ID   F9ZCA1_ODOSD            Unreviewed;       465 AA.
AC   F9ZCA1;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 68.
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   OrderedLocusNames=Odosp_1307 {ECO:0000313|EMBL:ADY32347.1};
OS   Odoribacter splanchnicus (strain ATCC 29572 / DSM 20712 / CIP 104287 / JCM
OS   15291 / NCTC 10825 / 1651/6) (Bacteroides splanchnicus).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Odoribacteraceae;
OC   Odoribacter.
OX   NCBI_TaxID=709991 {ECO:0000313|EMBL:ADY32347.1, ECO:0000313|Proteomes:UP000006657};
RN   [1] {ECO:0000313|EMBL:ADY32347.1, ECO:0000313|Proteomes:UP000006657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29572 / DSM 20712 / JCM 15291 / NCTC 10825 / 1651/6
RC   {ECO:0000313|Proteomes:UP000006657};
RX   PubMed=21677857; DOI=10.4056/sigs.1714269;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Goker M., Gronow S., Zeytun A., Nolan M., Lucas S., Lapidus A., Hammon N.,
RA   Deshpande S., Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N.,
RA   Mavromatis K., Ovchinikova G., Pati A., Tapia R., Han C., Goodwin L.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Brambilla E.M.,
RA   Rohde M., Detter J.C., Woyke T., Bristow J., Markowitz V., Hugenholtz P.,
RA   Eisen J.A., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Odoribacter splanchnicus type strain
RT   (1651/6).";
RL   Stand. Genomic Sci. 4:200-209(2011).
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}.
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DR   EMBL; CP002544; ADY32347.1; -; Genomic_DNA.
DR   RefSeq; WP_013611565.1; NZ_CP086000.1.
DR   AlphaFoldDB; F9ZCA1; -.
DR   STRING; 709991.Odosp_1307; -.
DR   PaxDb; 709991-Odosp_1307; -.
DR   GeneID; 69856322; -.
DR   KEGG; osp:Odosp_1307; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_019582_2_1_10; -.
DR   OrthoDB; 9803665at2; -.
DR   BioCyc; OSPL709991:G1GRN-1321-MONOMER; -.
DR   Proteomes; UP000006657; 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; 3.90.1150.160; -; 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:UP000006657}.
FT   MOD_RES         268
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   465 AA;  53225 MW;  CE96508C28C74546 CRC64;
     MKTENPNTPI FGTPEEARVA PKFEMPKTSM PGEVAYQLVH DEAMMDGNAR LNLATFVTTW
     MDDYARRVMT ENMDKNMIDK TEYPQTAEIE RRCVNIIAKL WHSPEPPYCT GTSTVGSSEA
     CMLGGIAALK RWQKRRRAKG LPTNKPNFII STCMQVVWEK FAIYWDVEMR MVPVTMEKIT
     MDPQDVVGMC DENTICVVPI QGVTITGLND NVKEINDALD KLNAEKGWEI CIHVDAATGG
     FIHPFIDPDT VWDFRLKWVL SISVSGHKFG LVYPGVGWVV WKDKQYLPEE MNFAVNYLGA
     NIPSISINFS RPGNQVLAQY YQFLRLGMEG YRQIQQNCID VCLYLKQQLK EMGIFEFFSD
     DMPNPLFIWK LKNDSSRKWT LYDLSDALHA QGWQVPAYTM PKNMEDVVIM RVVVRQGTGK
     DLADLLVKDI KTNIAQLNQL QEPTNSAILW NKREPQKPRG FNHSR
//