ID L7EYI6_9ACTN Unreviewed; 467 AA.
AC L7EYI6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Pyridoxal-dependent decarboxylase, pyridoxal binding domain protein {ECO:0000313|EMBL:ELP64493.1};
GN ORFNames=STRTUCAR8_06692 {ECO:0000313|EMBL:ELP64493.1};
OS Streptomyces turgidiscabies Car8.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=698760 {ECO:0000313|EMBL:ELP64493.1, ECO:0000313|Proteomes:UP000010931};
RN [1] {ECO:0000313|EMBL:ELP64493.1, ECO:0000313|Proteomes:UP000010931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Car8 {ECO:0000313|EMBL:ELP64493.1,
RC ECO:0000313|Proteomes:UP000010931};
RX PubMed=21087627; DOI=10.1016/j.plasmid.2010.11.002;
RA Huguet-Tapia J.C., Badger J.H., Loria R., Pettis G.S.;
RT "Streptomyces turgidiscabies Car8 contains a modular pathogenicity island
RT that shares virulence genes with other actinobacterial plant pathogens.";
RL Plasmid 65:118-124(2011).
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:ELP64493.1}.
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DR EMBL; AEJB01000450; ELP64493.1; -; Genomic_DNA.
DR RefSeq; WP_006380479.1; NZ_AEJB01000450.1.
DR AlphaFoldDB; L7EYI6; -.
DR STRING; 85558.T45_08594; -.
DR PATRIC; fig|698760.3.peg.6636; -.
DR Proteomes; UP000010931; Unassembled WGS sequence.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:UniProt.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
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 PANTHER; PTHR43727; DIAMINOPIMELATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43727:SF3; DIAMINOPIMELATE DECARBOXYLASE; 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:UP000010931}.
FT DOMAIN 56..293
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 295..389
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 362
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 467 AA; 48271 MW; 3354818955E5DF5C CRC64;
MEHNRSDRIS RRDEAVRAAV EQGLLHTHAP IVGLLDVTGI RESAAELRAA FDAVLAPGTP
VLHAFAVKAT PLVPVLRLLR EEGIGAEVAS PGELALARAA GVPPNRTVLD SPAKTPAELR
EALALGIAVN ADNPQELDRL DALMSSATSR SPVGIRVNPQ IGGGSIGATS TATATSKFGV
ALQDEGAREW IVGAYAERPW LTRLHAHTGS QGIPLSLMVR GVAETYALAE EINRRVGRRQ
IDTIDIGGGL PVNFASDATS PTFAQYARLL GDAVPGLFSG RYGLVTEFGR SLLAKHGTVV
ARVEYAKSAG GRPVAVTHAG VQVATRTVYA PGSWPLRIAA YDGKGHPKSG ADVVQDVAGP
ACFSGDLLAE GRALPLLEQG DYAAALDTGA YYFAHHYGYN SLARPGIYGF ASARGGDGGD
GDGGDGAVAF AVVREPQTVA EIVAESGGAH ASALTTLATP ASPSARP
//
