ID A0A0L0K438_9ACTN Unreviewed; 480 AA.
AC A0A0L0K438;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:KND32573.1};
GN ORFNames=IQ63_22800 {ECO:0000313|EMBL:KND32573.1};
OS Streptomyces acidiscabies.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=42234 {ECO:0000313|EMBL:KND32573.1, ECO:0000313|Proteomes:UP000037151};
RN [1] {ECO:0000313|Proteomes:UP000037151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 4445 {ECO:0000313|Proteomes:UP000037151};
RA Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT "Genome sequencing of plant-pathogenic Streptomyces species.";
RL Submitted (JUL-2014) 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:KND32573.1}.
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DR EMBL; JPPY01000134; KND32573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0K438; -.
DR PATRIC; fig|42234.21.peg.4717; -.
DR Proteomes; UP000037151; 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:UP000037151}.
FT DOMAIN 87..320
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 322..416
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT REGION 178..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 389
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 95
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 480 AA; 50353 MW; 6B9A5FA1F08E80ED CRC64;
MLRPTETTRQ YGYRTTSTGA DVRQAADGRA VDDGRAVRRD DAVRAAVEQG LLGPDTPIVG
LLDVTGIKES AAGLTAAFDA VVPPGTPVLH AFAVKATPLV PVLRLLREAG IGAEVASPGE
LALARAAGFG AHSTVLDSPA KTPAELREAL ALGIAVNADN PQELARIDAL RRETPSASPI
GIRVNPQVGG GTIESTSTAT PTSKFGVALR DEGAREWVIG AYAERPWLTR LHAHTGSQGV
PLTLMARGVA EAYALAEEIN RRIGRRQIDT VDIGGGLPVN YGSEDTTPTY AQYARLLKEA
VPGLFDGRYG LVTEFGRSLL AKQGTVVARV EYAKSAGGRR IAVTHAGVQV ATRTVYMPGS
WPLRIAAYDA KGRAKSGPEA VQDVAGPACF SGDLLARGRS LPLLEQGDYA AALDTGAYYF
AHHYAYNSLP RPALYGYVPG ADGHTRFALV RAAQTTAEIL AEAGGAYGDA LTTLGEPERP
//
