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Database: UniProt
Entry: C0C3Y7_9FIRM
LinkDB: C0C3Y7_9FIRM
Original site: C0C3Y7_9FIRM 
ID   C0C3Y7_9FIRM            Unreviewed;       425 AA.
AC   C0C3Y7;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   SubName: Full=Putative diaminopimelate decarboxylase {ECO:0000313|EMBL:EEG73145.1};
GN   ORFNames=CLOHYLEM_06799 {ECO:0000313|EMBL:EEG73145.1};
OS   [Clostridium] hylemonae DSM 15053.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=553973 {ECO:0000313|EMBL:EEG73145.1, ECO:0000313|Proteomes:UP000004893};
RN   [1] {ECO:0000313|EMBL:EEG73145.1, ECO:0000313|Proteomes:UP000004893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15053 {ECO:0000313|EMBL:EEG73145.1,
RC   ECO:0000313|Proteomes:UP000004893};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Clostridium hylemonae (DSM 15053).";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEG73145.1, ECO:0000313|Proteomes:UP000004893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15053 {ECO:0000313|EMBL:EEG73145.1,
RC   ECO:0000313|Proteomes:UP000004893};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2009) 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:PIRSR600183-50};
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       {ECO:0000256|RuleBase:RU003737}.
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:EEG73145.1}.
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DR   EMBL; ABYI02000031; EEG73145.1; -; Genomic_DNA.
DR   RefSeq; WP_006444158.1; NZ_GG657759.1.
DR   AlphaFoldDB; C0C3Y7; -.
DR   STRING; 553973.CLOHYLEM_06799; -.
DR   eggNOG; COG0019; Bacteria.
DR   HOGENOM; CLU_026444_0_2_9; -.
DR   OrthoDB; 9802241at2; -.
DR   Proteomes; UP000004893; Unassembled WGS sequence.
DR   GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:InterPro.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR   CDD; cd06828; PLPDE_III_DapDC; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR002986; DAP_deCOOHase_LysA.
DR   InterPro; IPR022643; De-COase2_C.
DR   InterPro; IPR022644; De-COase2_N.
DR   InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   PANTHER; PTHR43727; DIAMINOPIMELATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43727:SF2; DIAMINOPIMELATE DECARBOXYLASE 1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF02784; Orn_Arg_deC_N; 1.
DR   Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR   PRINTS; PR01181; DAPDCRBXLASE.
DR   PRINTS; PR01179; ODADCRBXLASE.
DR   SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50}.
FT   DOMAIN          31..278
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          279..369
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   ACT_SITE        342
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         55
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   425 AA;  47927 MW;  097C8B4588C42831 CRC64;
     MKKETFVTKE QLDEIIKDYP TPFHLYDEKG IRRNMQALRD AFSWNKGYKE YFAVKATPNP
     YLIDILREYG CGCDCSSYTE LMLSEAVGAT GDDIMFSSND TPAEEFIYAE KLGAIINLDD
     ITHIEFLEET IGYIPKTISC RYNPGGLFKI SNDIMDNPGD SKYGMTTEQL FEAFKILKSK
     GAEEFGIHAF LASNTVTNEY YPMLAKILFE EAVRLQKETG VHIKFINLSG GIGIPYTPDQ
     EPNDIRIIGD GVRRVYEEVL VPAGMGDVEI YTELGRFMLG PYGCLVTEAI HEKHTHKEYI
     GVDACAVNLM RPAMYGAYHH VTVMGREDCP CDHKYDVVGS LCENNDKFAI DRMLPKVEMG
     DILVIHDTGA HGFSMGYNYN GKLKSAELLL KEDGSAQLIR RAETPADYFA TFDCFDIGKK
     LLNMR
//
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