ID   T1DLB3_ANOAQ            Unreviewed;       417 AA.
AC   T1DLB3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Putative alanine--glyoxylate aminotransferase 2 mitochondrial {ECO:0000313|EMBL:JAB01050.1};
DE   Flags: Fragment;
OS   Anopheles aquasalis (Malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=42839 {ECO:0000313|EMBL:JAB01050.1};
RN   [1] {ECO:0000313|EMBL:JAB01050.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Whole body {ECO:0000313|EMBL:JAB01050.1};
RG   Brazilian Malaria Network (MCT/CNPq/MS/SCTIE/DECIT/PRONEX 555648/2009-5) and Research Network on Bioactive Molecules from Arthropod Vectors (NAP-MOBIARVE;
RG   University of Sao Paulo);
RA   Marinotti O., Ribeiro J.M.C., Costa-da-Silva A.L., Silva M.C.P.,
RA   Lopes A.R., Barros M.S., Sa-Nunes A., Konjin B.B., Carvalho E., Suesdek L.,
RA   Silva-Neto M.A.C., Capurro M.L.;
RT   "Transcriptome sequencing and developmental regulation of gene expression
RT   in Anopheles aquasalis.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; GAMD01000541; JAB01050.1; -; mRNA.
DR   AlphaFoldDB; T1DLB3; -.
DR   VEuPathDB; VectorBase:AAQUA_004969; -.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_like; 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; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 3.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   2: Evidence at transcript level;
KW   Aminotransferase {ECO:0000313|EMBL:JAB01050.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:JAB01050.1}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:JAB01050.1"
SQ   SEQUENCE   417 AA;  45756 MW;  71410A3582319333 CRC64;
     KRYLDMFGGI VTVSVGHCHP KVNAALKEQV DTLWHTTNIY MHPKVHEYAE KLVAKMPGDL
     KNVYFVNSGS EANDLAMMMA RLYTGHNDII SFRNAYHGAS PYTMGLTAHS TWRYPLPGVA
     NGIHHVMNPD PYTGLWGGNN CRDSPVQTTR HCDCSGKTGQ DCCAATMYYE QLEQTFKYSL
     PRGKVAAMFA ESIQGVGGTV QYPKGYLKRA ADLVRANGGL FVADEVQSGF GRTGEHYWGF
     EGHGVMPDIV TMAKGIGNGF PIGAVITSRK VAEVLSQALH FNTFGGNPLA SAVGMAVLDV
     IDEEELQKNS LEVGTYMLKG LERLRDKHDV IGDVRGKGLM IGVELVADKD TRQHLSAPHF
     VDIWEMCKDM GVLFGRGGLN ANVLRIKPPM CLTNADVDFA LHVLDQALEK HPANKEL
//