolic process; ISS:UniProtKB.
DR GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
DR GO; GO:2000213; P:positive regulation of glutamate metabolic process; IMP:UniProtKB.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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; PTHR11879; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..408
FT /note="Aspartate aminotransferase, cytoplasmic"
FT /id="PRO_0000123876"
FT BINDING 36
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT MOD_RES 251
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MUTAGEN 184
FT /note="C->Y: In hp731; decreases glutamate levels. Rescues
FT the defective backwards locomotion or 'reversals' movements
FT phenotype and decreases the increased glutamate levels in
FT ubr-1 mutants."
FT /evidence="ECO:0000269|PubMed:29649217"
SQ SEQUENCE 408 AA; 45493 MW; A4DDCBCB8C0EFD83 CRC64;
MSFFDGIPVA PPIEVFHKNK MYLDETAPVK VNLTIGAYRT EEGQPWVLPV VHETEVEIAN
DTSLNHEYLP VLGHEGFRKA ATELVLGAES PAIKEERSFG VQCLSGTGAL RAGAEFLASV
CNMKTVYVSN PTWGNHKLVF KKAGFTTVAD YTFWDYDNKR VHIEKFLSDL ESAPEKSVII
LHGCAHNPTG MDPTQEQWKL VAEVIKRKNL FTFFDIAYQG FASGDPAADA WAIRYFVDQG
MEMVVSQSFA KNFGLYNERV GNLTVVVNNP AVIAGFQSQM SLVIRANWSN PPAHGARIVH
KVLTTPARRE QWNQSIQAMS SRIKQMRAAL LRHLMDLGTP GTWDHIIQQI GMFSYTGLTS
AQVDHLIANH KVFLLRDGRI NICGLNTKNV EYVAKAIDET VRAVKSNI
