AAT_SYNY3
ID AAT_SYNY3 Reviewed; 389 AA.
AC Q55128;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
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, ECO:0000269|PubMed:25070637};
GN Name=aspC; OrderedLocusNames=sll0402;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=25070637; DOI=10.1105/tpc.114.127407;
RA Dornfeld C., Weisberg A.J., Ritesh K.C., Dudareva N., Jelesko J.G.,
RA Maeda H.A.;
RT "Phylobiochemical characterization of class-Ib aspartate/prephenate
RT aminotransferases reveals evolution of the plant arogenate phenylalanine
RT pathway.";
RL Plant Cell 26:3101-3114(2014).
CC -!- FUNCTION: Catalyzes the reversible conversion of aspartate and 2-
CC oxoglutarate to glutamate and oxaloacetate (PubMed:24302739,
CC PubMed:25070637). Has very weak prephenate aminotransferase activity
CC (PubMed:25070637). {ECO:0000269|PubMed:24302739,
CC ECO:0000269|PubMed:25070637}.
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, ECO:0000269|PubMed:25070637};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:25070637};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=486 uM for 2-oxoglutarate {ECO:0000269|PubMed:25070637};
CC KM=2538 uM for prephenate {ECO:0000269|PubMed:25070637};
CC Note=kcat is 54.2 sec(-1) with 2-oxoglutarate as substrate. kcat is
CC 1.1 sec(-1) with prephenate as substrate.
CC {ECO:0000269|PubMed:25070637};
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; BA000022; BAA10261.1; -; Genomic_DNA.
DR PIR; S74343; S74343.
DR AlphaFoldDB; Q55128; -.
DR SMR; Q55128; -.
DR IntAct; Q55128; 1.
DR STRING; 1148.1001121; -.
DR PaxDb; Q55128; -.
DR EnsemblBacteria; BAA10261; BAA10261; BAA10261.
DR KEGG; syn:sll0402; -.
DR eggNOG; COG0436; Bacteria.
DR InParanoid; Q55128; -.
DR OMA; SVAMTGW; -.
DR PhylomeDB; Q55128; -.
DR Proteomes; UP000001425; 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:0009058; P:biosynthetic process; IEA:InterPro.
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..389
FT /note="Aspartate aminotransferase"
FT /id="PRO_0000123854"
FT BINDING 38
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT BINDING 124
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT BINDING 174
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT BINDING 364
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT MOD_RES 238
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P58350"
SQ SEQUENCE 389 AA; 42352 MW; 7706C9C353EA317F CRC64;
MRLTQRVSQV VPSITLEITA KAKAMRTEGI DVLSFTAGEP DFTTPPHIVE AAKLALDEGK
TRYGPAAGEP ALRQAIAKKL REKNNLPYEA ANILVTNGGK HSLFNLMLAM IEQGDEVIIP
APYWLSYPEM VRLAEGTPVI VNTTAATDYK ITPEQLRQAI TSKSKLFVLN SPSNPTGAVY
TPAEIRALAA VILEYEDLYV VSDEIYERIL YDGTEHLSIG AVNDEIFQRT IISNGFAKSY
SMTGWRVGYL AGELPLIQAC STIQGHSTSN VCTFAQYGAI AALENPQTCV ETMVKAFTER
RQVIVEGINQ IAGLSCPNPK GAFYVFVDIA KTGLNSLEFS ARLLESHQVA VIPGAAFGAD
DCVRFSYATD MDTIKQGLAE LERFVSTLA
