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Database: UniProt
Entry: A0A195B5L8_9HYME
LinkDB: A0A195B5L8_9HYME
Original site: A0A195B5L8_9HYME 
ID   A0A195B5L8_9HYME        Unreviewed;       506 AA.
AC   A0A195B5L8;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Cysteine sulfinic acid decarboxylase {ECO:0000313|EMBL:KYM79565.1};
GN   ORFNames=ALC53_10004 {ECO:0000313|EMBL:KYM79565.1};
OS   Atta colombica.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Atta.
OX   NCBI_TaxID=520822 {ECO:0000313|EMBL:KYM79565.1, ECO:0000313|Proteomes:UP000078540};
RN   [1] {ECO:0000313|EMBL:KYM79565.1, ECO:0000313|Proteomes:UP000078540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Treedump-2 {ECO:0000313|EMBL:KYM79565.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYM79565.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Atta colombica WGS genome.";
RL   Submitted (SEP-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|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; KQ976598; KYM79565.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A195B5L8; -.
DR   STRING; 520822.A0A195B5L8; -.
DR   Proteomes; UP000078540; 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:UP000078540}.
FT   MOD_RES         315
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   506 AA;  57705 MW;  140429484100A4E0 CRC64;
     MEGAKQACRL VGWPVSILFA MAASSTNNII DLLERLLKIL KEENAFNRSD DQPVIRFRHP
     HYLQKIIPMS LDDKPASNRE IETVIRQTIQ YSVKTSSPHF HNQLYAGVDE YGLIGSWLTD
     VLNTSQYTYE VAPVFTLMER EVIQKSLELV GYPLMPEADG IMCPGGSISN MYGMLLARHK
     IFPCIKKSGI FSLKSPLVCF TSEDSHYSIL KSANWLGLGI DHVYKVKTDE FGRMQVADLK
     RLLIKARNDG KQPFFVNATA GTTVLGAIDP LPEIAAVCRN SLQACLGGTL LFSEKYRYRL
     RGIELSDSVS WNLHKMLGAP LQCSLFLVKD KNMLHEVNCA QAKYLFQQDK FYDVSWDTGD
     KSVQCGRKVD AMKFWLMWKA RGKIGLTRSV EQAMSCAEYF LKRIKETAGF RLVQSHYQCC
     NICFWYVPPT MRDESETPIW WQKLYFLTNE IKKRLVLGGS LMISYMPIPH KEIGNFFRMV
     VNCQPPPTKS SMDYVINQIE KVAIDL
//
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