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Database: UniProt/TrEMBL
Entry: A8L3H8_FRASN
LinkDB: A8L3H8_FRASN
Original site: A8L3H8_FRASN 
ID   A8L3H8_FRASN            Unreviewed;       473 AA.
AC   A8L3H8;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   25-OCT-2017, entry version 65.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   OrderedLocusNames=Franean1_6904 {ECO:0000313|EMBL:ABW16238.1};
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW16238.1, ECO:0000313|Proteomes:UP000001313};
RN   [1] {ECO:0000313|Proteomes:UP000001313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EAN1pec {ECO:0000313|Proteomes:UP000001313};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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; CP000820; ABW16238.1; -; Genomic_DNA.
DR   RefSeq; WP_020464304.1; NC_009921.1.
DR   ProteinModelPortal; A8L3H8; -.
DR   STRING; 298653.Franean1_6904; -.
DR   EnsemblBacteria; ABW16238; ABW16238; Franean1_6904.
DR   KEGG; fre:Franean1_6904; -.
DR   eggNOG; ENOG4105CVK; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000070228; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   OrthoDB; POG091H06F5; -.
DR   BioCyc; FSP298653:GHPI-6824-MONOMER; -.
DR   Proteomes; UP000001313; 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:UP000001313};
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:UP000001313}.
FT   MOD_RES     287    287       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   473 AA;  51976 MW;  866EB98934B5580B CRC64;
     MALHGRARGR RGDQAVEVRP HLVIPDEDGP VPRYRMPRSS MSAETAYQIV RDELMLDGNA
     RLNLATFVTT WMDEHADRLM TECAAKNMID KDEYPQTAEL EARCVNMLAD LWHAPDATDA
     VGCSTTGSSE ACMLAGLAML RRWRSTREPH RGEQGGGQRG TGARPNIVMG ANVQVCWEKF
     ARYWDVEPRL MPLAPGRTHL TAPEAVARCD ENTIGVVAVL GSTFDGTYEP VAEIVAALDQ
     LAASGGPDVP VHVDGASGGF IAPFCDPDLV WDFRLERVVS INASGHKYGL VYPGVGWALW
     RDARHLPAEL VFDVDYLGGS MPTFALNFSR PGAQVVAQYY SLLRLGRAGY RHTARTCRDN
     ARWLADEIAK LGPFELISDG SGIPAFAFTT RDAAEFSVFE VSEALRARGW LVPAYRFPPD
     LAELAVLRIV VRAEFSRDLA HLLVEDLHRV VGRLSGPRWR TAAGGADLAS FHH
//
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