ID A0A0M2LR12_9SPHN Unreviewed; 406 AA.
AC A0A0M2LR12;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:KKI18179.1};
GN ORFNames=XM50_18835 {ECO:0000313|EMBL:KKI18179.1};
OS Sphingomonas sp. Ag1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1642949 {ECO:0000313|EMBL:KKI18179.1, ECO:0000313|Proteomes:UP000033997};
RN [1] {ECO:0000313|EMBL:KKI18179.1, ECO:0000313|Proteomes:UP000033997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKI18179.1,
RC ECO:0000313|Proteomes:UP000033997};
RA Pei D., Yu W., Kukutla P., Xu J.;
RT "Draft Genome Sequences of Sphingomonas sp. Ag1 from Mosquito Anopheles
RT gambiae.";
RL Submitted (APR-2015) 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:KKI18179.1}.
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; LAZX01000094; KKI18179.1; -; Genomic_DNA.
DR RefSeq; WP_046411595.1; NZ_LAZX01000094.1.
DR AlphaFoldDB; A0A0M2LR12; -.
DR STRING; 1642949.XM50_18835; -.
DR PATRIC; fig|1642949.3.peg.1476; -.
DR OrthoDB; 9802241at2; -.
DR Proteomes; UP000033997; 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 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 45..285
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 286..381
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 354
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 66
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 406 AA; 42029 MW; CE2A0AB9C3D3BFD0 CRC64;
MSKPFGPLPP EFAAQRGELM IGDRAASAWV AEHGSPLFVY DPAIVADRVR AFRTAFPAVD
LHYAIKANPH PALLQAVAPL VDGLDVASAG ELDKALRVKP AGAISFAGPG KRDAELEAAI
TAGATLNVES EGEAARALAI GGRLGTAPRL AVRVNPDMEL KGSGMKMGGR PSPFGVDAER
AAALVRAIVA GGGAWRGFHI FAGSQALDSQ ALIETQAATL ALAERLSDEA GHMPPLVNLG
GGFGIPHFAG DTPIDLAAIG AALGDALSRT RLSSTFAIEL GRWLVGESGV YLTRVIDRKE
SRGETFLVVD GGLHHQLAAS GNFGTVVRRN YPVAVTHRMA EAGDEEVSVV GCLCTPLDRL
ADKVALPRAD VGDTIAIFIA GAYGATASPG LFLGHPPAVE CVVQRP
//
