ID T1KFR8_TETUR Unreviewed; 484 AA.
AC T1KFR8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN Name=107363404 {ECO:0000313|EnsemblMetazoa:tetur10g04110.1};
OS Tetranychus urticae (Two-spotted spider mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC Tetranychoidea; Tetranychidae; Tetranychus.
OX NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur10g04110.1, ECO:0000313|Proteomes:UP000015104};
RN [1] {ECO:0000313|Proteomes:UP000015104}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA Rombauts S.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:tetur10g04110.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-alanine = L-glutamate + pyruvate;
CC Xref=Rhea:RHEA:19453, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57972; EC=2.6.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00024611};
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; CAEY01000038; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015786109.1; XM_015930623.1.
DR AlphaFoldDB; T1KFR8; -.
DR STRING; 32264.T1KFR8; -.
DR EnsemblMetazoa; tetur10g04110.1; tetur10g04110.1; tetur10g04110.
DR GeneID; 107363404; -.
DR KEGG; tut:107363404; -.
DR eggNOG; KOG0258; Eukaryota.
DR HOGENOM; CLU_014254_3_0_1; -.
DR OMA; IGDPNLF; -.
DR OrthoDB; 5472891at2759; -.
DR UniPathway; UPA00528; UER00586.
DR Proteomes; UP000015104; Unassembled WGS sequence.
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:UP000015104};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 109..471
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 484 AA; 53598 MW; 5A19195EC5E176C8 CRC64;
MSTQSGESSH VLDLDSVNQN VKKMEYAVRG PLVIRAGEIE KELKAGKNDK PFNGVIRANI
GDCHATGQKP LTFIRQVIAC CTDTTLLDDP KYPKDVKEKV KLLLSYCGGN SVGSYSDSAG
IEIIRRHCAE YIAERDGIPS NWQDIVLTNG ASEAVKFVLA LINSSSTDDK PTGVLIPIPQ
YPLYTATLAE YAMHPIKYYL DEGNEWKLNI AELKRALDND RSLCRPKAIV IINPGNPTGS
VLNKENIKEI INFAKEEKLI IIADEVYQHN VYKEGAAFHS FKKVMHELGI NLELASLMSS
SKGFMGECGL RGGYCEFINL KPEIKALFLK MLSARLCCSI LGQITMDCVV APPKPGDPSY
DLFTSEKNST LESLKAKAKL AAETFNSIPG MKSNPVAGAM YAFPQIMLPE KAIKEARDAG
VEPDFFYAKN LLETTGICIV PGSGFGQIPG TYHFRTTILP QFEELKKMMD RLKTFHLQFL
EKYK
//