AAT_MUSP7
ID AAT_MUSP7 Reviewed; 400 AA.
AC C6C2Z3;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Aspartate aminotransferase {ECO:0000303|PubMed:25070637};
DE Short=AAT {ECO:0000305};
DE Short=AspAT {ECO:0000303|PubMed:25070637};
DE EC=2.6.1.1 {ECO:0000269|PubMed:25070637};
GN OrderedLocusNames=Dd703_1457 {ECO:0000312|EMBL:ACS85258.1};
OS Musicola paradisiaca (strain Ech703) (Dickeya paradisiaca) (Dickeya
OS dadantii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Musicola.
OX NCBI_TaxID=579405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ech703;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Dickeya dadantii Ech703.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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:25070637). Has very
CC weak prephenate aminotransferase activity (PubMed:25070637).
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:25070637};
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; CP001654; ACS85258.1; -; Genomic_DNA.
DR AlphaFoldDB; C6C2Z3; -.
DR SMR; C6C2Z3; -.
DR STRING; 579405.Dd703_1457; -.
DR EnsemblBacteria; ACS85258; ACS85258; Dd703_1457.
DR KEGG; dda:Dd703_1457; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_6; -.
DR OMA; RLGFCGG; -.
DR Proteomes; UP000002734; 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:1901605; P:alpha-amino acid metabolic process; IEA:UniProt.
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; Transferase.
FT CHAIN 1..400
FT /note="Aspartate aminotransferase"
FT /id="PRO_0000448263"
FT BINDING 37
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P00509"
FT BINDING 126
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT BINDING 176
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT BINDING 367
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 400 AA; 44119 MW; 34B328065779B6BF CRC64;
MRSVADRVKR IGLSETYAIL DKVKKMKAEG HVVYDLGGGE PDFSTPEHII NFTVSAMKNG
MTHYTASKGS PGLLKAIANR LFEENHISAC WDKNIIVTPS AKHALFITLM TLLNPGDEIV
IPSPCWVSYI AMAEMAGAKA VDLPLTRENK YQITRKALAA CITDKTRVLL LNNPNNPTGH
ILTEEEIQVI CQVALEHDLF VVMDEIYEHI RYITAPHRSI AAEPGMFERT ITVSGFSKAW
AMTGWRLGYL CAPEYVLNEI LKVQQHSVGC AGAFIQQGGL AALIGDRQPM EDMVKAYRKR
RDYMVDSLNR IPGIECYVPE GGLYVYADIR GLGMGDAQTF TLWLLAHAHV AVTPGTAFGK
EETMMIRLSF AGAMETIVAA MDSIAEAITE YDASLQQEAS
