ID A0A0V0XCH7_9BILA Unreviewed; 630 AA.
AC A0A0V0XCH7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=ornithine decarboxylase {ECO:0000256|ARBA:ARBA00034138};
DE EC=4.1.1.17 {ECO:0000256|ARBA:ARBA00034138};
GN Name=EHMT2 {ECO:0000313|EMBL:KRX85331.1};
GN ORFNames=T06_11096 {ECO:0000313|EMBL:KRX85331.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX85331.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX85331.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX85331.1};
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:KRX85331.1}.
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DR EMBL; JYDK01000002; KRX85331.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0XCH7; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00622; PLPDE_III_ODC; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 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 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 PRINTS; PR01179; ODADCRBXLASE.
DR PRINTS; PR01182; ORNDCRBXLASE.
DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS00878; ODR_DC_2_1; 1.
PE 3: Inferred from homology;
KW Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673}.
FT DOMAIN 262..495
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 498..586
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 559
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 285
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 630 AA; 71341 MW; 42CF974832633F1A CRC64;
MRFRQQLLMA SLLDFYSWNV HSLRLYRYKC APLNPVHWKE CWLLLQNDGT VLWYNDKQFS
AVKGQVNLRS AELHFGQRAL NEPSLHPPRA FTGHRDQFCY FALVDSGPGN AVGRRMEQWF
VAKHRLDLVA FMCAIARIFK VGTEFHVFVD SSFISSTTCA SDRFNNPASC CFSGPSSDDD
PLVVPCKLDS GDMYNQLKSI VGRKAEQQQI PNEPPTEEHV SKANCLVGFD IAVTTPLLLN
NQPAVACEED DSEEAFFLFD LGKLIRLHQR WIEHLPQIHP FYAVKCNDNK LLLSLLASMG
VNFDCASKNE IETVLSIGVS PERIIFANPC KPRSAIEYAN SQNVRYMTFD NEQELQKIHS
LYPKSELLMR ISTFNYNAVI SFEKKFGCNP ITEAPELLKK AIVLGCKVVG IWFGCRESSA
YTNSIANARK LFDLGNQFGC PLKLLDIGGG FSAVHENGAL PFESLAMEIN QALSFYFPSD
MNVTVIAEPG RYYAAKPFQL CTRVIAADDA DIGFMYFIND GIYGSFNCIL TENTVPQGQL
LKKRKTSKTY WSTVWGQTCD SLDIILKKCQ LPELFENELL LFQNMGAYSL TVSTEFNGFS
RTKVYPYIKE DDVDSFQPLF LNKANQWNSQ
//
