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Database: UniProt/TrEMBL
Entry: A0A0M4PZN0_9PSEU
LinkDB: A0A0M4PZN0_9PSEU
Original site: A0A0M4PZN0_9PSEU 
ID   A0A0M4PZN0_9PSEU        Unreviewed;       464 AA.
AC   A0A0M4PZN0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   25-OCT-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=WY02_03110 {ECO:0000313|EMBL:ALE77603.1};
OS   Pseudonocardia sp. AL041005-10.
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Pseudonocardia.
OX   NCBI_TaxID=445576 {ECO:0000313|EMBL:ALE77603.1};
RN   [1] {ECO:0000313|EMBL:ALE77603.1, ECO:0000313|Proteomes:UP000067245}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AL041005-10 {ECO:0000313|EMBL:ALE77603.1,
RC   ECO:0000313|Proteomes:UP000067245};
RX   PubMed=26438860; DOI=10.1073/pnas.1515348112;
RA   Sit C.S., Van Arnam E.B., Ramadhar T.R.;
RT   "Variable genetic architectures produce virtually identical molecules
RT   in bacterial symbionts of fungus-growing ants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:13150-13154(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:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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DR   EMBL; CP011862; ALE77603.1; -; Genomic_DNA.
DR   RefSeq; WP_062395338.1; NZ_CP011862.1.
DR   EnsemblBacteria; ALE77603; ALE77603; WY02_03110.
DR   KEGG; psea:WY02_03110; -.
DR   PATRIC; fig|445576.3.peg.723; -.
DR   KO; K01580; -.
DR   Proteomes; UP000067245; 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:UP000067245};
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}.
FT   MOD_RES     278    278       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   464 AA;  50891 MW;  76E05215115D4D6F CRC64;
     MPGAHSPSED RGDDRAVPVN PVFAAEPVDI PRFRIPGTGM HPEVAYQVVH DELMLDGNAR
     LNLATFVTTW AEPQAERLMA ESFDKNMIDK DEYPRTADLE QRCVRMLADL WHAPDPGRAV
     GCSTTGSSEA CMLGGLALKR RWQHRRKAAG LPADRPNIVM GVNVQICWDK FANYWDVEPR
     LVPMEGDRLH LGVEEAVALC DENTIGVVAI LGSTFDGSYE PVAQLCAALD DLQSRTGLDV
     PVHVDGASGA MIAPFCDPDL EWDFRLPRVA SINTSGHKYG LVHPGVGWAV WRDTDALPED
     LVFRVNYLGG DMPTFALNFS RPGGQVIAQY YNFLRLGHEG YARVQGTCRE IATGLARRIE
     ATGAFRLLTD GSQLPVFAFT VADGEPFSVF DVSAGLRETG WLVPAYTFPE NREDLAALRI
     VVRNGFSHDL AALLLDDLAR LLERLRRQAG PVRGSEAAGF AHGT
//
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