AAT4_ARATH
ID AAT4_ARATH Reviewed; 403 AA.
AC P46646; Q9SI69;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Aspartate aminotransferase, cytoplasmic isozyme 2;
DE EC=2.6.1.1;
DE AltName: Full=Transaminase A;
GN Name=ASP4; OrderedLocusNames=At1g62800; ORFNames=F23N19.17, F23N19_26;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=7894512; DOI=10.1046/j.1365-313x.1995.07010061.x;
RA Schultz C.J., Coruzzi G.M.;
RT "The aspartate aminotransferase gene family of Arabidopsis encodes
RT isoenzymes localized to three distinct subcellular compartments.";
RL Plant J. 7:61-75(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
CC -!- FUNCTION: Important for the metabolism of amino acids and Krebs-cycle
CC related organic acids. In plants, it is involved in nitrogen metabolism
CC and in aspects of carbon and energy metabolism.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P46646-1; Sequence=Displayed;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF19543.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U15035; AAA79372.1; -; mRNA.
DR EMBL; AC007190; AAF19543.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34006.1; -; Genomic_DNA.
DR PIR; H96652; H96652.
DR RefSeq; NP_564803.1; NM_104958.2. [P46646-1]
DR AlphaFoldDB; P46646; -.
DR SMR; P46646; -.
DR STRING; 3702.AT1G62800.2; -.
DR PaxDb; P46646; -.
DR PRIDE; P46646; -.
DR ProteomicsDB; 245170; -. [P46646-1]
DR EnsemblPlants; AT1G62800.1; AT1G62800.1; AT1G62800. [P46646-1]
DR GeneID; 842579; -.
DR Gramene; AT1G62800.1; AT1G62800.1; AT1G62800. [P46646-1]
DR KEGG; ath:AT1G62800; -.
DR Araport; AT1G62800; -.
DR eggNOG; KOG1411; Eukaryota.
DR HOGENOM; CLU_032440_1_2_1; -.
DR InParanoid; P46646; -.
DR OMA; TGANHMA; -.
DR PhylomeDB; P46646; -.
DR BioCyc; ARA:AT1G62800-MON; -.
DR PRO; PR:P46646; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P46646; baseline and differential.
DR Genevisible; P46646; AT.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; ISS: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:0006531; P:aspartate metabolic process; ISS:UniProtKB.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006536; P:glutamate metabolic process; ISS: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 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Aminotransferase; Cytoplasm;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..403
FT /note="Aspartate aminotransferase, cytoplasmic isozyme 2"
FT /id="PRO_0000123873"
FT BINDING 37
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P46645"
FT MOD_RES 249
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 199
FT /note="I -> F (in Ref. 1; AAA79372)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 403 AA; 44358 MW; BC6046EF6F970216 CRC64;
MNSILSSVLP APEDPVLSVI FACRDDPSPV KLNLSAGTYR TEEGKPLVLD VVRRAEQQLA
NDLDKEYLPL NGLPEFNKLS TKLILGDDSP ALKENRVVTT QCLSGTGSLR VGAEFLATHN
KESVIFVPNP TWGNHPRIFT LAGLSVQYFR YYDPKSRGLD FKGMLEDLGA APPGAIVVLQ
ACAHNPTGVD PTFEQWEKIR RLVRSKSLLP FFDSAYQGFA SGSLDADAQA VRMFVADGGE
CLIAQSYAKN MGLYGERIGS LTIVCTSEDV AKKVENQVLL VVRPMYLTPP IHGASIVATI
LKNSDMYNDW TIELKGMADR IISMRQQLYA ALEARGTPGD WSHIIKHIGM FTFTGLSEEQ
VRLMAKEYHI YMTYDGRISM ASLSSKTVPQ LADAIHAVVT RIA
