ID A0A0V0V136_9BILA Unreviewed; 1130 AA.
AC A0A0V0V136;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=ornithine decarboxylase {ECO:0000256|ARBA:ARBA00034138};
DE EC=4.1.1.17 {ECO:0000256|ARBA:ARBA00034138};
GN ORFNames=T09_8554 {ECO:0000313|EMBL:KRX57222.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX57222.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX57222.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX57222.1};
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 -!- 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:KRX57222.1}.
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DR EMBL; JYDN01000106; KRX57222.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0V136; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
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 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 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 PRINTS; PR01179; ODADCRBXLASE.
DR PRINTS; PR01182; ORNDCRBXLASE.
DR SMART; SM00332; PP2Cc; 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 PROSITE; PS00878; ODR_DC_2_1; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
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 Pyruvate {ECO:0000313|EMBL:KRX57222.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681}.
FT DOMAIN 73..473
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT ACT_SITE 1059
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 833
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 1130 AA; 128990 MW; 017BDFB3599C02DF CRC64;
MTSAKLTSSY LFFSCFNKVG RKFVRNDCSE MLCSVYAYQR RLCFTQIKYQ LTHIEVDQML
RRNEFANTMN DFIIGYHCNQ LVANAPCEDH RSEGYFQLDN SYFFGIFDGH AGTHCARTVA
SRLYDYMALP LLPEKLIREV SQGFHLPLVK MLNTSSNYVL SADLKDLHAK HLRDFSLECL
QKRDSLRNVR QAFKWAFKAL DDDLCEEAMQ MHSGSPDLSA LRCVLAGSCA CVAYVKGQDM
YIVQVGDSGA VLGVSTDEAH WTARKLNEDH TADNQKEVNR IRSEHPPGEA LTVLRCERLL
GELYPLRAFG DVRYKWPLKQ QKEIIEPYIK LRRPPMNYLT PPYLTCEPSV YYYRLTEDDK
FLILASDGLW EMVVPEAAVR FVANHAIGVE TLTPYQRLPD ATLRQILEDL RDRKRRESKR
PVDVNSATHL IRHALTSDVS DENVYAALSA TLSIPECAAR AYRDDITVTV VYFHQIQMKH
HVTAISHWTI IDDAVRDFNQ FSQLASTNGR PAGRPFKFKY FQLLTRALTY KHTSYGSHFC
DAQKRSISHR FRQRLLMASL LDFYSWNVHS LRLYRYKCAP LNPVHWKECW LLLQNDGTVL
WYNDKQFSAV KGQVNLRSAE LHFGQRALNE PSLHPPRAFT GHQDQFCYFA LVDSGPGGAV
GRRMEQWFVA KHRLDLVAFM CAIARIFKVG TEFHVFVDSS FISSTTCASD RFNNPASCCF
SGPSSDDDPL VVPCKLDSGD MYNQLKSIVG RKAEQQQIPN EPPTEEHVSK ANCLVGFDIA
VTTPLLLNNQ PAVTCEEDDS EEAFFLFDLG KLIRLHQRWI EHLPQIHPFY AVKCNDNKLL
LSLLASMGVN FDCASKNEIE TVLSIGVSPE RIIFANPCKP RSAIEYANSQ NVRYMTFDNE
QELQKIHSLY PKSELLMRIS TFNYNAVISF EKKFGCNPIT EAPELLKKAI VLGCRESSAY
TNSIANARKL FDLGNQFGCP LKLLDIGGGF SAVHENGALP FESLAMEINQ ALSFYFPSDM
NVTVIAEPGR YYAAKPFQLC TRKRKASKTY WSTVWGQTCD SLDIILKKCQ LPELFENELL
LFQNMGAYSL TVSTEFNGFS RTKVYPYIKE DDVDSFQPLF LNKANQWNSQ
//
