ID A0A0V0RDD5_9BILA Unreviewed; 452 AA.
AC A0A0V0RDD5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
DE Flags: Fragment;
GN Name=GGAT2 {ECO:0000313|EMBL:KRX12400.1};
GN ORFNames=T07_12716 {ECO:0000313|EMBL:KRX12400.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX12400.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX12400.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX12400.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX12400.1}.
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DR EMBL; JYDL01000432; KRX12400.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0RDD5; -.
DR STRING; 6336.A0A0V0RDD5; -.
DR UniPathway; UPA00528; UER00586.
DR Proteomes; UP000054630; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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:SF373; ALANINE AMINOTRANSFERASE-RELATED; 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:KRX12400.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRX12400.1}.
FT DOMAIN 80..442
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX12400.1"
FT NON_TER 452
FT /evidence="ECO:0000313|EMBL:KRX12400.1"
SQ SEQUENCE 452 AA; 49593 MW; BEF1208F520465A3 CRC64;
LDYESLNENV KKVQYAVRGE LYLRASELQK EGKKIIFTNV GNPHALGQKP LTFPRQVVAL
CQAPFLLDDP NVGLLFPADA ISRAKHYLSV TSGGLGAYSD SRGIPAIRKE VAEFIEKRDG
YPSDPELIYL TDGASKGVMQ ILNAIIRGAG DGVLVPVPQY PLYSAAISLF GGSLVPYYLE
ETANWGLDVT DLRQSVITAR SKGITVRAMV IINPGNPTGQ CLSEANLREI INFCIQENLV
LLGDEVYQQN VYQDERPFIS ARKVLMGMGP FISKELQLVS FHTVSKGYWG ECGQRGGYFE
MTNIPPQTVD EIYKVASVAL SPNVPAQIFM GLMVNPPKPG DISYDQFARE SKGILESLRR
RAHLMTDGFN SCRNVVCNFT EGAMYSFPQI RLPPRAIQAA KSAGKVPDVF YCLKLLEATG
ISTVPGSGFG QKDGVFHLRT TILPAEEDMP AI
//
