ALAT_SCHPO
ID ALAT_SCHPO Reviewed; 505 AA.
AC Q10334;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Putative alanine aminotransferase;
DE EC=2.6.1.2;
DE AltName: Full=Glutamate pyruvate transaminase;
DE Short=GPT;
DE AltName: Full=Glutamic--alanine transaminase;
DE AltName: Full=Glutamic--pyruvic transaminase;
GN ORFNames=SPBC582.08;
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]
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-alanine = L-glutamate + pyruvate;
CC Xref=Rhea:RHEA:19453, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57972; EC=2.6.1.2;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- PATHWAY: Amino-acid degradation; L-alanine degradation via transaminase
CC pathway; pyruvate from L-alanine: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. Alanine aminotransferase subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329671; CAB46671.1; -; Genomic_DNA.
DR PIR; T37975; T37975.
DR RefSeq; NP_595176.1; NM_001021084.2.
DR AlphaFoldDB; Q10334; -.
DR SMR; Q10334; -.
DR BioGRID; 277407; 15.
DR STRING; 4896.SPBC582.08.1; -.
DR MaxQB; Q10334; -.
DR PaxDb; Q10334; -.
DR EnsemblFungi; SPBC582.08.1; SPBC582.08.1:pep; SPBC582.08.
DR GeneID; 2540891; -.
DR KEGG; spo:SPBC582.08; -.
DR PomBase; SPBC582.08; -.
DR VEuPathDB; FungiDB:SPBC582.08; -.
DR eggNOG; KOG0258; Eukaryota.
DR HOGENOM; CLU_014254_3_0_1; -.
DR InParanoid; Q10334; -.
DR OMA; FGFECPP; -.
DR PhylomeDB; Q10334; -.
DR Reactome; R-SPO-8964540; Alanine metabolism.
DR UniPathway; UPA00528; UER00586.
DR PRO; PR:Q10334; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; ISS:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; ISS:PomBase.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0097054; P:L-glutamate biosynthetic process; IC:PomBase.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR045088; ALAT1/2-like.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11751; PTHR11751; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..505
FT /note="Putative alanine aminotransferase"
FT /id="PRO_0000123938"
FT MOD_RES 326
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 505 AA; 56628 MW; 6F6A0756A0458FAC CRC64;
MFTDYPNDIN CESPRMSDLD GFCQNAFSDL NSLNQQVFKA NYAVRGALAI LADEIQDDLL
ENPSSYPFSE IVYANIGNPQ QMGQSPITFV RQVLSLCQYP TLLDHAEEKW FQNLFPTDVV
QRSKMLLKES GSLGAYSASQ GIPLVRRHVA DFIRARDGFD CEPSDIYLTS GASHAARLIM
TLIIARPTDG VMVPAPQYPL YGAQIDLMSG SMVSYSLSEE NNWDIDFDQF KKSFDEASKK
GINVRLCVVI NPGNPTGACI SENSMEKVLR FAKAKGIVLL ADEVYQNNIY QNKFHSFRRK
LGELREKEPD NHWDQVSLIS VNSVSKGQFG ECGQRGGYLD VVNIPEPAKD QILKLATIDI
CPPVAGQLLV DMLVNPPKPG DPSYDLFIKE VDEIHEALRL QCRQLYEGTK RMKRVSCLEP
HGAMYLHPSV SLPEKLITTA KAQKIQPDEF YAIELLKRSG ICVVPGSGFG QPEGDYHIRI
TFLAKGTEYI ERFVKAHNEI MDLYE
