ID   A2E7I0_TRIV3            Unreviewed;       494 AA.
AC   A2E7I0;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=TVAG_379550 {ECO:0000313|EMBL:EAY11373.1};
OS   Trichomonas vaginalis (strain ATCC PRA-98 / G3).
OC   Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae;
OC   Trichomonas.
OX   NCBI_TaxID=412133 {ECO:0000313|EMBL:EAY11373.1, ECO:0000313|Proteomes:UP000001542};
RN   [1] {ECO:0000313|EMBL:EAY11373.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=G3 {ECO:0000313|EMBL:EAY11373.1};
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:EAY11373.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G3 {ECO:0000313|EMBL:EAY11373.1};
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; DS113320; EAY11373.1; -; Genomic_DNA.
DR   RefSeq; XP_001323596.1; XM_001323561.1.
DR   AlphaFoldDB; A2E7I0; -.
DR   STRING; 5722.A2E7I0; -.
DR   GeneID; 4769326; -.
DR   KEGG; tva:TVAG_2v0339620; -.
DR   VEuPathDB; TrichDB:TVAG_379550; -.
DR   VEuPathDB; TrichDB:TVAGG3_0339620; -.
DR   eggNOG; KOG0258; Eukaryota.
DR   InParanoid; A2E7I0; -.
DR   OMA; MMMQILI; -.
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:EAY11373.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001542};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          99..482
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   494 AA;  55742 MW;  1307CFF5CCFE723A CRC64;
     MSLKTISRLF AYSPRYLQNA RALNINTVNK EVVKSSYSIR GHLNTVSDQL RKRMAAGEKL
     PFDSIIPCNI GNPLAVGKDP LTFPRDVVSC IENTKLLNSA DISEEAKDRA KQIIASTGGR
     FGGYTKSQGI EIVRQHIAEF MYKRDGYPCK PDDIYLSDGA SSAISFLMTL LIQHNNVGIM
     TPFPTYPVYT SEAAVHGGKI VPFYLRESNN WSLDIEELVR AYNLAIKEGI DVRCMVIINP
     CNPTGHVLRP ETMRTIVDFC EQNNILLIAD EVYQDVVYNK ERPFYSFKKI ASQMKSNIQL
     VSLHSISKGF MGECGHRGGY FELYHFPEDV KAQIFKMATF GLCPNAVGQV IVDCMVHPPE
     APENKAIWES ERNSYITKLQ QKSVKLAECF NSLPGIKCKP ADGGWYLFPA LSLPLKALEA
     AKSCRWQREV MPPDFFWCLK LLEETGVIVV PGSGFGQVPG TFHFRSTFLP EDEKFDQVIE
     RITKFQNEFM TKYD
//