ID C9Z012_STRSW Unreviewed; 426 AA.
AC C9Z012;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Putative siderophore biosynthesis decarboxylase {ECO:0000313|EMBL:CBG75398.1};
GN OrderedLocusNames=SCAB_84521 {ECO:0000313|EMBL:CBG75398.1};
OS Streptomyces scabiei (strain 87.22).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG75398.1, ECO:0000313|Proteomes:UP000001444};
RN [1] {ECO:0000313|EMBL:CBG75398.1, ECO:0000313|Proteomes:UP000001444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.22 {ECO:0000313|EMBL:CBG75398.1,
RC ECO:0000313|Proteomes:UP000001444};
RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA Loria R.;
RT "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT cluster that contributes to plant-microbe interactions.";
RL Mol. Plant Microbe Interact. 23:161-175(2010).
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; FN554889; CBG75398.1; -; Genomic_DNA.
DR AlphaFoldDB; C9Z012; -.
DR STRING; 680198.SCAB_84521; -.
DR KEGG; scb:SCAB_84521; -.
DR eggNOG; COG0019; Bacteria.
DR HOGENOM; CLU_026444_0_3_11; -.
DR Proteomes; UP000001444; Chromosome.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:UniProt.
DR CDD; cd06843; PLPDE_III_PvsE_like; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR022643; De-COase2_C.
DR InterPro; IPR022644; De-COase2_N.
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 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000001444}.
FT DOMAIN 60..305
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 306..403
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 376
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 82
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 426 AA; 46139 MW; 1068B4C2ECC20204 CRC64;
MNQMHPVNQM HPVNQMHPVN QKHSMNEEPS MTLPTPAVRD RALSLPSTRL PAYVYDMTAL
RDHAARVRAA LPERVELYYA AKANPEPEIL AALGPYVDGY EVASGGELAH VAQAVPGRPL
AFGGPGKTPD EIRDALERGV ARFHVESEHE LRMLGELARR AAPARPVGVL LRFNLAVADG
SLAGSALAMG GRPAPFGLDP GRAADVLRPL TDGTHPHLEP LGVHAHLASG LDAPSLLSVA
RSVVDWATAL DMPVREVNVG GGMAVDYTRP ESRFAWQEYG AGLARLTDAH PDLTLRIEPG
RALTAYCGWY ATEVLDVKRS HGEEFAVVRG GTHHLRTPAT KGHDQPCSVL AVERWPHPWP
RPSAEGERVT LAGQLCTPKD VLARHVRAPG LRAGDRVAFA LAGAYAWNIS HHDFLMHPHP
GFHIVD
//
