GenomeNet

Database: UniProt/TrEMBL
Entry: A0A0D5LMI4_9RHIZ
LinkDB: A0A0D5LMI4_9RHIZ
Original site: A0A0D5LMI4_9RHIZ 
ID   A0A0D5LMI4_9RHIZ        Unreviewed;       464 AA.
AC   A0A0D5LMI4;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   05-JUL-2017, entry version 17.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=TM49_03605 {ECO:0000313|EMBL:AJY44977.1};
OS   Martelella endophytica.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Aurantimonadaceae; Martelella.
OX   NCBI_TaxID=1486262 {ECO:0000313|EMBL:AJY44977.1, ECO:0000313|Proteomes:UP000032611};
RN   [1] {ECO:0000313|EMBL:AJY44977.1, ECO:0000313|Proteomes:UP000032611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YC6887 {ECO:0000313|EMBL:AJY44977.1};
RX   PubMed=25953177;
RA   Khan A., Khan H., Chung E.J., Hossain M.T., Chung Y.R.;
RT   "Complete Genome Sequence of Martelella endophytica YC6887, Which Has
RT   Antifungal Activity Associated with a Halophyte.";
RL   Genome Announc. 3:0-0(2015).
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:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP010803; AJY44977.1; -; Genomic_DNA.
DR   RefSeq; WP_045679568.1; NZ_CP010803.1.
DR   EnsemblBacteria; AJY44977; AJY44977; TM49_03605.
DR   KEGG; mey:TM49_03605; -.
DR   PATRIC; fig|1486262.3.peg.734; -.
DR   KO; K01580; -.
DR   Proteomes; UP000032611; 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:UP000032611};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032611}.
FT   MOD_RES     273    273       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   464 AA;  51979 MW;  DF9444B6CE6BB778 CRC64;
     MDRKTAAEAL FDPNDETYGT ADLSAILPKS KFPDAERAPR LAYAAIHDEL LLDGNARQNL
     ATFCQTWEEP EVHQLMDDCI DKNMIDKDEY PQTAEIEARC IRMLADLWNA PQGPATGTST
     TGSSEAAMLG GLAMKRRWET KRKAEGKPID KPNLITGPVQ VCWHKFTRYW DIEHREIPME
     DGRLLMTPEE VLKLCDENTI GVVPTLGVTF TGEYEPVRAV SDALDDLQAR TGLDIPIHVD
     GASGGFLAPF CAPDLEWDFR LPRVKSINAS GHKFGLSPLG VGWVLWREEQ DLPEQMIFWV
     NYLGGNMRDI ALNFSRPGGQ VVCQYYNFLR LGRDGYRKVH EACYRSAAYL AEALEKTGLV
     DIVFDGDPAR GIPAVSWKLK EGLATNYTLF DLADRLRARG WQVPAYTLPA NCENQAIQRI
     LVRNGVSIDL CSLLIDDMMT AVEYFRAHPV SKPLTEDEAS GFHH
//
DBGET integrated database retrieval system