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Database: UniProt
Entry: A0A0S6X6Q7_9SPHN
LinkDB: A0A0S6X6Q7_9SPHN
Original site: A0A0S6X6Q7_9SPHN 
ID   A0A0S6X6Q7_9SPHN        Unreviewed;       408 AA.
AC   A0A0S6X6Q7;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:GAM07018.1};
GN   ORFNames=MBENS4_4014 {ECO:0000313|EMBL:GAM07018.1};
OS   Novosphingobium sp. MBES04.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1206458 {ECO:0000313|EMBL:GAM07018.1};
RN   [1] {ECO:0000313|EMBL:GAM07018.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBES04 {ECO:0000313|EMBL:GAM07018.1};
RA   Ohta Y., Nishi S., Kobayashi K., Tsubouchi T., Iida K., Tanizaki A.,
RA   Kurosawa K., Adachi A., Nishihara M., Sato R., Hasegawa R., Hatada Y.;
RT   "Draft Genome Sequence of Novosphingobium sp. Strain MBES04, Isolated from
RT   Sunken Wood from Suruga Bay, Japan.";
RL   Genome Announc. 3:e01373-14(2015).
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}.
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DR   EMBL; DF850489; GAM07018.1; -; Genomic_DNA.
DR   RefSeq; WP_039394007.1; NZ_DF850489.1.
DR   AlphaFoldDB; A0A0S6X6Q7; -.
DR   STRING; 1206458.MBENS4_4014; -.
DR   HOGENOM; CLU_026444_0_3_5; -.
DR   OrthoDB; 9802241at2; -.
DR   Proteomes; UP000053513; Unassembled WGS sequence.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:UniProt.
DR   GO; GO:0006596; P:polyamine biosynthetic process; IEA:InterPro.
DR   CDD; cd06839; PLPDE_III_Btrk_like; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR017530; DCO2ase_PEP1.
DR   InterPro; IPR022643; De-COase2_C.
DR   InterPro; IPR022644; De-COase2_N.
DR   InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR   InterPro; IPR002433; Orn_de-COase.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   NCBIfam; TIGR03099; dCO2ase_PEP1; 1.
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; PR01179; ODADCRBXLASE.
DR   PRINTS; PR01182; ORNDCRBXLASE.
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          44..290
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          291..386
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   ACT_SITE        359
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         67
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   408 AA;  42946 MW;  98CC52E2ABD892E9 CRC64;
     MKPLGPIPAG FEAIDGVLGV AGRPVTHWVE EAGDTPLFLY SAERIRARIA QLRAAMPKRL
     ALHYAVKANP FGPVLSLMHG LVDGFDIASG GELRELLSCG VAGGEISFAG PGKRDRELEA
     AIVHGVTLNL ESEGEATRAL ALGQKLGLRP RLAVRVNPDF DLKGSGMKMG GGAKPFGIDA
     ERVPALVRRL LDADADWRGF HIFAGSQALD ASAIAETQGQ TLDLAARLAQ EAGKAPPHCN
     LGGGLGIPYF GPDTPVDLEA VGGALAQRFE RLPEILQDTR FCMELGRYLV GEAGVYLTRV
     LDRKMSHGET FLVTDGGLHH QLAASGNFGT VVRRNYPVAL ATRFGAPVEE EVSIVGCLCT
     PLDKLAEKAG FPRADVGDLV AVFCAGAYGA SASPASFLGQ GPALERLV
//
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