ID C6KRK8_CAEEL Unreviewed; 403 AA.
AC C6KRK8;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 90.
DE SubName: Full=Aromatic amino acid beta-eliminating lyase/threonine aldolase domain-containing protein {ECO:0000313|EMBL:CAZ65516.1};
GN ORFNames=CELE_R102.4 {ECO:0000313|EMBL:CAZ65516.1}, R102.4
GN {ECO:0000313|EMBL:CAZ65516.1, ECO:0000313|WormBase:R102.4d};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CAZ65516.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CAZ65516.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAZ65516.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
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:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the threonine aldolase family.
CC {ECO:0000256|ARBA:ARBA00006966}.
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DR EMBL; BX284604; CAZ65516.1; -; Genomic_DNA.
DR RefSeq; NP_001255502.1; NM_001268573.1.
DR AlphaFoldDB; C6KRK8; -.
DR SMR; C6KRK8; -.
DR EPD; C6KRK8; -.
DR PeptideAtlas; C6KRK8; -.
DR EnsemblMetazoa; R102.4d.1; R102.4d.1; WBGene00011291.
DR EnsemblMetazoa; R102.4d.2; R102.4d.2; WBGene00011291.
DR EnsemblMetazoa; R102.4d.3; R102.4d.3; WBGene00011291.
DR GeneID; 177961; -.
DR AGR; WB:WBGene00011291; -.
DR WormBase; R102.4d; CE43916; WBGene00011291; -.
DR OrthoDB; 178754at2759; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00011291; Expressed in material anatomical entity and 5 other cell types or tissues.
DR ExpressionAtlas; C6KRK8; baseline and differential.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR InterPro; IPR023603; Low_specificity_L-TA-like.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; NF041359; GntG_guanitoxin; 1.
DR PANTHER; PTHR48097:SF9; L-THREONINE ALDOLASE; 1.
DR PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR Pfam; PF01212; Beta_elim_lyase; 2.
DR PIRSF; PIRSF017617; Thr_aldolase; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 1: Evidence at protein level;
KW Lyase {ECO:0000313|EMBL:CAZ65516.1};
KW Proteomics identification {ECO:0007829|EPD:C6KRK8,
KW ECO:0007829|PeptideAtlas:C6KRK8};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940}.
FT DOMAIN 38..160
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT DOMAIN 179..328
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 255
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 403 AA; 44478 MW; 28897BDC89C021B0 CRC64;
MTKVNGNSNG NGISASTDLL DTPSAYTQKS NKTHTSIDLR SDTVTVPSVE MRRAMAEAIV
GDDVYGEDTT TNRLEQRCAE LFGKEAGLFV TSGTMGNLLA IMAHCQRGEE IIVGRYNHIH
RWEQGNYAQF AGISATTLEV KPDGTMDLND IEQAIRVKGG YVQIKDESCD DLEVTSIPDC
HMPASKLICI ENTHNYTGGK ALPIEWMRSV KQLAERRDLK VHMDGARIYN AAVASNCSVS
KIASFADTVQ MCFSKGLGAP VGSIVVGPKD FIDRARHSRK ALGGGWRQSG ILAAAAHIAL
DHADATIRAD HERAKTLARM INDATPEEFR TKVFAAEKDI TNMVLVHCQN GVTVQQLTDF
FQKHDILAMT FDARRIRMVL NWNVSDENLE TIVEVYKKFL KQL
//
