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Database: UniProt
Entry: E3CNH4_STRVE
LinkDB: E3CNH4_STRVE
Original site: E3CNH4_STRVE 
ID   E3CNH4_STRVE            Unreviewed;       417 AA.
AC   E3CNH4;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   SubName: Full=Putative diaminopimelate decarboxylase {ECO:0000313|EMBL:EFQ60117.1};
GN   ORFNames=HMPREF9192_0145 {ECO:0000313|EMBL:EFQ60117.1};
OS   Streptococcus vestibularis F0396.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=904306 {ECO:0000313|EMBL:EFQ60117.1, ECO:0000313|Proteomes:UP000004896};
RN   [1] {ECO:0000313|EMBL:EFQ60117.1, ECO:0000313|Proteomes:UP000004896}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0396 {ECO:0000313|EMBL:EFQ60117.1,
RC   ECO:0000313|Proteomes:UP000004896};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (OCT-2010) 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:EFQ60117.1}.
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DR   EMBL; AEKO01000003; EFQ60117.1; -; Genomic_DNA.
DR   RefSeq; WP_003092158.1; NZ_AEKO01000003.1.
DR   AlphaFoldDB; E3CNH4; -.
DR   GeneID; 77297831; -.
DR   eggNOG; COG0019; Bacteria.
DR   OrthoDB; 9802241at2; -.
DR   Proteomes; UP000004896; 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..279
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          280..367
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   ACT_SITE        340
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   417 AA;  46306 MW;  E95D0D9E9C49C606 CRC64;
     MTKTPFITAD KLDQITAEFP TPFHLYDEKG IRETARAVNA AFSWNPGFKE FFAVKATPNP
     AILKILKEEG CGVDCATDTE LVMSNKIGFD STAISFTSND TRAEEFVYAR DINATINLDA
     YEDIFFLEEA AGLPETLSLR FNPGGVFSLG TDIMDHPEES KFGMTKEQLF KGYAYLKEKG
     VKSFGLHAFL ASNTVTNEYY PTLAAQLFEL AVEIKNELGV SLDFINLSGG VGVDYTPANK
     QNDIAVIGEG VHTKFDEILV PNDLGDISIY TELGRFMTAP HGLVVTKVLH IKDTYRRYVG
     VDASAVNLLR PAMYDAYHHI TNMTNPNGDI QVVDVTGSLC ENNDKFAKNR ELPEARIGDT
     LVIHDTGAHG FSMGYNYNGR LRSAEILYQE DGTARMIRRA ETMNDYFATL DGFDFEI
//
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