AGT2L_CAEEL
ID AGT2L_CAEEL Reviewed; 467 AA.
AC P91408;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Ethanolamine-phosphate phospho-lyase homolog 1 {ECO:0000312|WormBase:T01B11.2a};
DE EC=4.2.3.- {ECO:0000305};
DE AltName: Full=Alanine--glyoxylate aminotransferase 2-like {ECO:0000250|UniProtKB:Q8TBG4};
GN Name=eppl-1 {ECO:0000312|WormBase:T01B11.2a};
GN ORFNames=T01B11.2 {ECO:0000312|WormBase:T01B11.2a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q8TBG4};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- CAUTION: Does not seem to possess aminotransferase activity.
CC {ECO:0000250|UniProtKB:Q8TBG4}.
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DR EMBL; BX284604; CCD65920.1; -; Genomic_DNA.
DR PIR; T25848; T25848.
DR RefSeq; NP_001023346.1; NM_001028175.4.
DR AlphaFoldDB; P91408; -.
DR SMR; P91408; -.
DR BioGRID; 42758; 2.
DR DIP; DIP-24370N; -.
DR STRING; 6239.T01B11.2a.1; -.
DR EPD; P91408; -.
DR PaxDb; P91408; -.
DR PeptideAtlas; P91408; -.
DR EnsemblMetazoa; T01B11.2a.1; T01B11.2a.1; WBGene00020139.
DR GeneID; 177646; -.
DR KEGG; cel:CELE_T01B11.2; -.
DR UCSC; T01B11.2a.1; c. elegans.
DR CTD; 177646; -.
DR WormBase; T01B11.2a; CE12894; WBGene00020139; eppl-1.
DR eggNOG; KOG1403; Eukaryota.
DR GeneTree; ENSGT00940000171040; -.
DR HOGENOM; CLU_016922_8_0_1; -.
DR InParanoid; P91408; -.
DR OMA; MVPNYNP; -.
DR OrthoDB; 145181at2759; -.
DR PhylomeDB; P91408; -.
DR Reactome; R-CEL-1442490; Collagen degradation.
DR Reactome; R-CEL-1483213; Synthesis of PE.
DR Reactome; R-CEL-71064; Lysine catabolism.
DR PRO; PR:P91408; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00020139; Expressed in larva and 4 other tissues.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..467
FT /note="Ethanolamine-phosphate phospho-lyase homolog 1"
FT /id="PRO_0000120541"
FT MOD_RES 307
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 467 AA; 51645 MW; E5425970A6F73361 CRC64;
MSTLVNALGF FTSSTPAAAA TKDVRSKEEI LKRRKDTIGS KCQIFYSDDP FMVSRASMQY
LYDEKSNKFL DCISNVQHVG HCHPKVVEAI SKQLATSTCN VRFVSTQLTD CAEQILSTLP
GLDTVLFCNS GSEANDLALR LARDYTKHKD AIVIEHAYHG HVTTTMELSP YKFDHGSTVS
QPDWVHVAPC PDVFRGKHRL ADNELTNEDK LYAAGKQYSD DVKSILNDVE SRQCGVAAYF
AEALQSCGGQ VIPPKDYFKD VATHVRNHGG LMIIDEVQTG FGRIGRKYWA HQLYDDGFLP
DIVTMGKPMG NGFPVSAVAT RKEIADALGG EVGYFNTYGG NPVACAAVIS VMKVVKDENL
LEHSQQMGEK LEVALRDLQK KHECIGDIRG VGLFWGIDLV KDRNTREPDQ KLAIATILAL
RKSYGILLNA DGPHTNILKI KPPLCFNENN ILETVTALDQ VLTLMNR