ID   K9S6P9_9CYAN            Unreviewed;       511 AA.
AC   K9S6P9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=L-2,4-diaminobutyrate decarboxylase {ECO:0000313|EMBL:AFY66282.1};
DE            EC=4.1.1.86 {ECO:0000313|EMBL:AFY66282.1};
GN   ORFNames=GEI7407_1798 {ECO:0000313|EMBL:AFY66282.1};
OS   Geitlerinema sp. PCC 7407.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Geitlerinematales;
OC   Geitlerinemataceae; Geitlerinema.
OX   NCBI_TaxID=1173025 {ECO:0000313|EMBL:AFY66282.1, ECO:0000313|Proteomes:UP000010383};
RN   [1] {ECO:0000313|EMBL:AFY66282.1, ECO:0000313|Proteomes:UP000010383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7407 {ECO:0000313|EMBL:AFY66282.1,
RC   ECO:0000313|Proteomes:UP000010383};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished genome of Geitlerinema sp. PCC 7407.";
RL   Submitted (MAY-2012) 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}.
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DR   EMBL; CP003591; AFY66282.1; -; Genomic_DNA.
DR   RefSeq; WP_015171848.1; NC_019703.1.
DR   AlphaFoldDB; K9S6P9; -.
DR   STRING; 1173025.GEI7407_1798; -.
DR   KEGG; gei:GEI7407_1798; -.
DR   PATRIC; fig|1173025.3.peg.2021; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_011856_0_4_3; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000010383; Chromosome.
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   CDD; cd06450; DOPA_deC_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 1.20.1650.10; PLP-dependent transferases; 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   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:UP000010383}.
FT   MOD_RES         324
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   511 AA;  56357 MW;  6F5CD18122AABCCE CRC64;
     MLLDTLSQTS GTTSPFDRYF LSAEPESLAA YQEAIALAQQ VLLDDVRNHP QPYSGQDPRA
     LEQAIGDRFS DPFFEQNLQQ ILINVGEKIL SSSVRVAEPT CMAHLHCPPL IPALAAEVLV
     NATNQSMDSW DQSPSATILE QRLVTWLCKI YGYGAQADGV FTSGGTQSNF MGLLLARDRA
     CRDRLGWSVQ QQGLPPEARR FRILCSEVAH FTIRQGASLL GLGEQAVVPV KTDAAFRMCP
     QDAAEKLAEL RCQDLWPIAL VATAGTTDFG SIDPLEPLAA IAREAGLWFH VDAAFGGALI
     LSDRHRPKLA GIDAADSLTV DFHKLFYQPI SCGAFLVRDR AAFELMRVHA DYLNPEGNEA
     QGIPDLVTKS VQTTRRFDAL KLWVSLQAVG RQTFGEMIDT TITTAHQAAQ AIDAAPDLEL
     VNWPEINAVV FRYAPPALRQ DPAARDRLNQ INREVRWALL RQGRAVIAQT QIGDRVYLKF
     TLLNPRTTLA HLTDLLQEIQ RLGTTLEISH G
//