AAT_STRAW
ID AAT_STRAW Reviewed; 408 AA.
AC Q82DR2;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Aspartate aminotransferase {ECO:0000303|PubMed:24302739};
DE Short=AAT {ECO:0000303|PubMed:24302739};
DE Short=AspAT {ECO:0000305};
DE EC=2.6.1.1 {ECO:0000269|PubMed:24302739};
GN Name=aspC1 {ECO:0000312|EMBL:BAC72619.1};
GN ORFNames=SAVERM_4907 {ECO:0000312|EMBL:BAC72619.1};
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=RCR2011;
RX PubMed=24302739; DOI=10.1074/jbc.m113.486480;
RA Graindorge M., Giustini C., Kraut A., Moyet L., Curien G., Matringe M.;
RT "Three different classes of aminotransferases evolved prephenate
RT aminotransferase functionality in arogenate-competent microorganisms.";
RL J. Biol. Chem. 289:3198-3208(2014).
CC -!- FUNCTION: Catalyzes the reversible conversion of aspartate and 2-
CC oxoglutarate to glutamate and oxaloacetate (PubMed:24302739). Does not
CC have prephenate aminotransferase activity (PubMed:24302739).
CC {ECO:0000269|PubMed:24302739}.
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:24302739};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q56232};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q56232}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; BA000030; BAC72619.1; -; Genomic_DNA.
DR RefSeq; WP_010986326.1; NZ_JZJK01000077.1.
DR AlphaFoldDB; Q82DR2; -.
DR SMR; Q82DR2; -.
DR STRING; 227882.SAV_4907; -.
DR EnsemblBacteria; BAC72619; BAC72619; SAVERM_4907.
DR KEGG; sma:SAVERM_4907; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_11; -.
DR OMA; APYWTTY; -.
DR OrthoDB; 554560at2; -.
DR Proteomes; UP000000428; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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 Pfam; PF00155; Aminotran_1_2; 1.
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"
FT /id="PRO_0000448264"
FT BINDING 45
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P00509"
FT BINDING 134
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT BINDING 184
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT BINDING 382
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT MOD_RES 247
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P58350"
SQ SEQUENCE 408 AA; 43569 MW; 210DFB532CDA849A CRC64;
MSAATPPTER RVSARVGAIS ESATLAVDAK AKALKAAGRP VIGFGAGEPD FPTPDYIVQA
AIEACSNPKY HRYTPAGGLP ELKAAIAAKT LRDSGYEVDA SQVLVTNGGK QAIYEAFAAI
LDPGDEVIVP APYWTTYPES IRLAGGVPVD VVADETTGYR VSVEQLEAAR TENTKVLLFV
SPSNPTGAVY TREQIEEIGR WAAEKGLWVL TDEIYEHLVY GDAEFHSLPV VVPELADKCI
VVNGVAKTYA MTGWRVGWVI GPKDVIKAAT NLQSHATSNV SNVAQVAALA AVSGDLTAVA
EMREAFDRRR KTIVRMLNEI GGVLCPEPEG AFYAYPSVKA LLGKEIRGKR PQDTVELAAL
ILEEAEVAVV PGEAFGTPGY LRLSYALGDE DLVEGVSRIQ KLLSEAKD
