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Database: UniProt
Entry: A0A0V1P3A4_9BILA
LinkDB: A0A0V1P3A4_9BILA
Original site: A0A0V1P3A4_9BILA 
ID   A0A0V1P3A4_9BILA        Unreviewed;      1478 AA.
AC   A0A0V1P3A4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=ornithine decarboxylase {ECO:0000256|ARBA:ARBA00034138};
DE            EC=4.1.1.17 {ECO:0000256|ARBA:ARBA00034138};
DE   Flags: Fragment;
GN   Name=Odc1 {ECO:0000313|EMBL:KRZ90526.1};
GN   ORFNames=T08_14220 {ECO:0000313|EMBL:KRZ90526.1};
OS   Trichinella sp. T8.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ90526.1, ECO:0000313|Proteomes:UP000054924};
RN   [1] {ECO:0000313|EMBL:KRZ90526.1, ECO:0000313|Proteomes:UP000054924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS272 {ECO:0000313|EMBL:KRZ90526.1};
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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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   -!- SIMILARITY: Belongs to the PP2C family.
CC       {ECO:0000256|RuleBase:RU003465}.
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:KRZ90526.1}.
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DR   EMBL; JYDM01000055; KRZ90526.1; -; Genomic_DNA.
DR   STRING; 92180.A0A0V1P3A4; -.
DR   Proteomes; UP000054924; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:UniProt.
DR   GO; GO:0140938; F:histone H3 methyltransferase activity; IEA:UniProt.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
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; IPR000222; PP2C_BS.
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; PS01032; PPM_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   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW   ECO:0000256|RuleBase:RU003465};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054924}.
FT   DOMAIN          124..194
FT                   /note="Pre-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50867"
FT   DOMAIN          197..316
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          409..809
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   ACT_SITE        1407
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         1133
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   NON_TER         1478
FT                   /evidence="ECO:0000313|EMBL:KRZ90526.1"
SQ   SEQUENCE   1478 AA;  168554 MW;  58E6B3CB7C4FC8D8 CRC64;
     MRTKIMARLQ GSVDSIFIYV RLLFVQWVSK DERREKRMHI FQNENEFCLK VIFEIFRNYR
     RNLSVKMMMF RELVKSDIAN GQEKNPIPAY NRYGSNPPNL ENFVYSRSGK VEPNLPLLSW
     GKLQGCKCKN GCSARSRCPC ILENKTKKPA IGLDLRLRSA YFRPGLRVRD FNIRECGPAC
     ACDVTCPNKQ SQKPTTKKFY IEMTAAKGWG LFADSYLLPR TFICEYAGVL RVHDSDENAP
     ANPYCMQVIS KTDDMHGIYV DSQNFGNFSR FINHSCAPNA FAVPVLVEYE DLKLARTCIF
     ALRPIQQDHE ITIDYSYTFW NTKNAPLPCM CRSPLCRYSA DPYPPLPPLP PMDQTLPELP
     PNDCSEMLCS VYAYQRRLCF TQIKYQLTHI EVDQMLRRNE FANTMNDFII GYHCNQLVAN
     APCEDHRSEG YFQLDNSYFF GIFDGHAGTH CARTVASRLY DYMALPLLPE KLIREVSQGF
     HLPLVKMLNT SSNYVLSADL KDLHAKHLRD FSLECLQKRD SLRNVRQAFK WAFKALDDDL
     CEEAMQMHSG SPDLSALRCV LAGSCACVAY VKGQDMYIVQ VGDSGAVLGV STDEAHWTAR
     KLNEDHTADN QKEVNRIRSE HPPGEALTVL RCERLLGELY PLRAFGDVRY KWPLKQQKEI
     IEPYIKLRRP PMNYLTPPYL TCEPSVYYYR LTEDDKFLIL ASDGLWEMVV PEAAVRFVAN
     HAIGVETLTP YQRLPDATLR QILEDLRDRK RRESKRPVDV NSATHLIRHA LTSDVSDENV
     YAALSATLSI PECAARAYRD DITVTVVYFH QIQMKHHVTA ISHWTIIDDA VRDFNQFSQL
     ASTNGRPAGR FRQRLLMASL LDFYSWNVHS LRLYRYKCAP LNPVHWKECW LLLQNDGTVL
     WYNDKQFSAV KGQVNLRSAE LHFGQRALNE PSLHPPRAFT GHQDQFCYFA LVDSGPGGAV
     GRRMEQWFVA KHRLDLVAFM CAIARIFKVG TEFHVFVDSS FISSTTCASD RFNNPASCCF
     SGPSSDDDPL VVPCKLDSGD MYNQLKSIVG RKAEQQQIPN EPPTEEHVSK ANCLDGFDIA
     IRTPLLLNNQ PAVTCEEDDS EEAFFLFDLG KLIRLHQRWI EHLPQIHPFY AVKCNDNKLL
     LSLLASMGVN FDCASKNEIE TVLSIGVSPE RIIFANPCKP RSAIEYANSQ NVRYMTFDNE
     QELQKIHSLY PKSELLMRIS TFNYNAVISF EKKFGCNPIT EAPELLKKAI VLGCKVVGIW
     SGCRESSAYT NSIANARKLF DLGNQFGCPL KLLDIGGGFS AVHENGALPF ESLAMEINQA
     LSFYFPSDMN VTVIAEPGRY YAAKPFQLCT RVIAADDADI GFMYFINDGI YGSFNCILTE
     NTVPQGQLLK KRKASKTYWS TVWGQTCDSL DIILKKCQLP ELFENELLLF QNMGAYSLTV
     STEFNGFSRT KVYPYIKEDD VDSFQPLFLN KANQWNSQ
//
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