ID A0A1S3W791_ERIEU Unreviewed; 563 AA.
AC A0A1S3W791;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Ornithine decarboxylase {ECO:0000256|ARBA:ARBA00039485};
DE EC=4.1.1.17 {ECO:0000256|ARBA:ARBA00034138};
GN Name=LOC103110667 {ECO:0000313|RefSeq:XP_016042220.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016042220.1};
RN [1] {ECO:0000313|RefSeq:XP_016042220.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the first and rate-limiting step of polyamine
CC biosynthesis that converts ornithine into putrescine, which is the
CC precursor for the polyamines, spermidine and spermine. Polyamines are
CC essential for cell proliferation and are implicated in cellular
CC processes, ranging from DNA replication to apoptosis.
CC {ECO:0000256|ARBA:ARBA00037173}.
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 -!- 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|RuleBase:RU003737}.
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DR RefSeq; XP_016042220.1; XM_016186734.1.
DR eggNOG; KOG0622; Eukaryota.
DR InParanoid; A0A1S3W791; -.
DR OrthoDB; 48358at2759; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:InterPro.
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; 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:SF42; ORNITHINE DECARBOXYLASE; 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; PS00879; ODR_DC_2_2; 1.
PE 3: Inferred from homology;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721}.
FT DOMAIN 153..388
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 389..489
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
SQ SEQUENCE 563 AA; 63136 MW; 6964D49986D4A40A CRC64;
MNCGGLAKRK PPFIFACNNL RADKYVSDVH KSTYCSPASS SAPSNGSYQN HYQSLELAKS
CYFSKHSTLL TEMTDIVISM FNSSFQELEV PGDIAIPSLC CISEEHQITI NNFSNDEFDC
HFLNEGFTAK DILHQKINEV SSSDDKDVYV VDLGDILKKY LRWLKILPQV TPFYAVKCKD
SRTIVKTLAA VGAGFQSSRT EIQMVXSLGV PPERIIYANP CKQVSQIKYA ANNGIQMMTF
DSVVKLMKVA RARPKAKLVL QIATDDSKAV YCLSVKFGAT LKTSRLLLDR AKELNIDVIS
VSFHSGSGCT DHETFVPAIS DAWYVFDVGA EVLFNMYLLD IGGGFPGSED VKLKYEEITS
VINPALDKYF PSDWGVRIIA XPSRYYVASA FTLAVNIIAK KLVLKKGSDD EDESSEQTFM
YYVNDGSFNC ILYDHVHVKP LLQKRPKPDA KYYSSSIWGP MYDSLDRIAE LCDLPEMHLV
DWMLFQNMGA YTVAAASTFN RFQRLTIYYV LSQPMWQLMQ QIQSHDFPPE VEEQDISALP
MSCAWESGIK RHPAACASAS INM
//