AATC_SCHPO
ID AATC_SCHPO Reviewed; 409 AA.
AC O42652;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Aspartate aminotransferase, cytoplasmic;
DE EC=2.6.1.1;
DE AltName: Full=Transaminase A;
GN Name=aat2 {ECO:0000250|UniProtKB:P23542}; ORFNames=SPAC10F6.13c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000312|EMBL:CAA15726.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Plays a key role in amino acid metabolism. {ECO:0000250}.
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:0000250|UniProtKB:P23542};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P23542};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P23542}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
CC chloroplastic isozymes. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000255}.
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DR EMBL; CU329670; CAA15726.1; -; Genomic_DNA.
DR PIR; T37507; T37507.
DR RefSeq; NP_593264.1; NM_001018661.2.
DR PDB; 6JPK; X-ray; 2.10 A; A/B=1-409.
DR PDBsum; 6JPK; -.
DR AlphaFoldDB; O42652; -.
DR SMR; O42652; -.
DR BioGRID; 279456; 62.
DR STRING; 4896.SPAC10F6.13c.1; -.
DR iPTMnet; O42652; -.
DR MaxQB; O42652; -.
DR PaxDb; O42652; -.
DR PRIDE; O42652; -.
DR EnsemblFungi; SPAC10F6.13c.1; SPAC10F6.13c.1:pep; SPAC10F6.13c.
DR GeneID; 2543020; -.
DR KEGG; spo:SPAC10F6.13c; -.
DR PomBase; SPAC10F6.13c; -.
DR VEuPathDB; FungiDB:SPAC10F6.13c; -.
DR eggNOG; KOG1412; Eukaryota.
DR HOGENOM; CLU_032440_1_2_1; -.
DR InParanoid; O42652; -.
DR OMA; WDQNKRQ; -.
DR PhylomeDB; O42652; -.
DR BRENDA; 2.6.1.1; 5613.
DR Reactome; R-SPO-70263; Gluconeogenesis.
DR Reactome; R-SPO-8963693; Aspartate and asparagine metabolism.
DR PRO; PR:O42652; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
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:0006532; P:aspartate biosynthetic process; ISO:PomBase.
DR GO; GO:0006531; P:aspartate metabolic process; ISS:UniProtKB.
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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Aminotransferase; Cytoplasm; Phosphoprotein;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P23542"
FT CHAIN 2..409
FT /note="Aspartate aminotransferase, cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P23542"
FT /id="PRO_0000309451"
FT BINDING 38
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P23542"
FT MOD_RES 255
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23542"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:6JPK"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:6JPK"
FT HELIX 51..62
FT /evidence="ECO:0007829|PDB:6JPK"
FT HELIX 77..87
FT /evidence="ECO:0007829|PDB:6JPK"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:6JPK"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:6JPK"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:6JPK"
FT HELIX 107..122
FT /evidence="ECO:0007829|PDB:6JPK"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:6JPK"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:6JPK"
FT HELIX 140..147
FT /evidence="ECO:0007829|PDB:6JPK"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:6JPK"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:6JPK"
FT HELIX 167..176
FT /evidence="ECO:0007829|PDB:6JPK"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:6JPK"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:6JPK"
FT HELIX 199..211
FT /evidence="ECO:0007829|PDB:6JPK"
FT STRAND 215..221
FT /evidence="ECO:0007829|PDB:6JPK"
FT TURN 223..227
FT /evidence="ECO:0007829|PDB:6JPK"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:6JPK"
FT HELIX 235..241
FT /evidence="ECO:0007829|PDB:6JPK"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:6JPK"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:6JPK"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:6JPK"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:6JPK"
FT HELIX 274..289
FT /evidence="ECO:0007829|PDB:6JPK"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:6JPK"
FT HELIX 297..308
FT /evidence="ECO:0007829|PDB:6JPK"
FT HELIX 310..340
FT /evidence="ECO:0007829|PDB:6JPK"
FT HELIX 349..352
FT /evidence="ECO:0007829|PDB:6JPK"
FT STRAND 355..359
FT /evidence="ECO:0007829|PDB:6JPK"
FT HELIX 364..374
FT /evidence="ECO:0007829|PDB:6JPK"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:6JPK"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:6JPK"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:6JPK"
FT HELIX 394..407
FT /evidence="ECO:0007829|PDB:6JPK"
SQ SEQUENCE 409 AA; 46140 MW; 6CE10FFCC18D3E4A CRC64;
MSDYGFANIE EAKADAIFKL NAQYHQDEDP KKVNMSVGAY RDDTGKPWIL PAVKKASKIV
EEQASFNHEY LPIAGLPRFT KAAAEVLFRP NPHLLSEDRV ASMQSVSGTG ANFLAASFIE
TFYVKHTGAH VYISNPTWPV HRTLWEKLGV TVDTYPYWDA KNRSFDYEGM LSTIKSAPEG
SIFLLHACAH NPTGIDPTRE QWLSIFESLL SRKHLVVFDI AYQGFASGDL NRDSWALNEF
VKYNKDFFVC QSFAKNMGLY GERTGCMHYV AKDASTKNKV LSQLCIVQRN TISNPPAYGA
RIAAEILNSP QLFAEWEQDL KTMSSRIIEM RKRLRDSLVA LKTPGSWDHI TQQIGMFSFT
GLTPAQVQFC QERYHLYFSA NGRISMAGLN NSNVEHVAQA FNHAVRELP
