ID   G4FKY1_9SYNE            Unreviewed;       478 AA.
AC   G4FKY1;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=Diaminobutyrate decarboxylase {ECO:0000313|EMBL:EHA63641.1};
DE            EC=4.1.1.86 {ECO:0000313|EMBL:EHA63641.1};
GN   ORFNames=Syn8016DRAFT_0682 {ECO:0000313|EMBL:EHA63641.1};
OS   Synechococcus sp. WH 8016.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=166318 {ECO:0000313|EMBL:EHA63641.1, ECO:0000313|Proteomes:UP000002752};
RN   [1] {ECO:0000313|EMBL:EHA63641.1, ECO:0000313|Proteomes:UP000002752}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8016 {ECO:0000313|Proteomes:UP000002752};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Palenik B., Woyke T.J.;
RT   "The draft genome of Synechococcus sp. WH 8016.";
RL   Submitted (SEP-2011) 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|RuleBase:RU000382}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHA63641.1}.
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DR   EMBL; AGIK01000001; EHA63641.1; -; Genomic_DNA.
DR   RefSeq; WP_006852823.1; NZ_AGIK01000001.1.
DR   AlphaFoldDB; G4FKY1; -.
DR   STRING; 166318.Syn8016DRAFT_0682; -.
DR   PATRIC; fig|166318.3.peg.756; -.
DR   eggNOG; COG0076; Bacteria.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000002752; Unassembled WGS sequence.
DR   GO; GO:0033983; F:diaminobutyrate decarboxylase activity; IEA:UniProtKB-EC.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 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; IPR015422; PyrdxlP-dep_Trfase_small.
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.
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         308
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   478 AA;  50948 MW;  0561ABA0FB7D0DC0 CRC64;
     MIIPHLVFLV GPSKNPEPVA LSAFASPDAL DPQLLQFLEG ASERLCNWIG SAAERGPLPA
     LRVLPDAAPQ THGRTMEQLL DDLQQVMDGA FQPSHPGAIA HLDPPPLSAS IAADLICAGL
     NNNLLAEELS PSLSHLERQL CAWFAERIGF PAGSSGVAAS GGTLSNLIAL VAARHHAGLD
     HTPDAVVVVS ADAHVSWHKA ARVMGLQNDA VREIPVDGQG RIDLQQLEDE LTALSREGRP
     CIAVVATAGT TVRGAIDPVS ALADLCSRLG RWLHVDGAIG AVFALSPTST HLLDGIARAD
     SITVNPQKVL GITKTSSLLL VRNPSVLAEA FSTGLPYMEP ALEHDHGGEL GLQGSRPAEV
     LKLWLGLRQL GESGIEQVLS AAIARREYLQ QQLDPNRLMI LSGPLHVLAC RPQRGQAQQH
     ESWSIETRRL LLSQGIMVSR PLHQGRHHLK AVLGNPHTHD GLLDQLASAL NQSVEVRP
//