ID   C7M0P8_ACIFD            Unreviewed;       470 AA.
AC   C7M0P8;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 82.
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=Afer_1640 {ECO:0000313|EMBL:ACU54556.1};
OS   Acidimicrobium ferrooxidans (strain DSM 10331 / JCM 15462 / NBRC 103882 /
OS   ICP).
OC   Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC   Acidimicrobiaceae; Acidimicrobium.
OX   NCBI_TaxID=525909 {ECO:0000313|EMBL:ACU54556.1, ECO:0000313|Proteomes:UP000000771};
RN   [1] {ECO:0000313|EMBL:ACU54556.1, ECO:0000313|Proteomes:UP000000771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10331 / JCM 15462 / NBRC 103882 / ICP
RC   {ECO:0000313|Proteomes:UP000000771};
RX   PubMed=21304635; DOI=10.4056/sigs.1463;
RA   Clum A., Nolan M., Lang E., Glavina Del Rio T., Tice H., Copeland A.,
RA   Cheng J.F., Lucas S., Chen F., Bruce D., Goodwin L., Pitluck S.,
RA   Ivanova N., Mavrommatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Goker M., Spring S., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Chain P., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Acidimicrobium ferrooxidans type strain
RT   (ICP).";
RL   Stand. Genomic Sci. 1:38-45(2009).
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; CP001631; ACU54556.1; -; Genomic_DNA.
DR   RefSeq; WP_015799035.1; NC_013124.1.
DR   AlphaFoldDB; C7M0P8; -.
DR   STRING; 525909.Afer_1640; -.
DR   GeneID; 80815637; -.
DR   KEGG; afo:Afer_1640; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_019582_2_2_11; -.
DR   OrthoDB; 3401800at2; -.
DR   Proteomes; UP000000771; 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   CDD; cd06450; DOPA_deC_like; 1.
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:UP000000771}.
FT   MOD_RES         282
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   470 AA;  52372 MW;  0BADC41B0AFE7155 CRC64;
     MIRLARRHSS PRRHTFSKDL PINPLFVREL TEGVPRARLR SDGLGPDLAY QVIHDEIAMD
     GNARLNLATF VTTWMEPQAD RLYAEAVDKN MIDKDEYPQT AAIEGRCVRM LADLWHAPDP
     DTTIGVSTTG SSEACMLAGL ALKRRWQIAR RATGAPTDRP NIVVSSAVQV VWEKFANYFE
     VEPRYVPVTP EHPTLDADGV LAAVDERTIG VVPILGVTYT GVYEPVAEIA RALDELYERT
     GLDIPIHVDG ASGGFVAPFL EPQLDWDFRL PRVVSINASG HKFGLVYPGL GWVVWRQATD
     VPEELIFRVA YLGGDMPTLA LNFSRPGAQV LLQYYTFLRL GREGFTAVHA SAQRVARMIA
     DELASLGPFE VIGDGRDIPV VAWRLRPGEV RPWDLNHLSH ELRAYGWQVP AYPMPDAMSD
     VTVMRAVVRS EFSADMATLF LDDLAECVEV LERHGTPPPV HPTVRESFHH
//