ID A0A0G1YLD9_9BACT Unreviewed; 392 AA.
AC A0A0G1YLD9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 03-MAY-2023, entry version 25.
DE SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:KKW07159.1};
GN ORFNames=UY42_C0017G0005 {ECO:0000313|EMBL:KKW07159.1};
OS Parcubacteria group bacterium GW2011_GWA2_49_16.
OC Bacteria.
OX NCBI_TaxID=1618851 {ECO:0000313|EMBL:KKW07159.1, ECO:0000313|Proteomes:UP000034608};
RN [1] {ECO:0000313|EMBL:KKW07159.1, ECO:0000313|Proteomes:UP000034608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKW07159.1}.
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DR EMBL; LCPY01000017; KKW07159.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1YLD9; -.
DR PATRIC; fig|1618851.3.peg.471; -.
DR Proteomes; UP000034608; 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; 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; 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50}.
FT DOMAIN 23..368
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT DOMAIN 31..268
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT ACT_SITE 332
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 54
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 392 AA; 43137 MW; 7E1B22D4699B997B CRC64;
MTSAIFLDQQ RAETLIAEHG SPLYVYDLDY LKRRVRELKR ICKSVDCLPR YAIKANPHRR
IIKLFNELGL HFDASSDYEV DQAIAAGVNP AQISLSSQQP PRNMRQSLQS GIQFVATSLH
QLELVSQSGW QGVLAVRLNP GLGAGHSRRT TTGGAASSFG IWHEYIPKIL DWQTRSGANI
NRVHIHIGSG GDSKIWRAAI QKSLELVKKM PSVEILNMGG GFKIARIEGE KPANLGKIMD
VFENELEVFA QQTNRKIRFE IEPGAWLVGH AGVLLSRVVD IVDTGKDGWR FIKLDTGMND
LLRPAMYGAQ HSIEVLNNSK NSEEYVVVGH NCETGDILTP APGDPETIKP RRLNEAQIGD
LVTVGGAGAY AASMRAVGYN SFPSAAEVFV NE
//