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Database: UniProt/TrEMBL
Entry: I6XZH2_PSEPQ
LinkDB: I6XZH2_PSEPQ
Original site: I6XZH2_PSEPQ 
ID   I6XZH2_PSEPQ            Unreviewed;       491 AA.
AC   I6XZH2;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   20-JUN-2018, entry version 34.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   OrderedLocusNames=HMPREF9154_2502 {ECO:0000313|EMBL:AFN45150.1};
OS   Pseudopropionibacterium propionicum (strain F0230a) (Propionibacterium
OS   propionicum).
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Pseudopropionibacterium.
OX   NCBI_TaxID=767029 {ECO:0000313|EMBL:AFN45150.1, ECO:0000313|Proteomes:UP000003118};
RN   [1] {ECO:0000313|Proteomes:UP000003118}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0230a {ECO:0000313|Proteomes:UP000003118};
RA   Durkin A.S., Radune D., Hostetler J., Torralba M., Gillis M.,
RA   Methe B., Sutton G., Nelson K.E.;
RT   "The complete genome of chromosome of Propionibacterium propionicum
RT   F0230a.";
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
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; CP002734; AFN45150.1; -; Genomic_DNA.
DR   EnsemblBacteria; AFN45150; AFN45150; HMPREF9154_2502.
DR   KEGG; ppc:HMPREF9154_2502; -.
DR   PATRIC; fig|767029.3.peg.2434; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   OrthoDB; POG091H06F5; -.
DR   Proteomes; UP000003118; 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   InterPro; IPR010107; Glutamate_decarboxylase.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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:UP000003118};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171, ECO:0000313|EMBL:AFN45150.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003118}.
FT   MOD_RES     304    304       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   491 AA;  55134 MW;  B4B439F0602F93A3 CRC64;
     MRQDRFIPGA CEGQAPSPER IEVAMSPSHP HRTASAGTRQ VELNPLFARP GEATELPRTR
     LPRGESLPET AYQIVHDEAM LDGNARLNLA TFVGTWMDDH ANRLALESAD KNMIDKDEYP
     RTAEIETRCW QMLADLWHSP DPEHTIGTST IGSSEAAMLG GLALKRRWQQ ARRAAGKSAD
     RPNLVMSSAV QVCWEKFCNY WDVEARYVPV SREHPIFDGH DLEHYVDENT IGVVAIMGIT
     YTGRYEPVAG IAAALDRIQA ETGLDVRIHV DGASGAMVAP FLQPDLEWDF RLERVVSINT
     SGHKYGLVYP GLGWVVWRTA DDLPEDLVFR VSYLGGDMPT FALNFSRPGS QVLLQYYLFL
     RLGFDGYRRV HETSRSVATF LSGEIGAMDD FELCSDGTDI PVFAWRLTQR PGRNWGLHDL
     SDRLRMKGWL VPTYPLPNDL ADELVQRVVV RNGFSHDLAH AFLDDLRCEV DHLNTLTAPM
     PAITRQSGFH H
//
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