ID   Q58P26_ENTHI            Unreviewed;       413 AA.
AC   Q58P26; A0A175JMS4; A0A5K1VJ27; C4M0T2;
DT   26-APR-2005, integrated into UniProtKB/TrEMBL.
DT   26-APR-2005, sequence version 1.
DT   24-JAN-2024, entry version 107.
DE   RecName: Full=ornithine decarboxylase {ECO:0000256|ARBA:ARBA00034138};
DE            EC=4.1.1.17 {ECO:0000256|ARBA:ARBA00034138};
GN   Name=ODC {ECO:0000313|EMBL:AME17988.1};
GN   ORFNames=CL6EHI_100430 {ECO:0000313|EMBL:GAT94805.1};
OS   Entamoeba histolytica.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=5759 {ECO:0000313|EMBL:AAX35675.1};
RN   [1] {ECO:0000313|EMBL:AAX35675.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Prasad K.P., Madhubala R.;
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007829|PDB:4AIB}
RP   X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS) OF 1-395.
RX   PubMed=23326423; DOI=10.1371/journal.pone.0053397;
RA   Preeti, Tapas S., Kumar P., Madhubala R., Tomar S.;
RT   "Structural insight into DFMO resistant ornithine decarboxylase from
RT   Entamoeba histolytica: an inkling to adaptive evolution.";
RL   PLoS ONE 8:e53397-e53397(2013).
RN   [3] {ECO:0000313|EMBL:AME17988.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HM1:IMSS {ECO:0000313|EMBL:AME17988.1};
RA   Teran-Figueroa Y., Arteaga-Nieto P., Calvo-Mendez C.;
RT   "Ornithine decarboxylase gene of Entamoeba histolytica: Structural analysis
RT   and the protein model.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:GAT94805.1, ECO:0000313|Proteomes:UP000078387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HM1:IMSS clone 6 {ECO:0000313|EMBL:GAT94805.1,
RC   ECO:0000313|Proteomes:UP000078387};
RA   Mukherjee Avik.K., Izumyama S., Nakada-Tsukui K., Nozaki T.;
RT   "First whole genome sequencing of Entamoeba histolytica HM1:IMSS-clone-6.";
RL   Submitted (MAY-2016) 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}.
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DR   EMBL; AY929249; AAX35675.1; -; Genomic_DNA.
DR   EMBL; KT716494; AME17988.1; -; Genomic_DNA.
DR   EMBL; BDEQ01000001; GAT94805.1; -; Genomic_DNA.
DR   PDB; 4AIB; X-ray; 2.87 A; A/B/C/D=1-395.
DR   PDBsum; 4AIB; -.
DR   AlphaFoldDB; Q58P26; -.
DR   SMR; Q58P26; -.
DR   STRING; 5759.Q58P26; -.
DR   EnsemblProtists; GAT94805; GAT94805; CL6EHI_100430.
DR   EnsemblProtists; rna_EHI_100430-1; rna_EHI_100430-1; EHI_100430.
DR   VEuPathDB; AmoebaDB:EHI5A_035410; -.
DR   VEuPathDB; AmoebaDB:EHI7A_108630; -.
DR   VEuPathDB; AmoebaDB:EHI8A_013650; -.
DR   VEuPathDB; AmoebaDB:EHI_100430; -.
DR   VEuPathDB; AmoebaDB:KM1_043220; -.
DR   HOGENOM; CLU_026444_1_1_1; -.
DR   InParanoid; Q58P26; -.
DR   OMA; SFFVCDL; -.
DR   OrthoDB; 48358at2759; -.
DR   BRENDA; 4.1.1.17; 2080.
DR   Proteomes; UP000078387; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004586; F:ornithine decarboxylase activity; IMP:CACAO.
DR   GO; GO:0033387; P:putrescine biosynthetic process from ornithine; IBA:GO_Central.
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; IPR022657; De-COase2_CS.
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.
DR   PROSITE; PS00879; ODR_DC_2_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4AIB}; Lyase {ECO:0000313|EMBL:AME17988.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50}.
FT   DOMAIN          36..263
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          264..361
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   ACT_SITE        334
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         57
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   413 AA;  46432 MW;  BEB7F00C87870E45 CRC64;
     MKQTSLEVKE FALNLISQFE PENQPLGFWI FDTEGVEKAV ERWKKNMPTV RPCFAVKCNP
     EPHLVKLLGE LGCGFDCASL NEIKEVLDLG FNPEDITYSQ TFKPYNQLIE ASHLGINHTI
     VDSIDEVQKI AKYAPKMGIM IRIMENDTSA GHVFGEKFGL HDDEVEIVLK EIKDKGLNLD
     GVHFHVGSDS HNSEVFTKAL TKARNTVTLA EQFGMKPYLI DIGGGFSQVA PFEEFAATIE
     KTIKELEFPE RTRFIAEPGR YMASNAFHLV SSLHGKRVRI QNGKKQIEYT SGDGLHGSFG
     CCIWFEKQKS CECITQKVNE NTKMYESIIY GPSCNGSDKV ATQELPEMEP GKDWLLFPNM
     GAYTISMATN FNGFEERNHV IYTLPLKSTK IIQIPKSIEC NSVPSLNGIP HYA
//