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
//