ID E3LY39_CAERE Unreviewed; 504 AA.
AC E3LY39;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN ORFNames=CRE_03967 {ECO:0000313|EMBL:EFO84597.1}, GCK72_001062
GN {ECO:0000313|EMBL:KAF1769247.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EFO84597.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|EMBL:EFO84597.1};
RG The Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF1769247.1, ECO:0000313|Proteomes:UP000483820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX506 {ECO:0000313|EMBL:KAF1769247.1,
RC ECO:0000313|Proteomes:UP000483820};
RC TISSUE=Whole organism {ECO:0000313|EMBL:KAF1769247.1};
RA Teterina A.A., Willis J.H., Phillips P.C.;
RT "Chromosome-level assembly of the Caenorhabditis remanei genome.";
RL Submitted (DEC-2019) 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}.
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DR EMBL; DS268418; EFO84597.1; -; Genomic_DNA.
DR EMBL; WUAV01000001; KAF1769247.1; -; Genomic_DNA.
DR RefSeq; XP_003111097.1; XM_003111049.1.
DR AlphaFoldDB; E3LY39; -.
DR STRING; 31234.E3LY39; -.
DR EnsemblMetazoa; CRE03967.1; CRE03967.1; WBGene00060597.
DR GeneID; 9801570; -.
DR KEGG; crq:GCK72_001062; -.
DR CTD; 9801570; -.
DR eggNOG; KOG0258; Eukaryota.
DR HOGENOM; CLU_014254_3_0_1; -.
DR InParanoid; E3LY39; -.
DR OMA; FGFECPP; -.
DR OrthoDB; 5472891at2759; -.
DR UniPathway; UPA00528; UER00586.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR Proteomes; UP000483820; Chromosome i.
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:UP000008281};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 109..478
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 504 AA; 55672 MW; 6318DFEB48333C77 CRC64;
MRTTQVLTGL VARRFFGTSS RIMASGKTLN VSNINPNVIK MEYAVRGPIV IRAVELEKEL
ANGAQKPFPN VIKANIGDAH AMGQKPITFI RQLLACIANP SLMETDKSLP ADVIEHANAF
LGSCGGKSAG AYSQSTGVEI VRKHVAEYIS RRDGGVPSNS EDICLSGGAS ESIRNVLKLF
INRNNAKKVG VMIPIPQYPL YSATIEEFGL GQVGYYLSES SNWSLDEAEL ERSFNDHSKE
YDIRVLCIIN PGNPTGQVLS RDNIETVIKF AQKKKLFILA DEVYQDNVYA QGSEFHSFKK
VLVEMGEPYS KLELASFHSV SKGYMGECGM RGGYVEFLNL DPEVYVLFKK MISAKLCSTV
LGQAVIDAVV NPPKEGEPSY SQWKKERDAV LASLKERATL VEKAYSSIDG ISCNPVQGAM
YAFPQITIPP KAVEKAQSRN QQPDFFYAME LLESTGICIV PGSGFGQKDG TYHFRTTILP
QPELFKDMLA RFTDFHAKFL AEYK
//
