AATM_SCHPO
ID AATM_SCHPO Reviewed; 437 AA.
AC O94320;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Aspartate aminotransferase, mitochondrial;
DE EC=2.6.1.1;
DE AltName: Full=Transaminase A;
DE Flags: Precursor;
GN ORFNames=SPBC725.01;
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:CAA22173.1}
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. Important for
CC metabolite exchange between mitochondria and cytosol (By similarity).
CC {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:Q01802};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q01802};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q01802}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {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; CU329671; CAA22173.1; -; Genomic_DNA.
DR PIR; T40653; T40653.
DR RefSeq; NP_595481.1; NM_001021392.2.
DR AlphaFoldDB; O94320; -.
DR SMR; O94320; -.
DR BioGRID; 277700; 48.
DR STRING; 4896.SPBC725.01.1; -.
DR MaxQB; O94320; -.
DR PaxDb; O94320; -.
DR PRIDE; O94320; -.
DR EnsemblFungi; SPBC725.01.1; SPBC725.01.1:pep; SPBC725.01.
DR GeneID; 2541186; -.
DR KEGG; spo:SPBC725.01; -.
DR PomBase; SPBC725.01; -.
DR VEuPathDB; FungiDB:SPBC725.01; -.
DR eggNOG; KOG1411; Eukaryota.
DR HOGENOM; CLU_032440_1_0_1; -.
DR InParanoid; O94320; -.
DR OMA; VGACTIV; -.
DR PhylomeDB; O94320; -.
DR Reactome; R-SPO-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-SPO-70263; Gluconeogenesis.
DR Reactome; R-SPO-8963693; Aspartate and asparagine metabolism.
DR Reactome; R-SPO-8964539; Glutamate and glutamine metabolism.
DR PRO; PR:O94320; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:PomBase.
DR GO; GO:0005739; C:mitochondrion; 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:0019266; P:asparagine biosynthetic process from oxaloacetate; ISS:PomBase.
DR GO; GO:0006532; P:aspartate biosynthetic process; ISS:PomBase.
DR GO; GO:0006533; P:aspartate catabolic process; ISS:PomBase.
DR GO; GO:0006531; P:aspartate metabolic process; ISS:UniProtKB.
DR GO; GO:0006534; P:cysteine metabolic process; NAS:PomBase.
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 3: Inferred from homology;
KW Aminotransferase; Mitochondrion; Pyridoxal phosphate; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q01802, ECO:0000305"
FT CHAIN ?..437
FT /note="Aspartate aminotransferase, mitochondrial"
FT /id="PRO_0000309452"
FT BINDING 72
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 413
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT MOD_RES 284
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 437 AA; 48243 MW; 991D245BB1047A63 CRC64;
MLARNLRCLH PNTFASLKTN VSYHGVKCLA SQSKRGFKVW ADVPMGPPDP IFGITEAYKK
DGDVKKMNLG AGTYRDDAGK PYVLPSVRQA ETELLSQKLD KEYAPITGIP SFRVQATKLA
YGDVYESIKD RLVSAQSISG TGALCIAANF LASFYPSKTI YVSDPTWGNH KNVFSRAGLT
VKSYKYYDPA TRGLDIKGML SDLTSAPDGS IILLHACAHN PTGVDPTKAQ WDDILKTMQK
KNHFALLDMA YQGFASGDFA RDAYATRLFA SSNVPMLLCQ SFAKNMGLYG ERAGCFSILA
NDAEEAARIE SQTKILIRAL YSNPPVNGAR IANHILSNPA LREQWAGEVV GMSERLKSMR
KALRNILEKD LKNKHSWKHI TDQIGMFCYT GLNPQQVDVL AKQYHIYLTK NGRISISGLN
TSNVRYFAEA INAVTSN
