ID A0A1H4TPB7_9PSEU Unreviewed; 432 AA.
AC A0A1H4TPB7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:SEC58285.1};
GN ORFNames=SAMN04489727_4287 {ECO:0000313|EMBL:SEC58285.1};
OS Amycolatopsis tolypomycina.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=208445 {ECO:0000313|EMBL:SEC58285.1, ECO:0000313|Proteomes:UP000199622};
RN [1] {ECO:0000313|EMBL:SEC58285.1, ECO:0000313|Proteomes:UP000199622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44544 {ECO:0000313|EMBL:SEC58285.1,
RC ECO:0000313|Proteomes:UP000199622};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNSO01000004; SEC58285.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4TPB7; -.
DR STRING; 208445.SAMN04489727_4287; -.
DR OrthoDB; 9802241at2; -.
DR Proteomes; UP000199622; Unassembled WGS sequence.
DR GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:InterPro.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; 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; IPR002986; DAP_deCOOHase_LysA.
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: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; PR01181; DAPDCRBXLASE.
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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50}.
FT DOMAIN 17..374
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT DOMAIN 38..272
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT REGION 411..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 347
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 47
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 432 AA; 46395 MW; 4CE7E15DB613A6A8 CRC64;
MTEIDYQDLA ARFGTPLYVY DGDVLHATIT GLRAVLHPAI EVFYSLKANP NISVFAALHH
GGARAEVSSI VELQTVLTAG ARPDDIIFLG PGKSEQELRA CLETGVYAIV CESFDELDDI
ERLGAELGKV QRVLLRINPT CAISGSRLTM GGKPRQFGID EAQVLAAGPR LAEYRHADVA
GIQVYMGTRI LDADVIGKNT RYALDLAERV AAETGIRLEA VDIGGGLGVA YFEGEDDLDA
ADVAAEINPM LEAFHRAHPA TRLIMESGRF LAGRAGVYVL GVRYVKESMG ERFAIADGGT
HHHMAAVGIG SFVKRNFPAV LLTPRAAGED TDDTVEPGPW TVTGPLCTPN DTLLKQVKLP
DLRAGDLVGV LNSGAYGPSA SPGLFLSHGF PAEVLVRGGA AFLVRDRDEP EDLLRKQHLH
QPLTDSKESE PR
//
