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Database: UniProt
Entry: A0A0V0U2V5_9BILA
LinkDB: A0A0V0U2V5_9BILA
Original site: A0A0V0U2V5_9BILA 
ID   A0A0V0U2V5_9BILA        Unreviewed;       475 AA.
AC   A0A0V0U2V5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Glutamate decarboxylase 1 {ECO:0000313|EMBL:KRX45592.1};
GN   Name=GAD1 {ECO:0000313|EMBL:KRX45592.1};
GN   ORFNames=T05_15633 {ECO:0000313|EMBL:KRX45592.1};
OS   Trichinella murrelli.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX45592.1, ECO:0000313|Proteomes:UP000055048};
RN   [1] {ECO:0000313|EMBL:KRX45592.1, ECO:0000313|Proteomes:UP000055048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS417 {ECO:0000313|EMBL:KRX45592.1};
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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:KRX45592.1}.
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DR   EMBL; JYDJ01000073; KRX45592.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0U2V5; -.
DR   Proteomes; UP000055048; Unassembled WGS sequence.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   CDD; cd06450; DOPA_deC_like; 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; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR45677:SF10; GLUTAMATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055048}.
FT   MOD_RES         288
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   475 AA;  54095 MW;  DD297853228C8A5D CRC64;
     MNTSKNRMIE ENQKLMENKF YNDILPLNRS GWLTTEMFIK AVVDLLLEFI KETNNPNTKV
     INFHHPTELI AKLDLRIPIN PTSLQKVIED CKEVLKYQVR TGHPRFFNQL STGLDLISMI
     GEWLTATVNT NIPGGAISNL YAVNAARHYM FPRCKAIGMV ETPNLAMFTS EDSHYSIRGA
     AALVGIGVDN CFPIPVDEKG KMIPSKLEEE VILAKKNGYV PFFVCAVGGT TVYGAFDPIN
     EIANICKKYR MWLHVDAAWG GGILLSKKHR HLANGIEKAD SVTWNPHKLM GALLQCSACL
     ICHEGLLFQC NQMCADYLFQ QDKPYDVSYD SGDKAIQCGR HNDVFKLWIM WRAKGMNGFE
     QQVNRLMELA KYFTEKIKKT PGYELIMENP EFLNICFWYV PKNVRHLEST EKKARLDKVA
     PKIKAKMMSS GSTMVGYQPD KDKPNFFRMI ISNPATTYED LDFFIEEIIR LGESL
//
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