ID G7ECK7_9GAMM Unreviewed; 541 AA.
AC G7ECK7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:GAA58630.1};
DE EC=4.1.1.15 {ECO:0000313|EMBL:GAA58630.1};
GN ORFNames=P20652_0487 {ECO:0000313|EMBL:GAA58630.1};
OS Pseudoalteromonas sp. BSi20652.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=388384 {ECO:0000313|EMBL:GAA58630.1, ECO:0000313|Proteomes:UP000005499};
RN [1] {ECO:0000313|Proteomes:UP000005499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bsi20652 {ECO:0000313|Proteomes:UP000005499};
RX PubMed=22275105; DOI=10.1128/JB.06427-11;
RA Bian F., Xie B.B., Qin Q.L., Shu Y.L., Zhang X.Y., Yu Y., Chen B.,
RA Chen X.L., Zhou B.C., Zhang Y.Z.;
RT "Genome sequences of six Pseudoalteromonas strains isolated from Arctic sea
RT ice.";
RL J. Bacteriol. 194:908-909(2012).
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:GAA58630.1}.
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DR EMBL; BADT01000032; GAA58630.1; -; Genomic_DNA.
DR RefSeq; WP_008166163.1; NZ_BADT01000032.1.
DR AlphaFoldDB; G7ECK7; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000005499; Unassembled WGS sequence.
DR GO; GO:0004351; F:glutamate 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR022517; Asp_decarboxylase_pyridox.
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 NCBIfam; TIGR03799; NOD_PanD_pyr; 1.
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 337
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 541 AA; 59655 MW; 359FF84854E5A884 CRC64;
MDQKRCAVAS KESLKRIFTV PEAPDSTLSK IELEISSNLA GFLNENIAAI EKPLHVIEKD
FQSAVIPEDP TFVSAYAQDI MEQLVAHSVH TAAPSFIGHM TSALPHFLLP LSKLMVGLNQ
NLVKIETSKA FTPLERQVLG MMHHLAYAQD DSFYSKWMHS AKTSLGAFCS GGTVANITAL
WIARNRLLKP DGDFRGIGAQ GLIAGMLHYG YKGLAVLISE RGHYSLGKSV DLLGIGRDNL
IGIKTSEDNK VDVNAMREKA FELESQGIKV MAIIGVAGTT ETGNIDPLDD MADLSEEIGC
HFHVDAAWGG ATLLSNTHRP LLKGIERADS ITIDAHKQMY VPMGAGLVLF KDPAATDAIE
HHAEYILRKG SKDLGSHTLE GSRPGMAMLV HACLRVIGRK GYEMLIDRSI KKAHYFANLI
KEDEDFELIS EPELCLLTYR YVPKQIKQAI ADADAATRLD IFASLNRFTA SMQKRQRESG
RSFVSRTRLT PSKYDNQPTV VFRVVLANPL TSGAILKEIL AEQKELAKTD PVFKKYLSKY
M
//
