ID A0A0T5ZII7_9CHLR Unreviewed; 385 AA.
AC A0A0T5ZII7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Diaminopimelate decarboxylase, diaminopimelate decarboxylase {ECO:0000313|EMBL:KRT62438.1};
DE EC=4.1.1.20 {ECO:0000313|EMBL:KRT62438.1};
GN Name=lysA {ECO:0000313|EMBL:KRT62438.1};
GN ORFNames=XU10_C0028G0017 {ECO:0000313|EMBL:KRT62438.1};
OS Chloroflexi bacterium CSP1-4.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1640513 {ECO:0000313|EMBL:KRT62438.1, ECO:0000313|Proteomes:UP000051896};
RN [1] {ECO:0000313|EMBL:KRT62438.1, ECO:0000313|Proteomes:UP000051896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-4 {ECO:0000313|EMBL:KRT62438.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-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:KRT62438.1}.
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DR EMBL; LDXM01000028; KRT62438.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T5ZII7; -.
DR STRING; 1640513.XU10_C0028G0017; -.
DR PATRIC; fig|1640513.3.peg.2069; -.
DR Proteomes; UP000051896; 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:InterPro.
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 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 Lyase {ECO:0000313|EMBL:KRT62438.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50}.
FT DOMAIN 8..252
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 253..346
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 320
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 16
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 385 AA; 39935 MW; 7FCC96082F20C03E CRC64;
MGSAFPDPWL RLYALKANGL PPLISELPGL GYGAGAVSGG ELTLAGRAGF PVAQTALEGI
GKTPADLRRA VALAAAGTPL LWISLESAHE AAALAGLVRA ARGRRGVDPT LRLDCLVRLN
PAVRPETQHG LAVGAGGSKF GVLAAELEGV IAAGGGPDGP LRWRGIHVHV GSQLGAVDAW
RAGFRAGLSA LRLRRAALPD FDTLDAGSGF PVTTNDSPTP AHFARAAAEA LAEPGADRPL
RLAVEPGRAV VARSGWLLAR VLHVREREPR QVVLDAGMGE LIRPALYGAV HPMAALTVRG
RPVTDPRPGA AAVRVDGPIC ESTDTFGEAR LPPVRRGDLV VIGHAGAYAS AMASTYNGRP
RPPEIAWDGE RVVLLRRRGS AEALP
//
