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Database: UniProt
Entry: A0A2A2SKK3_9SPHN
LinkDB: A0A2A2SKK3_9SPHN
Original site: A0A2A2SKK3_9SPHN 
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
//
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