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Database: UniProt
Entry: D0ENK2_SPOLT
LinkDB: D0ENK2_SPOLT
Original site: D0ENK2_SPOLT 
ID   D0ENK2_SPOLT            Unreviewed;       448 AA.
AC   D0ENK2;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=ornithine decarboxylase {ECO:0000256|ARBA:ARBA00034138};
DE            EC=4.1.1.17 {ECO:0000256|ARBA:ARBA00034138};
OS   Spodoptera litura (Asian cotton leafworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Amphipyrinae; Spodoptera.
OX   NCBI_TaxID=69820 {ECO:0000313|EMBL:ACW82828.1};
RN   [1] {ECO:0000313|EMBL:ACW82828.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Choi S.-Y., Park H.Y., Paek A., Kim G.S., Jeong S.E.;
RT   "Insect's ornithine decarboxylase (ODC) complements SPE1 knock-out of yeast
RT   Saccharomyces cerevisiae.";
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-ornithine = CO2 + putrescine; Xref=Rhea:RHEA:22964,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:46911,
CC         ChEBI:CHEBI:326268; EC=4.1.1.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00034037};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR600183-50};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC       L-ornithine pathway; putrescine from L-ornithine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00034115}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       {ECO:0000256|ARBA:ARBA00008872, ECO:0000256|RuleBase:RU003737}.
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DR   EMBL; GQ861425; ACW82828.1; -; mRNA.
DR   AlphaFoldDB; D0ENK2; -.
DR   BRENDA; 4.1.1.17; 9768.
DR   GO; GO:0004586; F:ornithine decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00622; PLPDE_III_ODC; 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; 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; IPR002433; Orn_de-COase.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   PANTHER; PTHR11482; ARGININE/DIAMINOPIMELATE/ORNITHINE DECARBOXYLASE; 1.
DR   PANTHER; PTHR11482:SF6; ORNITHINE DECARBOXYLASE 1-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.
DR   PROSITE; PS00878; ODR_DC_2_1; 1.
DR   PROSITE; PS00879; ODR_DC_2_2; 1.
PE   2: Evidence at transcript level;
KW   Lyase {ECO:0000313|EMBL:ACW82828.1};
KW   Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50}.
FT   DOMAIN          41..276
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          277..373
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   ACT_SITE        346
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         65
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   448 AA;  48431 MW;  DF9FF935F2D7B285 CRC64;
     MKVVEEEQLI TVMDGPWSTT DLIREIVESG TQEDPFYVMD LGEVVARYHR WKELMPRVEP
     FYAVKCNDDK LLVSTLAALG TGFDCASKAE IELVTSIGVA PDRIIFANPA KMASHIRFAS
     AVGVDVMTFD SETELMKIKQ YMPHAQLVIR IRCDAASAQC PLGIKFGCDP VTEAPRLLKL
     AAVFGLDVIG VSFHVGSGAS ETDVYARAIA LSRALFLVGH NVGHKAMRIL DIGGGFPGGT
     HTSIQEVSAV INSALEEHFP ERSVRVIAEP GRYFAAAAYT LAAMVHAKRE VTSKECADET
     HTMYFINDGV YGSFNCVLYD HQHVVAEPLN DNGSVPAPCS VWGPTCDGLD CVLPATRLPS
     LAIGDWLIFR DMGAYTLPVA SPFNGFPVPT VRPVVDARLA CILKELRPLS ASQFAAGRVV
     ESPALGTSRP ASRAASPCRA VFVECALK
//
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