ID E2AVJ9_CAMFO Unreviewed; 496 AA.
AC E2AVJ9;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Glutamate decarboxylase-like protein 1 {ECO:0000313|EMBL:EFN62550.1};
GN ORFNames=EAG_13865 {ECO:0000313|EMBL:EFN62550.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN62550.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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 EMBL; GL443122; EFN62550.1; -; Genomic_DNA.
DR RefSeq; XP_011264748.1; XM_011266446.2.
DR AlphaFoldDB; E2AVJ9; -.
DR STRING; 104421.E2AVJ9; -.
DR EnsemblMetazoa; XM_011266446.3; XP_011264748.1; LOC105256498.
DR GeneID; 105256498; -.
DR KEGG; cfo:105256498; -.
DR InParanoid; E2AVJ9; -.
DR OMA; QHEYSNV; -.
DR OrthoDB; 888358at2759; -.
DR Proteomes; UP000000311; 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 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:SF8; CYSTEINE SULFINIC ACID 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000311}.
FT MOD_RES 300
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 496 AA; 56939 MW; ED0C2AA626E93EC6 CRC64;
MAEPRTNNIT TMLENLLRIL KEEHVFNRSE DQRVIQFLHP KELQAKISFS LDKEPVKEEQ
LETLIRQVIR YSVKTNSLNF HNQLYGGIDE YGLMGSWLTE SLNTTQATYE IAPVFTMIEH
EVIKKSLELV GYPSMPHADG IMCPGGSMAN MYGLIMARYK MFPEIKKLGA SWLDKPLTCL
TSQDSHYSIL KAAHWLGIGT DNVYKVKTDK YGCMQADNLK EVIMQIKNKG HVPFFVNATA
GTTVLGAIDP LQEIAEICRR ENIWLHVDAC LGGTLLFSEK YRSRLRGIEL SNSVAWNCHK
MLGAPLQCSL FLVKGEKALY KANCSNADYL FQQDKFYDVS WDTGDKSVQC GRKVDAMKFW
LMWKARGTIG LGSLVDNAMR CVEYFLKRIR ETPGFRLVQS DYQLCTICFW YIPPKMRDQP
ETLNWWKQLY NITIEIKKYL TLRGSVMINY TPLLHKECGN FLRMVVTCQP PPTESSMDYV
IKEIEKVALE LDKSLS
//
