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Database: UniProt/SWISS-PROT
Entry: ALAM_DICDI
LinkDB: ALAM_DICDI
Original site: ALAM_DICDI 
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   28-MAR-2018, entry version 88.
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 (Slime mold).
OC   Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; 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.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   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.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- CATALYTIC ACTIVITY: L-alanine + 2-oxoglutarate = pyruvate + L-
CC       glutamate.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid degradation; L-alanine degradation via
CC       transaminase 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}.
DR   EMBL; AAFI02000082; EAL64484.1; -; Genomic_DNA.
DR   RefSeq; XP_637993.1; XM_632901.1.
DR   ProteinModelPortal; Q54MJ7; -.
DR   SMR; Q54MJ7; -.
DR   STRING; 44689.DDB0232139; -.
DR   PaxDb; Q54MJ7; -.
DR   EnsemblProtists; EAL64484; EAL64484; DDB_G0285899.
DR   GeneID; 8625344; -.
DR   KEGG; ddi:DDB_G0285899; -.
DR   dictyBase; DDB_G0285899; -.
DR   eggNOG; KOG0258; Eukaryota.
DR   eggNOG; COG0436; LUCA.
DR   InParanoid; Q54MJ7; -.
DR   KO; K00814; -.
DR   OMA; APGTEWV; -.
DR   PhylomeDB; Q54MJ7; -.
DR   Reactome; R-DDI-70614; Amino acid synthesis and interconversion (transamination).
DR   UniPathway; UPA00528; UER00586.
DR   PRO; PR:Q54MJ7; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   Proteomes; UP000002195; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
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   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Complete proteome; Mitochondrion;
KW   Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT   TRANSIT       1     18       Mitochondrion. {ECO:0000255}.
FT   CHAIN        19    534       Probable alanine aminotransferase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000328384.
FT   COMPBIAS     31     35       Poly-Thr.
FT   COMPBIAS     38     41       Poly-Asn.
FT   MOD_RES     352    352       N6-(pyridoxal phosphate)lysine.
FT                                {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
//
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