ID Q17994_CAEEL Unreviewed; 414 AA.
AC Q17994;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 164.
DE RecName: Full=Aspartate aminotransferase {ECO:0000256|RuleBase:RU000480};
DE EC=2.6.1.1 {ECO:0000256|RuleBase:RU000480};
GN Name=got-2.2 {ECO:0000313|EMBL:CCD64538.1,
GN ECO:0000313|WormBase:C14F11.1};
GN ORFNames=C14F11.1 {ECO:0000313|WormBase:C14F11.1}, CELE_C14F11.1
GN {ECO:0000313|EMBL:CCD64538.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD64538.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CCD64538.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD64538.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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; BX284606; CCD64538.1; -; Genomic_DNA.
DR PIR; T15494; T15494.
DR RefSeq; NP_741810.1; NM_171702.4.
DR AlphaFoldDB; Q17994; -.
DR SMR; Q17994; -.
DR DIP; DIP-24489N; -.
DR STRING; 6239.C14F11.1a.2; -.
DR EPD; Q17994; -.
DR PaxDb; 6239-C14F11-1a-2; -.
DR PeptideAtlas; Q17994; -.
DR EnsemblMetazoa; C14F11.1.1; C14F11.1.1; WBGene00015778.
DR GeneID; 180897; -.
DR KEGG; cel:CELE_C14F11.1; -.
DR UCSC; C14F11.1b.1; c. elegans.
DR AGR; WB:WBGene00015778; -.
DR WormBase; C14F11.1; CE02477; WBGene00015778; got-2.2.
DR eggNOG; KOG1411; Eukaryota.
DR GeneTree; ENSGT00950000183082; -.
DR HOGENOM; CLU_032440_1_0_1; -.
DR InParanoid; Q17994; -.
DR OMA; VGACTIV; -.
DR OrthoDB; 1123851at2759; -.
DR PhylomeDB; Q17994; -.
DR Reactome; R-CEL-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-CEL-70263; Gluconeogenesis.
DR Reactome; R-CEL-8963693; Aspartate and asparagine metabolism.
DR Reactome; R-CEL-8964539; Glutamate and glutamine metabolism.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00015778; Expressed in larva and 4 other cell types or tissues.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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:0006533; P:aspartate catabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Aminotransferase {ECO:0000256|RuleBase:RU000480,
KW ECO:0000313|EMBL:CCD64538.1};
KW Proteomics identification {ECO:0007829|EPD:Q17994,
KW ECO:0007829|PeptideAtlas:Q17994};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Transferase {ECO:0000256|RuleBase:RU000480}.
FT DOMAIN 43..409
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 414 AA; 45617 MW; D055D18D212B52D0 CRC64;
MSVSKKLFST AVRGKSWWSH VEMGPPDAIL GVTEAFKADS NPKKINLGVG AYRDDQGKPF
VLPSVKEAER QVIAANLDKE YAGIVGLPEF TKLSAQLALG ENSDVIKNKR IFTTQSISGT
GALRIGSEFL SKYAKTKVIY QPTPTWGNHV PIFKFAGVDV KQYRYYDKST CGFDETGALA
DIAQIPEGST ILLHACAHNP TGVDPSRDQW KKISDIVKKR NLFVFFDMAY QGFASGDVDN
DAFAVRYFVE QGHNIVLSQS FAKNMGLYGE RVGAFSVVTS DADEAARVAS QVKILIRPLY
SNPPVHGARI ASRILADPAL NKQWLGDVKL MADRIITMRT TLKDLLAKEG STRNWEHITN
QIGMFCFTGI NPQQVEKLIK EHSVYLTKDG RISVAGISSN NVAYLAHALH QVTK
//
