ID T0J098_9SPHN Unreviewed; 439 AA.
AC T0J098;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Diaminopimelate decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=L284_11880 {ECO:0000313|EMBL:EQB15329.1};
OS Novosphingobium lindaniclasticum LE124.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1096930 {ECO:0000313|EMBL:EQB15329.1, ECO:0000313|Proteomes:UP000015527};
RN [1] {ECO:0000313|EMBL:EQB15329.1, ECO:0000313|Proteomes:UP000015527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LE124 {ECO:0000313|EMBL:EQB15329.1,
RC ECO:0000313|Proteomes:UP000015527};
RX PubMed=24029761;
RA Saxena A., Nayyar N., Sangwan N., Kumari R., Khurana J.P., Lal R.;
RT "Genome Sequence of Novosphingobium lindaniclasticum LE124T, Isolated from
RT a Hexachlorocyclohexane Dumpsite.";
RL Genome Announc. 1:e00715-13(2013).
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:EQB15329.1}.
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DR EMBL; ATHL01000076; EQB15329.1; -; Genomic_DNA.
DR AlphaFoldDB; T0J098; -.
DR PATRIC; fig|1096930.3.peg.2365; -.
DR eggNOG; COG0019; Bacteria.
DR OrthoDB; 9802241at2; -.
DR Proteomes; UP000015527; 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; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000015527}.
FT DOMAIN 27..279
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 280..376
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 349
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 51
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 439 AA; 47720 MW; 04FF22CB1A78535B CRC64;
MTRSDEDELL KRAADRFGTP CFVYFTQRIE QRISLLRTNF GPDLGLSYAV KANPNPALLE
WLSGEVDHLD ISSAGELRLA QEAGWDPALL SFTGPGKREA EIREAIRAGV GHLVIESLRE
ARIADRIARQ AARVQPVLVR ISPESLPKGF GDQMAGKPTP FGIDMEVAHD AISIIQSLTG
LSLAGFHIYA GTQCLKADVI AETYRHLLDI FARLCSAHDV KPAMLVMGSG LGVPYHQGET
PVDLRFVSRM LNGELSTFRK EPRFTNAKIV LELGRYLVSQ AGYFVTRVVS TKTSRGRRIA
ICDGGMNNHL PASGHFGMVM RRSYRMHSIG VRNGSADETE AVDVVGPLCT SIDRLASGVE
LPRLDEGDLI AVHNSGAYGL TASPVHFISH PMPEEVMVVA DTLLRITRSF ASGPARACDS
EDAVRLVDGT HPAAANQNA
//