UniProt: A0A0C3REM0

Database: UniProt
Entry: A0A0C3REM0_9PORP

LinkDB:  A0A0C3REM0_9PORP 
Original site:  A0A0C3REM0_9PORP

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (5)   
   InterPro (4)   
   Pfam (1)   
Literature (1)   
   PubMed (1)   
All databases (13)   

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ID   A0A0C3REM0_9PORP        Unreviewed;       465 AA.
AC   A0A0C3REM0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 42.
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=BA92_08150 {ECO:0000313|EMBL:KIO44976.1}, DMB45_13695
GN   {ECO:0000313|EMBL:PXZ42866.1};
OS   Sanguibacteroides justesenii.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Sanguibacteroides.
OX   NCBI_TaxID=1547597 {ECO:0000313|EMBL:KIO44976.1, ECO:0000313|Proteomes:UP000031980};
RN   [1] {ECO:0000313|EMBL:KIO44976.1, ECO:0000313|Proteomes:UP000031980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OUH 308042 {ECO:0000313|EMBL:KIO44976.1,
RC   ECO:0000313|Proteomes:UP000031980};
RA   Sydenham T.V., Hasman H., Justensen U.S.;
RT   "Porphyromonadaceae bacterium OUH 308042 = ATCC BAA-2681 = DSM 28342 draft
RT   genome.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PXZ42866.1, ECO:0000313|Proteomes:UP000248308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OUH 969102 {ECO:0000313|EMBL:PXZ42866.1,
RC   ECO:0000313|Proteomes:UP000248308};
RX   PubMed=25814588;
RA   Sydenham T.V., Hasman H., Justesen U.S.;
RT   "Draft Genome Sequences of Sanguibacteroides justesenii, gen. nov., sp.
RT   nov., Strains OUH 308042T (= ATCC BAA-2681T) and OUH 334697 (= ATCC BAA-
RT   2682), Isolated from Blood Cultures from Two Different Patients.";
RL   Genome Announc. 3:e00005-15(2015).
RN   [3] {ECO:0000313|EMBL:PXZ42866.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OUH 969102 {ECO:0000313|EMBL:PXZ42866.1};
RA   Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA   Wayne K.J., Tettelin H., Glass J.I., Rusch D., Podicherti R., Tsui H.-C.T.,
RA   Winkler M.E.;
RL   Submitted (MAY-2018) 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:KIO44976.1}.
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DR   EMBL; JPIU01000038; KIO44976.1; -; Genomic_DNA.
DR   EMBL; QJPL01000010; PXZ42866.1; -; Genomic_DNA.
DR   RefSeq; WP_041504370.1; NZ_QJPL01000010.1.
DR   AlphaFoldDB; A0A0C3REM0; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000031980; Unassembled WGS sequence.
DR   Proteomes; UP000248308; 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:UP000031980}.
FT   MOD_RES         268
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   465 AA;  53558 MW;  FB2E8463DC18463F CRC64;
     MKTENPNTPI FGTSEEARVA PKYEMPKTSM PGEVAYQIVH DEAMLDGNSR LNLATFVSTW
     MDDYARRVMT ENMDKNMIDK TEYPQTAEIE RRCVNIIAKL WNSPEKPYCT GTSTVGSSEA
     CMLGGIAALK RWQKRRKAKG LPIDKPNFII STCMQVVWEK FAIYWDVEMR MVPVTMDKIT
     LDPQEVVKMC DENTICVVPI QGVTITGLND NVKEINDALD KLNAEKGWEI CIHVDAATGG
     FIHPFIDPET VWDFRLKWVL SISVSGHKFG LVYPGVGWVV WKDKQYLPQE MNFAVNYLGA
     DIPSISINFS RPGNQVLAQY YQFLRLGWEG YRQIQQNCLN VCLYLKKRLQ DMGIFEFFSN
     EMPNPLFIWK LKDDPKRKWT LYDLSDALHV EGWQVPAYTM PKDMEDVVIM RVVVRQGTGF
     DLADLLMEDM KRCVDQLNKL EEPTNSAILW NKKMPQKPRG FNHSR
//

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