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Database: UniProt/TrEMBL
Entry: P73043_SYNY3
LinkDB: P73043_SYNY3
Original site: P73043_SYNY3 
ID   P73043_SYNY3            Unreviewed;       467 AA.
AC   P73043;
DT   01-FEB-1997, integrated into UniProtKB/TrEMBL.
DT   01-FEB-1997, sequence version 1.
DT   25-OCT-2017, entry version 111.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   Name=gad {ECO:0000313|EMBL:BAA17064.1};
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708 {ECO:0000313|EMBL:BAA17064.1, ECO:0000313|Proteomes:UP000001425};
RN   [1] {ECO:0000313|EMBL:BAA17064.1, ECO:0000313|Proteomes:UP000001425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa {ECO:0000313|Proteomes:UP000001425};
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T.,
RA   Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S.,
RA   Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M.,
RA   Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the
RT   entire genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC       {ECO:0000256|RuleBase:RU361171}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         ECO:0000256|RuleBase:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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DR   EMBL; BA000022; BAA17064.1; -; Genomic_DNA.
DR   PIR; S75150; S75150.
DR   ProteinModelPortal; P73043; -.
DR   STRING; 1148.SYNGTS_0488; -.
DR   EnsemblBacteria; BAA17064; BAA17064; BAA17064.
DR   KEGG; syn:sll1641; -.
DR   HOGENOM; HOG000070228; -.
DR   InParanoid; P73043; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   PhylomeDB; P73043; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006536; P:glutamate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR010107; Glutamate_decarboxylase.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001425};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001425}.
FT   MOD_RES     279    279       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   467 AA;  53041 MW;  7C0BDFA030743153 CRC64;
     MVHKKIDLNQ LSEAESLLTP TYAARGLANS VSKYEMPETE MLPAIAYNLI HDELGLDGNS
     RLNLATFVTT WMEPEARQLM ADTFDKNMID KDEYPQTAEI ELRCVNILSR LWNAPASAEA
     TGCSTIGSSE AAMLGGMAMK WKWRQRRQAA GKPGDRPNLV MGINVQVCWE KFCRYWEVEP
     RFVPMEGDRY HISPEEAVKL IDENTIGVIG ILGSTFDGSY EPIEALNDAL ETLNQRTGWQ
     VPLHIDAASG GFIAPFLDPD LRWDFRLPWV KSINTSGHKY GLVYPGVGWI IWRDKEELPE
     ELIFHCNYLG GDLPNFALNF SRPGNQVVAQ YYNFLRLGKE GYRKIQQTCR DTALYLSGKI
     AQLGPFELLT DGGDIPVFAW RLKDEVLANT CYTLYDMADK LRERGWLVPA YRMPKNREDL
     VVQRIVVKEG FSRDMADLLL ADMERAIAYF ASQPDHKPKQ EGSHFSH
//
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