ID   A2EMD3_TRIV3            Unreviewed;       496 AA.
AC   A2EMD3;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=TVAG_098820 {ECO:0000313|EMBL:EAY06171.1};
OS   Trichomonas vaginalis (strain ATCC PRA-98 / G3).
OC   Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae;
OC   Trichomonas.
OX   NCBI_TaxID=412133 {ECO:0000313|EMBL:EAY06171.1, ECO:0000313|Proteomes:UP000001542};
RN   [1] {ECO:0000313|EMBL:EAY06171.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=G3 {ECO:0000313|EMBL:EAY06171.1};
RA   Amadeo P., Zhao Q., Wortman J., Fraser-Liggett C., Carlton J.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EAY06171.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G3 {ECO:0000313|EMBL:EAY06171.1};
RX   PubMed=17218520; DOI=10.1126/science.1132894;
RA   Carlton J.M., Hirt R.P., Silva J.C., Delcher A.L., Schatz M., Zhao Q.,
RA   Wortman J.R., Bidwell S.L., Alsmark U.C.M., Besteiro S.,
RA   Sicheritz-Ponten T., Noel C.J., Dacks J.B., Foster P.G., Simillion C.,
RA   Van de Peer Y., Miranda-Saavedra D., Barton G.J., Westrop G.D., Mueller S.,
RA   Dessi D., Fiori P.L., Ren Q., Paulsen I., Zhang H., Bastida-Corcuera F.D.,
RA   Simoes-Barbosa A., Brown M.T., Hayes R.D., Mukherjee M., Okumura C.Y.,
RA   Schneider R., Smith A.J., Vanacova S., Villalvazo M., Haas B.J., Pertea M.,
RA   Feldblyum T.V., Utterback T.R., Shu C.L., Osoegawa K., de Jong P.J.,
RA   Hrdy I., Horvathova L., Zubacova Z., Dolezal P., Malik S.B.,
RA   Logsdon J.M. Jr., Henze K., Gupta A., Wang C.C., Dunne R.L., Upcroft J.A.,
RA   Upcroft P., White O., Salzberg S.L., Tang P., Chiu C.-H., Lee Y.-S.,
RA   Embley T.M., Coombs G.H., Mottram J.C., Tachezy J., Fraser-Liggett C.M.,
RA   Johnson P.J.;
RT   "Draft genome sequence of the sexually transmitted pathogen Trichomonas
RT   vaginalis.";
RL   Science 315:207-212(2007).
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}.
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DR   EMBL; DS113430; EAY06171.1; -; Genomic_DNA.
DR   RefSeq; XP_001318394.1; XM_001318359.1.
DR   AlphaFoldDB; A2EMD3; -.
DR   STRING; 5722.A2EMD3; -.
DR   GeneID; 4764035; -.
DR   KEGG; tva:TVAG_2v0100000; -.
DR   VEuPathDB; TrichDB:TVAG_098820; -.
DR   VEuPathDB; TrichDB:TVAGG3_0100000; -.
DR   eggNOG; KOG0258; Eukaryota.
DR   InParanoid; A2EMD3; -.
DR   OMA; ESNEWAL; -.
DR   UniPathway; UPA00528; UER00586.
DR   Proteomes; UP000001542; Unassembled WGS sequence.
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 {ECO:0000313|EMBL:EAY06171.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001542};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          121..484
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   496 AA;  55866 MW;  90BCDAC4F4A6192B CRC64;
     MLSNASSFAK NFALPNPSYG SRRPININSI NQQLIQSQYG VRGHLNTIAD QFMKRIRSGE
     KMPFKDLIQC SIGNPFAVGK SPLSFTRQVV ACIEDRSLLN LPQMPAEVKD RVNVILNSMA
     CEFGGYTKSA GIDIVRQHVA EFINKRDGYP TKPDDIFLSS GVIDAIVFLL TLLINNDNVG
     IMMPFPTYPI YASETILRHG KVVPFYLKES DDWSIDLFDL QQSYTEATKQ GIDIRAMVIV
     NPCNPTGRVL SAQDMRTIIE FCDQNKICII ADEVYQDCVY NSAKPFISFK KMVSQVKSDV
     QLISLHSISK GFMGECGHRG GYMELYHFPI DVKEQISKMS TYSLCPNTVG QVILDTMVHP
     PESDECKSIW DQQKASYIEN LKVKSEELYE CLNKLPGIST KKADGGWYLF PSLKLPLKAL
     EAAKSCRIGR KVQPPDFFWC LKLLEETGVQ MNPGSGFGQV PGTSHFRSTF LAEGKMFDEA
     LERITEFQNN FMKKYD
//