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Database: UniProt
Entry: A0A0V1BFT2_TRISP
LinkDB: A0A0V1BFT2_TRISP
Original site: A0A0V1BFT2_TRISP 
ID   A0A0V1BFT2_TRISP        Unreviewed;      1282 AA.
AC   A0A0V1BFT2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=ornithine decarboxylase {ECO:0000256|ARBA:ARBA00034138};
DE            EC=4.1.1.17 {ECO:0000256|ARBA:ARBA00034138};
GN   Name=Odc1 {ECO:0000313|EMBL:KRY35644.1};
GN   ORFNames=T01_4593 {ECO:0000313|EMBL:KRY35644.1};
OS   Trichinella spiralis (Trichina worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY35644.1, ECO:0000313|Proteomes:UP000054776};
RN   [1] {ECO:0000313|EMBL:KRY35644.1, ECO:0000313|Proteomes:UP000054776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS3 {ECO:0000313|EMBL:KRY35644.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) 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}.
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:KRY35644.1}.
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DR   EMBL; JYDH01000051; KRY35644.1; -; Genomic_DNA.
DR   eggNOG; KOG0700; Eukaryota.
DR   eggNOG; KOG1082; Eukaryota.
DR   Proteomes; UP000054776; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR   GO; GO:0140938; F:histone H3 methyltransferase activity; IEA:UniProt.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:UniProt.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00622; PLPDE_III_ODC; 1.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR022643; De-COase2_C.
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   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
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   Pfam; PF00481; PP2C; 1.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   PRINTS; PR01179; ODADCRBXLASE.
DR   PRINTS; PR01182; ORNDCRBXLASE.
DR   SMART; SM00332; PP2Cc; 1.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS00878; ODR_DC_2_1; 1.
DR   PROSITE; PS51746; PPM_2; 1.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   3: Inferred from homology;
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054776}.
FT   DOMAIN          58..128
FT                   /note="Pre-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50867"
FT   DOMAIN          131..250
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          248..603
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   ACT_SITE        1228
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         954
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   1282 AA;  145367 MW;  23B8972435E80E0F CRC64;
     MMMFRELVKS DITDGQEKNP IPAYNRYGSN PPDLENFVYS RSGKVEPNLP LITWRKLQGC
     KCKNGCSAKS RCPCILENKM KKPAIGLDLR LRSGYFQQGL RVRDFNIREC GPACACDMTC
     PNKQSQKPTT KKIYIEMTAA KGWGLFADSY LLPRTFICEY VGVLRVHDSD ENAPTNPYCM
     QVISKTNDMH GIYVDSQNFG NFSRFINHSC APNALAVPVL VEYEDLKLAR TCIFALQPIQ
     QDHEITIDYS YTFWNAKNAP LPFFDGHAGT HCARTVASRL YDYMALPLLP EKLIREVSQG
     FHLPLVKMLN TSSNYVLNVR QAFKWAFKAL DDDLCEEAMQ MHSGSPDLSA LRRVLAGSCA
     CVAYVKGQDM YIVQVGDSGA VLGVSTDEAH WTARKLNEDH TADNQKEVNR IRSEHPPGEA
     LTVLRCERLL GELYPLRAFG DVRYKWPLKQ QKEIIEPYIK LRRPPMNYLT PPYLTCEPSV
     YYYRLTEDDK FLILASDGLW EMVVPEAAVR FVANHAIGVE TLTPYQRLPD ATLRQILEDL
     RDRKRRESKR PVDVNSATHL IRHALTSDVS DENVYAALSA TLSIPECAAR AYRDDITVTV
     VYFHQIHMKH HVTAISHWTI IDDAVRDFNQ FSQLASTNGR PFKFKYFQLL TRAKYEHASY
     GSHFCDAQVT LFGFRQRLLM ASLLDFYSWN VHSLRLYRHK CAPLNPVRWK ECWLLLQNDG
     TVLWYNDKQF SAVKGQVNLR SAELHFGQRA LNEPGLHPPR AFTGHQDQFC YFALVDNGPG
     GAVGRRMEQW FVAKHRLDLV AFMCAIARIF KVGTEFHVFV DSSFISSTTC ASDRFNNSTS
     CCFSGPSSDD DPLVVPCKLD SGDMYNQLKS IVERKAEQQQ IPNEPPTEEH VSKANCSVGF
     DIAVTPLLNN QPAVTCEEDD SEEAFFLFDL GKLIRLHQRW IEHLPQIHPF YAVKCNDNKL
     LLSLLASMGV NFDCASKNEI ETVLSIGVSP ERIIFANPCK PRSAIEYANS QNVRYMTFDN
     EQELQKIHSL YPKSELLMRI STFNYNAVIS FEKKFGCNPI TEAPELLKKA IVLGCKVVGI
     WSGCRESSAY TNSIANARKL FDLGNQFGCP LKLLDIGGGF SAVHENGALP FESLAMEINQ
     ALSFYFPSDM NVTVIAEPGR YYAAKPFQLC TRVIAADDAD IGFMYFINDG IYGSFNCILT
     ENTVPQGQLL KKRKASKTYW STVWGQTCDS LDIILKKCQL PELFENELLL FQNMGAYSLT
     VSTEFNGFSR TKVYPYIKED DG
//
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