ID A0A0T2YJ17_9BURK Unreviewed; 401 AA.
AC A0A0T2YJ17;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:KRB98940.1};
GN ORFNames=ASE11_11495 {ECO:0000313|EMBL:KRB98940.1};
OS Hydrogenophaga sp. Root209.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hydrogenophaga.
OX NCBI_TaxID=1736490 {ECO:0000313|EMBL:KRB98940.1, ECO:0000313|Proteomes:UP000050889};
RN [1] {ECO:0000313|Proteomes:UP000050889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root209 {ECO:0000313|Proteomes:UP000050889};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB98940.1, ECO:0000313|Proteomes:UP000050889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root209 {ECO:0000313|EMBL:KRB98940.1,
RC ECO:0000313|Proteomes:UP000050889};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KRB98940.1}.
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DR EMBL; LMIE01000030; KRB98940.1; -; Genomic_DNA.
DR RefSeq; WP_056274836.1; NZ_LMIE01000030.1.
DR AlphaFoldDB; A0A0T2YJ17; -.
DR STRING; 1736490.ASE11_11495; -.
DR OrthoDB; 9802147at2; -.
DR Proteomes; UP000050889; Unassembled WGS sequence.
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; 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50}.
FT DOMAIN 30..379
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT DOMAIN 38..283
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT ACT_SITE 352
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 60
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 401 AA; 42308 MW; DE93AB2BFAABBE0B CRC64;
MRPSETIRGE LCVGGVPLSR LAERVGQTPF YAYDRRLLVE RVASVREALP AGIGLHYAVK
ANPLPALVGF MRTLVDGLDV ASAGEMAVAL DAGADPVHVS FAGPGKREPE IAQAVAAGVL
VNLESFREVE LLARASQRLG LPARVAVRVN PDFDLRGAGM RMGGGAKPFG VDAEQVPLVL
RAIGDAALQF EGFHLYPGSQ NLNGESIAEA LRQCHQLVVR LAATAPAPVR QVNFGGGWGI
PYFPGEKALD LAPVAEALMG IKNSMASELP GGQLVLELGR YLVGEAGVYV ARVLDRKVSR
GQVFLVTDGG LHHHLAASGN FGQVIRRNYP VCIGTQMDSA EREKASIVGP LCTPLDMLAD
RAELAPAHPG DLVVVYQSGA YGPSASPQAF LGHPRCAEVL V
//
