ID A0A1S2PZV8_9ACTN Unreviewed; 404 AA.
AC A0A1S2PZV8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Decarboxylase {ECO:0000313|EMBL:OIJ98895.1};
GN ORFNames=BIV23_29420 {ECO:0000313|EMBL:OIJ98895.1};
OS Streptomyces monashensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1678012 {ECO:0000313|EMBL:OIJ98895.1, ECO:0000313|Proteomes:UP000179642};
RN [1] {ECO:0000313|EMBL:OIJ98895.1, ECO:0000313|Proteomes:UP000179642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 1 {ECO:0000313|EMBL:OIJ98895.1,
RC ECO:0000313|Proteomes:UP000179642};
RA Lee L.-H., Ser H.-L., Law J.W.-F.;
RT "Genome sequence of Streptomyces sp. MUSC 1.";
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}.
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:OIJ98895.1}.
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DR EMBL; MLYO01000053; OIJ98895.1; -; Genomic_DNA.
DR RefSeq; WP_071384016.1; NZ_MLYO01000053.1.
DR AlphaFoldDB; A0A1S2PZV8; -.
DR OrthoDB; 9802241at2; -.
DR Proteomes; UP000179642; 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 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; IPR002433; Orn_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 PRINTS; PR01182; ORNDCRBXLASE.
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:UP000179642}.
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; 44420 MW; E9FC40232FEA86C5 CRC64;
MRPATLDRVV RLTDDDLPAY LYDLPALREH VRAIRAALPD RVELLYAAKA NADPRILRTL
AGHVDGFEVA SGGELSHVRG LLPEAPTAFG GPGKTPKELA RALDAGVERL HVESEHELLL
LAGLLAGRTA DVLLRVNLPV DLGQVALAMG GQPSPFGMDP GRLDRCLELI ASDPRIRLRG
LHLHLASGLT AAAQLALVDE VLTWAEDWAH HHGIDLCEVN VGGGMGVDYA HPHRKFDWPA
FGAGLRPLLA RHPHLTLRIE PGRSVTAYCG WYVTQVLDIK FSRRQAFAVL RGGTHHLRTP
AAKQHDQPFE VIPDDDWPWP WDRPEARDEP VTLVGQLCTP KDVLARRVTV KRLRVGDRVA
FAMAGAYAWN ISHHAFLMHP HPTFHHVEDA EPSATGGAYA RQTP
//
