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Database: UniProt
Entry: A0A182UYD2_ANOME
LinkDB: A0A182UYD2_ANOME
Original site: A0A182UYD2_ANOME 
ID   A0A182UYD2_ANOME        Unreviewed;       512 AA.
AC   A0A182UYD2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Glutamate decarboxylase {ECO:0008006|Google:ProtNLM};
OS   Anopheles merus (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=30066 {ECO:0000313|EnsemblMetazoa:AMEM005773-PA, ECO:0000313|Proteomes:UP000075903};
RN   [1] {ECO:0000313|EnsemblMetazoa:AMEM005773-PA, ECO:0000313|Proteomes:UP000075903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAF {ECO:0000313|EnsemblMetazoa:AMEM005773-PA,
RC   ECO:0000313|Proteomes:UP000075903};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles merus MAF (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AMEM005773-PA}
RP   IDENTIFICATION.
RC   STRAIN=MAF {ECO:0000313|EnsemblMetazoa:AMEM005773-PA};
RG   VectorBase;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [3] {ECO:0000313|EnsemblMetazoa:AMEM005773-PA}
RP   IDENTIFICATION.
RC   STRAIN=MAF {ECO:0000313|EnsemblMetazoa:AMEM005773-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAR-2023) to UniProtKB.
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|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR   AlphaFoldDB; A0A182UYD2; -.
DR   STRING; 30066.A0A182UYD2; -.
DR   EnsemblMetazoa; AMEM005773-RA; AMEM005773-PA; AMEM005773.
DR   VEuPathDB; VectorBase:AMEM005773; -.
DR   VEuPathDB; VectorBase:AMEM21_011656; -.
DR   OrthoDB; 888358at2759; -.
DR   Proteomes; UP000075903; Unassembled WGS sequence.
DR   GO; GO:0016831; F:carboxy-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; 3.90.1150.170; -; 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; IPR021115; Pyridoxal-P_BS.
DR   PANTHER; PTHR45677:SF10; GLUTAMATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 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}.
FT   MOD_RES         324
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   512 AA;  58097 MW;  6953EA85F78A2081 CRC64;
     MTSINVEKYK LSDKTAKLTA KDIIPVVQSS DSAETREFLN KIAELLVDYV NIQNDRKEKI
     LDFHHPEDMK KLLTLDIPED AVTLQQLVKD CAMTLKYQVK TGHPHFFNQL SCGLDVVSMA
     GEWLTATANT NMFTYEIAPV FILMENVVLS KMRKIIGWDG GDSILAPGGS ISNLYAFLAA
     RHKMFPNYKE HGARALPGEL VMFTSDQCHY SVKSCAAVCG LGTDNCVMVP SDEHGRLIPA
     ELERLILERK ARGQIPFFVN ATAGTTVLGA FDPINAVADI CEKYNCWFHV DAAWGGGLLL
     SKKYRHPRFT GIERCDSITW NPHKLMGALL QCSTIHFKED GLLISCNQMS AEYLFMTDKL
     YDISYDTGDK VIQCGRHNDI FKLWLQWRSK GTEGFGKHMD HLMELAEYEV KRIKQQSDKF
     YLIMEPECVN VSFWYIPKRL RGVPHDAKKE QELAKICPII KSRMMMSGTL MVGYQPDDRR
     PNFFRSIISS IAVTEADVDF MLNEIDRLGQ DL
//
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