ID A0A2A2SKK3_9SPHN Unreviewed; 405 AA.
AC A0A2A2SKK3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Pyridoxal-dependent decarboxylase, exosortase A system-associated {ECO:0000313|EMBL:PAX09807.1};
GN ORFNames=CKY28_02700 {ECO:0000313|EMBL:PAX09807.1};
OS Sphingomonas lenta.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1141887 {ECO:0000313|EMBL:PAX09807.1, ECO:0000313|Proteomes:UP000218151};
RN [1] {ECO:0000313|Proteomes:UP000218151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1PNM-20 {ECO:0000313|Proteomes:UP000218151};
RA Feng G., Zhu H.;
RL Submitted (SEP-2017) 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:PAX09807.1}.
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DR EMBL; NSLI01000001; PAX09807.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2SKK3; -.
DR OrthoDB; 9802241at2; -.
DR Proteomes; UP000218151; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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 Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000218151}.
FT DOMAIN 38..383
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT DOMAIN 46..288
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT ACT_SITE 356
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 65
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 405 AA; 42036 MW; 7C3DDCC2032AB948 CRC64;
MKPIGPLPPE FAGRSGELVV AGRTAGEWVA EHGSPVFVYD RSVAAARVGR FRAAFPGVDL
HYAIKANPFA PLVEAMAGMV DGLDVASAGE LRLALAHKPA DAISFAGPGK RDAELEAAVA
AGVTVNLESE NEAERALAIA ERLGDTPRLA VRVNPSFELR GSGMRMGGRP SPFGVDTERV
PALVRRIVAA GADWRGFHVY AGSQTLDAQA VADTQAATVA LAARLAEEAG AEPPLVNLGG
GFGVPYFAGD AALDVERVGA ALVEALRARP GVLARSRFAI ELGRWLVAEC GVYLTRVVDR
KESGGETFLV VDGGLHHQLA ASGNFGTVVR RNYPIAVAGR METEPEEVVS VVGCLCTPLD
RLGDRVALPR ADVGDVIALF LAGAYGASAS PASFLGHPPA AEVLG
//