ID A0A176KSD7_9ACTN Unreviewed; 404 AA.
AC A0A176KSD7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Decarboxylase {ECO:0000313|EMBL:OAA95268.1};
GN ORFNames=A6P39_39975 {ECO:0000313|EMBL:OAA95268.1};
OS Streptomyces sp. FXJ1.172.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=710705 {ECO:0000313|EMBL:OAA95268.1};
RN [1] {ECO:0000313|EMBL:OAA95268.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FXJ1.172 {ECO:0000313|EMBL:OAA95268.1};
RA Liu M., Liu N., Shang F., Huang Y.;
RT "Activation and identification of NC-1, a novel cryptic cyclodepsipeptide
RT from red soil-derived Streptomyces sp. FXJ1.172.";
RL Submitted (APR-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}.
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:OAA95268.1}.
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DR EMBL; LWRP01000209; OAA95268.1; -; Genomic_DNA.
DR RefSeq; WP_067057399.1; NZ_CP119133.1.
DR AlphaFoldDB; A0A176KSD7; -.
DR STRING; 710705.A6P39_39975; -.
DR OrthoDB; 9802241at2; -.
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}.
FT DOMAIN 27..267
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 268..365
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 338
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 49
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 404 AA; 44459 MW; 9293365D1E99B8EF CRC64;
MRPALFDLVG RLTDDDLPAY VYDLPALREH VHAIRAALPD RVELLYAAKA NSEPRILRTL
AGHVDGFEVA SGGELSHVRG LALDAPLAFG GPGKTPPELA RALDAEVERL HIESEHELLL
LTSLLGDRTV NVLLRVNLPV DLGQVALAMG GHPSPFGMDP AQLDHCLDLI AANARIRLRG
LHLHLASGLT APAQLALIEE VLTWAEDWAY HRGINLPEVN VGGGMGVDYT HPHKMFDWAA
FGAGLRPLLA RHPHLTLRIE PGRSITAYCG WYITQVLDIK VSRGQAFAVL RGGTHHLRTP
AAKQHDQPFE VIPDDNWPWP WDRPEARDEP VTLVGQLCTP KDVLARRVMV KRLRVGDRVA
FAMAGAYAWN ISHHAFLMHP HPTFHHVDDA EVSVTGDACA YQLS
//
