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Database: UniProt
Entry: A0A0M5IWU1_SPHS1
LinkDB: A0A0M5IWU1_SPHS1
Original site: A0A0M5IWU1_SPHS1 
ID   A0A0M5IWU1_SPHS1        Unreviewed;       409 AA.
AC   A0A0M5IWU1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:ALC11556.1};
GN   ORFNames=LH20_06275 {ECO:0000313|EMBL:ALC11556.1};
OS   Sphingopyxis sp. (strain 113P3).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=292913 {ECO:0000313|EMBL:ALC11556.1, ECO:0000313|Proteomes:UP000061305};
RN   [1] {ECO:0000313|EMBL:ALC11556.1, ECO:0000313|Proteomes:UP000061305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=113P3 {ECO:0000313|EMBL:ALC11556.1,
RC   ECO:0000313|Proteomes:UP000061305};
RX   PubMed=26472829;
RA   Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA   Tsuda M., Fujita N., Kawai F.;
RT   "Complete Genome Sequence of Polyvinyl Alcohol-Degrading Strain
RT   Sphingopyxis sp. 113P3 (NBRC 111507).";
RL   Genome Announc. 3:e01169-15(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; CP009452; ALC11556.1; -; Genomic_DNA.
DR   RefSeq; WP_053553455.1; NZ_CP009452.1.
DR   AlphaFoldDB; A0A0M5IWU1; -.
DR   STRING; 292913.LH20_06275; -.
DR   KEGG; sphp:LH20_06275; -.
DR   PATRIC; fig|292913.6.peg.1277; -.
DR   OrthoDB; 9802241at2; -.
DR   Proteomes; UP000061305; Chromosome.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:UniProt.
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; IPR022657; De-COase2_CS.
DR   InterPro; IPR022644; De-COase2_N.
DR   InterPro; IPR000183; Orn/DAP/Arg_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   SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
DR   PROSITE; PS00879; ODR_DC_2_2; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000061305}.
FT   DOMAIN          46..292
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          293..387
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   ACT_SITE        360
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         68
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   409 AA;  41901 MW;  8705266459E41E96 CRC64;
     MKPHGPIPPG YSADADGMLI VGGERADALA ARAGDTPLFV YDSALLKARV AEWRAAMPSE
     VQLHYAMKAN PFAPLLTFMA GIVDGFDVAS GGELAAALAS GMEAEHISFA GPGKRDRELE
     AAIKAGATIN LESAGEAERA LHIAARLGAR PRLAVRVNPD FDLKGSGMKM GGGAKPFGVD
     AEDVPALVRR LVDAGADWQG FHIFAGSQAL SAAAIAETQA QTVALAARLA NGIGAAPPLV
     NLGGGMGVPY FPGDSAVDTA AVGAALAETL AARDPVLGAS RFAMELGRWL VAEAGVYITR
     IVDRKVSHGE IFLVTDGGLH HQLAASGNFG TVIRRNYPIA IASHFGAEAV ETVSVVGCLC
     TPLDRLGDQV ALPRAEAGDL VAIFQAGAYG ASASPAAFLG QGPAREILV
//
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