ID   A0A1H7X5H7_9ACTN        Unreviewed;       458 AA.
AC   A0A1H7X5H7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:SEM29096.1};
GN   ORFNames=SAMN05660976_04763 {ECO:0000313|EMBL:SEM29096.1};
OS   Nonomuraea pusilla.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=46177 {ECO:0000313|EMBL:SEM29096.1, ECO:0000313|Proteomes:UP000198953};
RN   [1] {ECO:0000313|EMBL:SEM29096.1, ECO:0000313|Proteomes:UP000198953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43357 {ECO:0000313|EMBL:SEM29096.1,
RC   ECO:0000313|Proteomes:UP000198953};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOBF01000011; SEM29096.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7X5H7; -.
DR   STRING; 46177.SAMN05660976_04763; -.
DR   Proteomes; UP000198953; Unassembled WGS sequence.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:UniProt.
DR   GO; GO:0006596; P:polyamine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
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   PANTHER; PTHR43727; DIAMINOPIMELATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43727:SF3; DIAMINOPIMELATE DECARBOXYLASE; 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:UP000198953}.
FT   DOMAIN          66..300
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          303..396
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   ACT_SITE        369
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         76
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   458 AA;  47438 MW;  99A81F4C39FE458A CRC64;
     MIQSSATLAP APTSRAARVA PVVRHAVRTG ALGAEHPVAG FVDVEGVRES VADLQAAFDA
     AASGAAPGVL HTFAAKAASL IPVLRLLADS GMGCEVASPG ELRIALDAGF APSAIVFDSP
     AKTRDELRQA LALGVAVNAD SFSELRRVDE LRPEGCASVL GLRVNPQVGT GSIGAMSTAT
     ATSKFGVPLR DPGARERVVR AFAERPWLTR LHAHVGSQGC PIELIAAGIA ETYRLAEEIN
     ATLGVRQVTS IDIGGGLPVN FDGDEVRPTF AEYARALREA VPGLFDGSYA LVTEFGRSLL
     AKNGFIAALV EYTKDAGGRR VAITHAGAQV ATRTVLMPDA WPLRVGAFDA DGLPKDAPVL
     PQDVAGPCCF AGDVVAHARE LPELEEGDIV VLYDTGAYYF STPWAYNSLP YPAVHGYTVS
     GGGEVRLAPV RPAQTLDEIA AASGLAHAGA LTGLLAPA
//