ID   ALAM_DICDI              Reviewed;         534 AA.
AC   Q54MJ7;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=Probable alanine aminotransferase, mitochondrial;
DE            Short=ALT;
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;
DE   Flags: Precursor;
GN   Name=gpt; ORFNames=DDB_G0285899;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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         Evidence={ECO:0000250};
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: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. Alanine aminotransferase subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000082; EAL64484.1; -; Genomic_DNA.
DR   RefSeq; XP_637993.1; XM_632901.1.
DR   AlphaFoldDB; Q54MJ7; -.
DR   SMR; Q54MJ7; -.
DR   STRING; 44689.Q54MJ7; -.
DR   PaxDb; 44689-DDB0232139; -.
DR   EnsemblProtists; EAL64484; EAL64484; DDB_G0285899.
DR   GeneID; 8625344; -.
DR   KEGG; ddi:DDB_G0285899; -.
DR   dictyBase; DDB_G0285899; -.
DR   eggNOG; KOG0258; Eukaryota.
DR   HOGENOM; CLU_014254_3_0_1; -.
DR   InParanoid; Q54MJ7; -.
DR   OMA; FGFECPP; -.
DR   PhylomeDB; Q54MJ7; -.
DR   Reactome; R-DDI-8964540; Alanine metabolism.
DR   UniPathway; UPA00528; UER00586.
DR   PRO; PR:Q54MJ7; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 1.10.287.1970; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; ALANINE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11751:SF29; ALANINE TRANSAMINASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Mitochondrion; Pyridoxal phosphate; Reference proteome;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..18
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..534
FT                   /note="Probable alanine aminotransferase, mitochondrial"
FT                   /id="PRO_0000328384"
FT   MOD_RES         352
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   534 AA;  59495 MW;  3C75A9FA6ACDA4C0 CRC64;
     MFKRSLKVLL SNPPINRVKP SSTIIQPLSN TTTTTIINNN NITNFEKMTH KKSMTIDNIC
     QNVRNAQYAV RGELVIRAEA ISHQLQKQKT EGTKTLPFEE IVYCNIGNPQ QLKQKPLTYF
     RQVVSLVECP DLLDNPYVEK IYPADVISRA KEILGSINNT TGAYSNSQGI GLVLRSVADF
     IERRDGHKSD PSEIFLTDGA SVGVQRILKL LIKDRSDGIL IPIPQYPLYS ATIELYNGSQ
     LGYLLNEEKG WSLEISQLEH SYNDAVSKGI NPRALVIINP GNPTGQCLDR ANMEEIVKFC
     LEKNVVLLAD EVYQENVYVK ESKPFISFKK VVKDMGGDYA DLEMVSFHSV SKGFVGECGK
     RGGYMELNGV TQDVKAEIYK LASIGLCPNV IGQLVVDLMV RPPVAGEQSH DLYLKERDNI
     YESLKKRANL LTNALNNLEG VTCNPSEGAM YAFPQIRLPA KAVEYANSIG KAPDAYYCIQ
     LLEATGICVV PGSGFGQKDG TWHFRTTFLP SEEAIEGVCK RIADFHQSFM NKYK
//