ID   E1VG43_9GAMM            Unreviewed;       558 AA.
AC   E1VG43;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   SubName: Full=Putative glutamate decarboxylase {ECO:0000313|EMBL:CBL43785.1};
GN   ORFNames=HDN1F_02020 {ECO:0000313|EMBL:CBL43785.1};
OS   gamma proteobacterium HdN1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=83406 {ECO:0000313|EMBL:CBL43785.1, ECO:0000313|Proteomes:UP000002677};
RN   [1] {ECO:0000313|EMBL:CBL43785.1, ECO:0000313|Proteomes:UP000002677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HdN1 {ECO:0000313|Proteomes:UP000002677};
RA   Widdel F., Rabus R., Grundmann O., Werner I., Schreiber F., Ehrenreich P.,
RA   Behrends A., Wilkes H., Kube M., Reinhardt R., Zedelius J.;
RT   "Alkane degradation by a new type of denitrifying bacterium with possible
RT   involvement of the electron acceptor in substrate activation.";
RL   Environ. Microbiol. 0:0-0(2010).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FP929140; CBL43785.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1VG43; -.
DR   STRING; 83406.HDN1F_02020; -.
DR   KEGG; gpb:HDN1F_02020; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_011856_0_4_6; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000002677; Chromosome.
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:UP000002677}.
FT   MOD_RES         343
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   558 AA;  62519 MW;  6AB7B435B529F9E7 CRC64;
     MHQDKRPATQ RFAEANMDAM YRIFTVPEAP GSTLGQIDNM ISQNLMGFLQ NHIVAVEKDL
     SEVEKDFADA HIPEKPWFVS DQTQFLLDKL VAQSVHTASP SFVGHMTSAL PYFMLPLSRI
     MMALNQNLVK IETSKAFTPL ERQVLGMMHR LIYERDDKFY DQWMHKSGHS LGVLCSGGTI
     ANMTALWVAR NAMFKPSKGF KGINHTGVFG ALKHHGLEGM AVLVSERGHY SLAKAADVLG
     IGRDHLLTVR TDDNNKVNIR KMRQKLEECR SRNIGVMAIV GVCGTSETGT VDPLNDLADL
     AEEFGCHYHV DAAWGGATLF SQKYSHILEG IRRADSVTID GHKQLYVPMG AGMVFFKNPT
     ALSNIQHHAE YIIRQGSKDL GSHTLEGSRP GMAMLVHSGL RIIGRSGYEI LINEGIEKAR
     AFADMVRAEP DFEMITEPEL NILTYRYVPE FVKKKLATAN AREIDHIHDL LNRLTKLIQK
     TQRARGKSFV SRTRLTPEKY GHRLTVVFRV VLANPLTNHQ ILRGVLEEQR TIASLEDCQQ
     LLRQLSEACA EARHVSNG
//