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Database: UniProt
Entry: A0A166RN80_9ACTN
LinkDB: A0A166RN80_9ACTN
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ID   A0A166RN80_9ACTN        Unreviewed;       473 AA.
AC   A0A166RN80;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
GN   ORFNames=UG55_101138 {ECO:0000313|EMBL:OAA26858.1};
OS   Frankia sp. EI5c.
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=683316 {ECO:0000313|EMBL:OAA26858.1, ECO:0000313|Proteomes:UP000077018};
RN   [1] {ECO:0000313|EMBL:OAA26858.1, ECO:0000313|Proteomes:UP000077018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EI5c {ECO:0000313|EMBL:OAA26858.1,
RC   ECO:0000313|Proteomes:UP000077018};
RX   PubMed=27389275;
RA   D'Angelo T., Oshone R., Abebe-Akele F., Simpson S., Morris K., Thomas W.K.,
RA   Tisa L.S.;
RT   "Permanent Draft Genome Sequence for Frankia sp. Strain EI5c, a Single-
RT   Spore Isolate of a Nitrogen-Fixing Actinobacterium, Isolated from the Root
RT   Nodules of Elaeagnus angustifolia.";
RL   Genome Announc. 4:e00660-16(2016).
RN   [2] {ECO:0000313|EMBL:OAA26858.1, ECO:0000313|Proteomes:UP000077018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EI5c {ECO:0000313|EMBL:OAA26858.1,
RC   ECO:0000313|Proteomes:UP000077018};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2;
CC         Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
CC         Evidence={ECO:0000256|ARBA:ARBA00000018,
CC         ECO:0000256|RuleBase:RU361171};
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:OAA26858.1}.
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DR   EMBL; LRTK01000011; OAA26858.1; -; Genomic_DNA.
DR   STRING; 683316.UG55_101138; -.
DR   PATRIC; fig|683316.3.peg.1910; -.
DR   OrthoDB; 3401800at2; -.
DR   Proteomes; UP000077018; 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:0006536; P:glutamate metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.160; -; 1.
DR   Gene3D; 4.10.280.50; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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   NCBIfam; TIGR01788; Glu-decarb-GAD; 1.
DR   PANTHER; PTHR43321; GLUTAMATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43321:SF3; GLUTAMATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077018}.
FT   REGION          454..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         287
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   473 AA;  51669 MW;  CAAD4F9295214133 CRC64;
     MALHGQAKGE RVGQTVAIRP QLVIPDEASX VPRYRLPRSS MPAATAYQLV HDELMLDGNA
     RLNLATFVTT WMDDHANLLM AECASKNMID KDEYPQTAEL ESRCVNMLAD LWHAPDASNT
     IGCSTTGSSE ACMLAGLAML RRWRAARKNG GTRGGGAPGG APPAPNIVMG ANVQVCWEKF
     ARYWDVEPRL VPLAPGRTHL TPEEAVAHCD ANTIGVVAIL GSTFDGTYEP VELIAQELDR
     LAERGGPDVP IHVDAASGGF IAPFCDPDLR WDFRLKRVVS INTSGHKYXL VYPGVGWVVW
     RDVQXLPADL VFDVDYLGGR MPTFALNFSR PGAQVVAQYY SLLRLGHAGY QLSARTCRDN
     ARWIADEVAK LGPFELVSDG SGIPAFAFTT RDGAGFSVFE VSEALRXXGW LVPAYRFPPN
     LTDLTVLRIV VRPEFSRDLA QLLVEDLERV VRRLGSRGGP PARDPAEGAA FHH
//
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