ID   D6AH11_STRFL            Unreviewed;       464 AA.
AC   D6AH11;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Decarboxylase {ECO:0000313|EMBL:EFE79113.2};
GN   ORFNames=SSGG_06480 {ECO:0000313|EMBL:EFE79113.2};
OS   Streptomyces filamentosus NRRL 15998.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=457431 {ECO:0000313|EMBL:EFE79113.2, ECO:0000313|Proteomes:UP000003986};
RN   [1] {ECO:0000313|Proteomes:UP000003986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 15998 {ECO:0000313|Proteomes:UP000003986};
RA   Molnar K.;
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000003986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 15998 {ECO:0000313|Proteomes:UP000003986};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Ward D., Young S., Kodira C.D., Zeng Q., Koehrsen M.,
RA   Godfrey P., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA   Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA   Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA   Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland B.L.C., Ilzarbe M.,
RA   Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces roseosporus strain NRRL 15998.";
RL   Submitted (DEC-2008) 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; DS999644; EFE79113.2; -; Genomic_DNA.
DR   AlphaFoldDB; D6AH11; -.
DR   Proteomes; UP000003986; Unassembled WGS sequence.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:UniProt.
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; 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: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   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   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50}.
FT   DOMAIN          73..307
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          311..403
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        376
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         83
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   464 AA;  48192 MW;  6ACE707C41DA4279 CRC64;
     MGAAIRDSGR MTQTTSAPHH EHGTAPPAAR LDAVVEAAVK QGLLGEGDPV AGFIDTEGVR
     ASVGALHDAF AATPGVLHTF AAKACSLIPV LRLLAGCGMG CEVASPGELR LALEAGFPAS
     RIVLDSPAKT REEIRLALAL GVAVNADSLA ELRRIDALRN PSTTSVLGLR INPQVGGGSI
     GPMSTATDTS KFGVALRDPG AREAIVEAFR ERPWLTRLHA HVGSQGCPLE LIAAGVARTY
     ELAEEINGTL GVRQITSLDI GGGLPVNFAD ETVRPTYADY VAALTAAAPG LFSGHYALVT
     EFGRSLLAKN GFIGARVEYT KDAGGRRIAL THAGAQTATR TVLMPDAWPL RIGAFGPDGV
     PKGGPVLAQD IAGPCCFAGD VVAYGRELPE LAEDDVVVLY DTGAYYFSTP WAYNSLPRPA
     VYGFRVAGPT GAVTFATVRE PQSLDSIAAE SGLAHVDALI ERDG
//