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
//