ID F9X9J3_ZYMTI Unreviewed; 511 AA.
AC F9X9J3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN ORFNames=MYCGRDRAFT_92510 {ECO:0000313|EMBL:EGP87937.1};
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP87937.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP87937.1, ECO:0000313|Proteomes:UP000008062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(2011).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Amino-acid degradation; L-alanine degradation via transaminase
CC pathway; pyruvate from L-alanine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00025708}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. Alanine aminotransferase subfamily.
CC {ECO:0000256|ARBA:ARBA00025785}.
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; CM001199; EGP87937.1; -; Genomic_DNA.
DR RefSeq; XP_003852961.1; XM_003852913.1.
DR AlphaFoldDB; F9X9J3; -.
DR STRING; 336722.F9X9J3; -.
DR EnsemblFungi; Mycgr3T92510; Mycgr3P92510; Mycgr3G92510.
DR GeneID; 13400415; -.
DR KEGG; ztr:MYCGRDRAFT_92510; -.
DR eggNOG; KOG0258; Eukaryota.
DR HOGENOM; CLU_014254_3_0_1; -.
DR InParanoid; F9X9J3; -.
DR OMA; FGFECPP; -.
DR OrthoDB; 5472891at2759; -.
DR UniPathway; UPA00528; UER00586.
DR Proteomes; UP000008062; Chromosome 4.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; 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 Reference proteome {ECO:0000313|Proteomes:UP000008062};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 122..493
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 511 AA; 56410 MW; DEA3B6DE48A55974 CRC64;
MSVAGVLSSV PLPTFVQKRL FTQNTPANRS LGIDNINPHV KEAKYAVRGE LAIKSEEYRA
QLAKGEGKDL PFDSVISANI GNPQQLDQKP ITFFRQVASL VENPLLLEHE DVLKNSLGYN
SDAIQRAQKL LKDVKSVGAY SQSQGAPGIR QSVAEFIERR DGFPADPANI YLCGGASAGV
NALMTVICSS PQTGILVPIP QYPLYTATLS LLNAQVVPYY LEEESNWSTN VDGMRTALKE
AQAKGIDVRA VVVINPGNPT GGSLESSNIK SVIELAAEEK LVVLADEVYQ TNVFEGEFNS
FKKCLRELQK SEKNKEGKFD NIEMASLHSI SKGMVGECGH RGGYYEMVGF DEKVVEQVYK
FVSIMLCPPV IGQCLVELMV NPPKEGEPSY AQYRKEYDTT FNNLKERANA LYHAFKEMEG
VECQEPQGSM YLYPTIKLPQ KAIEAAKEAG KSADEFYCLR LLDATGVCIV PGAGFGQKEG
TLHFRTTFLA PGTDWVKRIT KFHAEFLEKY R
//
