ID W0V384_9BURK Unreviewed; 409 AA.
AC W0V384;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Pyridoxal-dependent decarboxylase, C-terminal sheet domain protein {ECO:0000313|EMBL:CDG83294.1};
GN ORFNames=GJA_2663 {ECO:0000313|EMBL:CDG83294.1};
OS Janthinobacterium agaricidamnosum NBRC 102515 = DSM 9628.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=1349767 {ECO:0000313|EMBL:CDG83294.1, ECO:0000313|Proteomes:UP000027604};
RN [1] {ECO:0000313|EMBL:CDG83294.1, ECO:0000313|Proteomes:UP000027604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 102515 / DSM 9628 {ECO:0000313|Proteomes:UP000027604};
RX PubMed=25883287; DOI=10.1128/genomeA.00277-15;
RA Graupner K., Lackner G., Hertweck C.;
RT "Genome Sequence of Mushroom Soft-Rot Pathogen Janthinobacterium
RT agaricidamnosum.";
RL Genome Announc. 3:e00277-e00277(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}.
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; HG322949; CDG83294.1; -; Genomic_DNA.
DR RefSeq; WP_038492658.1; NZ_HG322949.1.
DR AlphaFoldDB; W0V384; -.
DR STRING; 1349767.GJA_2663; -.
DR KEGG; jag:GJA_2663; -.
DR PATRIC; fig|1349767.4.peg.4391; -.
DR eggNOG; COG0019; Bacteria.
DR HOGENOM; CLU_026444_0_3_4; -.
DR OrthoDB; 9802147at2; -.
DR Proteomes; UP000027604; Chromosome I.
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; IPR022657; De-COase2_CS.
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.
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:UP000027604}.
FT DOMAIN 44..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; 44148 MW; B0DF9948CD60E86B CRC64;
MSAPVHAPMT QFEVRGDCLR IGDWSLPQLA RRVGRTPFYA YERRQIERRI GMLREALPAG
IELHYAMKAN PMPALVNLMA GLVDGIDVAS GGELKTALDT PMAPERISFA GPGKTDAELG
CAVAAGVLIN LESEQEMEKV ALLGQYQRVR PKVALRINPD FELKHAGMKM GGGPHQFGID
QQRVPAMLVR LGQLGLDFYG FHIFSGSQNL SAPAICEAQR LSVALALELL PQAPKAMRLL
NIGGGFGVPY FPGEQALELQ PVADNLARQL ALLQRVSPQT RLVLELGRYL VAPAGVYVCR
VLERKISRGQ VFLITDGGLH HHLAASGNFG QVLRKNYPVA IGNHIVSDAR EIVSVVGPLC
TPLDLLADRM EMAYAEVGDL VVVFQSGAYG LSASPGAFLS HPAALEVLV
//
