ID   A0A1M6B226_MALRU        Unreviewed;       552 AA.
AC   A0A1M6B226;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:SHI42781.1};
GN   ORFNames=SAMN02745165_00011 {ECO:0000313|EMBL:SHI42781.1};
OS   Malonomonas rubra DSM 5091.
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC   Geopsychrobacteraceae; Malonomonas.
OX   NCBI_TaxID=1122189 {ECO:0000313|EMBL:SHI42781.1, ECO:0000313|Proteomes:UP000184171};
RN   [1] {ECO:0000313|EMBL:SHI42781.1, ECO:0000313|Proteomes:UP000184171}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5091 {ECO:0000313|EMBL:SHI42781.1,
RC   ECO:0000313|Proteomes:UP000184171};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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; FQZT01000001; SHI42781.1; -; Genomic_DNA.
DR   RefSeq; WP_072904712.1; NZ_FQZT01000001.1.
DR   AlphaFoldDB; A0A1M6B226; -.
DR   STRING; 1122189.SAMN02745165_00011; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000184171; Unassembled WGS sequence.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR022517; Asp_decarboxylase_pyridox.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR03799; NOD_PanD_pyr; 1.
DR   PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
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:UP000184171}.
FT   MOD_RES         337
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   552 AA;  61596 MW;  32B5581B1056A95B CRC64;
     MTKKEMAQAN LENLYRIFTV PEAPDSTLGQ IDHAITDNVT GFLQEHVVAL QREMEEIEKD
     FTNPCIPEEP TFVSEYTEFV KDKLVAQSVH TAAPSFVGHM TSALPYFMLP LSRIMIALNQ
     NVVKVETSKA FTPMERQVLA MLHRLIYNFD DNFYPEWIHK SQYALGAFCS GGTIANITAL
     WAARNRLLGP SGDFKGIAQE GLFRAMQHLQ CNGLAVLVSR RGHYSLGKAI DVLGLGRENL
     IAVDTDENNR IDMKQLRYQY ALLKEKGIRP IALVGIAGTT ETGNVDPLNE MADFASEIGC
     HFHVDAAWGG PTLFSEKYRH LLSGIERADS VTIDAHKQLY VPMGAGMVLF KDPTALSAIE
     HHAAYILRHG SKDLGSHTLE GSRPGKSMLV HAGLSIIGRK GYELLIDMGI EKAKMFAEKV
     NQHPDFELIS EPELNILTYR YNPSWLQLAM SQGSAEQVSK ANQLLDQVTR LVQKHQREAG
     KSFVSRTSLR AKAYCDETLT VFRVVLANPL TTDEILSAVL EEQCAIVQGK EIQQLLQDVK
     NIFSDFEQRQ AC
//