ID A0A0K0EJD3_STRER Unreviewed; 429 AA.
AC A0A0K0EJD3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, 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};
OS Strongyloides stercoralis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000957900.1};
RN [1] {ECO:0000313|WBParaSite:SSTP_0000957900.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A0K0EJD3; -.
DR STRING; 6248.A0A0K0EJD3; -.
DR WBParaSite; SSTP_0000957900.1; SSTP_0000957900.1; SSTP_0000957900.
DR Proteomes; UP000035681; 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:UP000035681}.
FT DOMAIN 54..291
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 307..395
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 368
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 77
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 429 AA; 47493 MW; 5710E0B4CC6F7965 CRC64;
MLDIAGNNVI FEILTDKKIA VYNGDVDNLK IAQKIASTKN TQNDDSPFIV MNLDTVIRKY
EEFRQLLPRV KPFYAVKCNN DPILLKVLSL LGTGFDCASK GEIEDVVKND LASNDNIIYA
NPCKTKNFII HARNCGIKMM TFDHEEELIK IASVYRDAEL VIRIAVSDPT AQCPLNLKFG
CDPIKEAPYL IDKASSLGVK VIGVSFHVGS GCNDPTAFKL AIQYARDLFD YGEKVGQKMF
LLDIGGGFPG HDRAKTSFST IASVIAPELD SLFPESCGVK IIAEPGRYFA ASPSSVTANV
IAKSKVSASR ITKNSDDNGK DGYMYYINDG VYGSFNCILF DHEHCYGHPL FEHEGEPTFP
TTIWGPTCDS LDQVEDLTYL RELQEGDWIH YPAMGAYTTA AASTFNGFCK PKTYYVISES
SWELLCKTI
//
