ID   D9VRL3_9ACTN            Unreviewed;       487 AA.
AC   D9VRL3;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   SubName: Full=Orn/DAP/Arg decarboxylase 2 {ECO:0000313|EMBL:EFL18733.1};
GN   ORFNames=SSNG_05985 {ECO:0000313|EMBL:EFL18733.1};
OS   Streptomyces sp. C.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL18733.1, ECO:0000313|Proteomes:UP000005763};
RN   [1] {ECO:0000313|EMBL:EFL18733.1, ECO:0000313|Proteomes:UP000005763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C {ECO:0000313|EMBL:EFL18733.1,
RC   ECO:0000313|Proteomes:UP000005763};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces sp. strain C.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR   EMBL; GG657750; EFL18733.1; -; Genomic_DNA.
DR   RefSeq; WP_007267658.1; NZ_GG657750.1.
DR   AlphaFoldDB; D9VRL3; -.
DR   STRING; 253839.SSNG_05985; -.
DR   eggNOG; COG0019; Bacteria.
DR   HOGENOM; CLU_042407_0_0_11; -.
DR   Proteomes; UP000005763; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_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; 1.
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   4: Predicted;
FT   DOMAIN          62..271
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
SQ   SEQUENCE   487 AA;  51756 MW;  D9F094942A350CC7 CRC64;
     MSDAPLYLQP RLSAAMASLL RSGSFLQSLV DGLGSPLNVL LPDQIALNLG AFRSVLRGHQ
     LSGRVFFAHK ANRSSALVRR LTTTEAGLDA ASLAELQHAL GSGFTGDKVM VTGPKDPEFL
     WLAARAGAIV NADGIGELVE AAGFVRSHGL PRLRILLRLS EFETSGARTL SRTSRFGTSF
     KALGRLLDTL ESFKEELEPI GVGYHLDTTG LDEKATALEG CLIAVEELRL RGFGPRAVDV
     GGGFGISYLA HADQWERYTS ALTQAVLGKH TPMTWGGHGY GLRAEKGTLK GALGLYPAYR
     PVAGAGYLDE LLACPAPGLG RPLGTLLLEG LCDLYAEPGR ALVDQCGVTL GKVLEVRASG
     GGPAMVRLAM NSGDVGLEEH GILVDPVLLR RDGAPGVGRP VGVHLAGNLC LESDLITRRT
     VFLPDLPQPG DLLAFPNTAG YCMDFTATAA QQQPSARRVA VREEGGSWRW CLDEKYWPVL
     DTGGQRA
//