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
//