ID A0A132SC54_9MYCO Unreviewed; 408 AA.
AC A0A132SC54;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:KWX56725.1};
GN ORFNames=ASJ79_02115 {ECO:0000313|EMBL:KWX56725.1};
OS Mycobacterium sp. NAZ190054.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1747766 {ECO:0000313|EMBL:KWX56725.1, ECO:0000313|Proteomes:UP000070146};
RN [1] {ECO:0000313|EMBL:KWX56725.1, ECO:0000313|Proteomes:UP000070146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAZ190054 {ECO:0000313|EMBL:KWX56725.1,
RC ECO:0000313|Proteomes:UP000070146};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) 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:KWX56725.1}.
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; LMVQ01000582; KWX56725.1; -; Genomic_DNA.
DR RefSeq; WP_067963215.1; NZ_LMVQ01000582.1.
DR AlphaFoldDB; A0A132SC54; -.
DR Proteomes; UP000070146; Unassembled WGS sequence.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:UniProt.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000070146}.
FT DOMAIN 44..291
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 292..386
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 359
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 66
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 408 AA; 43245 MW; 3A9AAACD9CEB47AF CRC64;
MNLRPMIAAF GSIDGQLAVG GMPLDRLTAR VGSTPYFAYD RRLLTERVET LRAALPPALK
LSYAVKANPM PAVVQHLAGL VDALDVASAL EMQTALDTTM PASRVFFAGP GKTEAEIVQA
VAAGVTVEME SETEARRVIR AGDTLGIRPR VALRVNPDFR VKGSGMRMGG GPQQFGVDAE
QAPDLLADLA TADLDFLGFH VFAGAQNLNA QILCEAQRQT VELILGLAEK APAPVRYVNL
GGGFGIPYFD KDVPLDIAPL GANLAELVGD EITPNLPEAE VVVELGRYIV GECGVYVTRV
VDRKVSRGRT YLVVDGGMHH QLSASGNFGQ VIRRNYPIAV GNRLHEPAES AVTVVGCLCT
PLDLLGDDVT LPDADVGDSI VLFQAGAYGL TASPTAFLGH PQPIEVLV
//