ID E1MF94_9ACTO Unreviewed; 538 AA.
AC E1MF94;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:EFN92828.1};
DE EC=4.1.1.20 {ECO:0000313|EMBL:EFN92828.1};
GN Name=lysA {ECO:0000313|EMBL:EFN92828.1};
GN ORFNames=HMPREF9278_2080 {ECO:0000313|EMBL:EFN92828.1};
OS Mobiluncus mulieris FB024-16.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Mobiluncus.
OX NCBI_TaxID=866770 {ECO:0000313|EMBL:EFN92828.1, ECO:0000313|Proteomes:UP000004387};
RN [1] {ECO:0000313|EMBL:EFN92828.1, ECO:0000313|Proteomes:UP000004387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB024-16 {ECO:0000313|EMBL:EFN92828.1,
RC ECO:0000313|Proteomes:UP000004387};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (AUG-2010) 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:EFN92828.1}.
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; AEGV01000035; EFN92828.1; -; Genomic_DNA.
DR RefSeq; WP_004018076.1; NZ_AEGV01000035.1.
DR AlphaFoldDB; E1MF94; -.
DR Proteomes; UP000004387; 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 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; IPR022657; De-COase2_CS.
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; 2.
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.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Lyase {ECO:0000313|EMBL:EFN92828.1};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50}.
FT DOMAIN 74..221
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 249..360
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 361..461
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 433
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 103
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 538 AA; 57397 MW; D97F0ACAEECDFDC7 CRC64;
MSQDSLAPED PAWLAPGDPG LQALAAPEPS ERPDMWPAGL NRAASGELRI HGQNLVALLA
QQHGRTPVFI MDMDDFRKRA RAWREAFTKT FGKGNAQVYY AGKAFLCLGL ARVATAQGLG
LDTASPGELT LALASGIDPL RVGLHGNGKS AALLHQAVSA GIGRIIIDSL AEIPRLQRVL
DALPQAATVP VMIRLTTGVH AGGHEYIATA HEDQKFGLSL EPGTHAGLCP DDSDWDGCYV
VSPADSPALA AVKLILADDR LELVGLHSHI GSQISAFAGF TAAAQKIIEF RGAVARETGY
LVPEIDLGGG YGVAYTAATP PGMAPHEIAE KLYRAVQDAC EQHDQPLPAV SVEPGRSLVA
PTTITLYRVL NIKDQPVGTR LDGSVVYRRY VAVDGGMSDN IRPALYDAHY TATLANRLSA
APLVATRVVG THCESGDIVV RNVALPADLT EGDLLAVPMT GAYGWSMSSN YNWFTRPGVL
GVWQVSGDDT DSASRGAIPE TKETWRADWL ISGENAEEML AHHDPAFRKY LWTHPVIP
//
