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
//