ID A0A1G6X3G6_9SPHI Unreviewed; 404 AA.
AC A0A1G6X3G6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Diaminopimelate decarboxylase {ECO:0000256|RuleBase:RU003738};
DE EC=4.1.1.20 {ECO:0000256|RuleBase:RU003738};
GN ORFNames=SAMN05216464_102389 {ECO:0000313|EMBL:SDD72658.1};
OS Mucilaginibacter pineti.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1391627 {ECO:0000313|EMBL:SDD72658.1, ECO:0000313|Proteomes:UP000199072};
RN [1] {ECO:0000313|EMBL:SDD72658.1, ECO:0000313|Proteomes:UP000199072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47C3B {ECO:0000313|EMBL:SDD72658.1,
RC ECO:0000313|Proteomes:UP000199072};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + meso-2,6-diaminoheptanedioate = CO2 + L-lysine;
CC Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20;
CC Evidence={ECO:0000256|RuleBase:RU003738};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR600183-50, ECO:0000256|RuleBase:RU003738};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.
CC {ECO:0000256|RuleBase:RU003738}.
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; FNAI01000002; SDD72658.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6X3G6; -.
DR STRING; 1391627.SAMN05216464_102389; -.
DR OrthoDB; 9802241at2; -.
DR UniPathway; UPA00034; UER00027.
DR Proteomes; UP000199072; Unassembled WGS sequence.
DR GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR CDD; cd06828; PLPDE_III_DapDC; 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; IPR022644; De-COase2_N.
DR InterPro; IPR022653; De-COase2_pyr-phos_BS.
DR InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR InterPro; IPR029066; PLP-binding_barrel.
DR NCBIfam; TIGR01048; lysA; 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; 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; PS00878; ODR_DC_2_1; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003738};
KW Decarboxylase {ECO:0000256|RuleBase:RU003738};
KW Lyase {ECO:0000256|RuleBase:RU003738};
KW Lysine biosynthesis {ECO:0000256|RuleBase:RU003738};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000199072}.
FT DOMAIN 18..379
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT DOMAIN 40..271
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT ACT_SITE 352
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 48
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 404 AA; 45294 MW; A411AC1A7E4375A7 CRC64;
MFNNTTINRF QDLDTPFYYY DMEVLRQTLD ACREASAKHG FHVHYAMKAN FNPRVLDMIQ
SFGFGADCVS GNEVRAAIEH GFGKDKVVFA GVGKSDKEIN FALDADIFCF NVESVQELEI
INELAGAKGK KANVAIRINP NVDAHTHHFI TTGLDENKFG INIWQLPDVA TALRKCENLK
FLGIHFHIGS QITDLEVYKS LCTRINEMQD WFEDHGFPVK VLNTGGGLGV DYYSPNGNIA
DFESYFQVFK SFLNVKPGQE VHFELGRALV AQSASLISRV LYVKNGKKKN FLILDAGMTE
LIRPMLYQAY HLIENLSRRA EVRGLRSEAE KQASDLTPHT TELKYDVVGP ICESTDCFQK
DVDLPESFRG DLIAVRTAGA YGEVMASGYN LRDHVQSVYS EGVA
//
