ID A0A087QUW8_APTFO Unreviewed; 460 AA.
AC A0A087QUW8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=ornithine decarboxylase {ECO:0000256|ARBA:ARBA00034138};
DE EC=4.1.1.17 {ECO:0000256|ARBA:ARBA00034138};
GN ORFNames=AS27_15670 {ECO:0000313|EMBL:KFM05022.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM05022.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM05022.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM05022.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 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|RuleBase:RU003737}.
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DR EMBL; KL225942; KFM05022.1; -; Genomic_DNA.
DR RefSeq; XP_019326626.1; XM_019471081.1.
DR AlphaFoldDB; A0A087QUW8; -.
DR STRING; 9233.A0A087QUW8; -.
DR GeneID; 103895858; -.
DR KEGG; afor:103895858; -.
DR CTD; 4953; -.
DR OrthoDB; 48358at2759; -.
DR Proteomes; UP000053286; 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; 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: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; PS00878; ODR_DC_2_1; 1.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
PE 3: Inferred from homology;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000053286}.
FT DOMAIN 45..281
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 282..387
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 360
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 69
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 460 AA; 50863 MW; 59ECD38E32FDFBB5 CRC64;
MSNFSNEEFE FTFLDEGFTA KDILDQKINE VSSSDDKDAF YVADLGDIVK KHMRWHKALP
RVTPFYAVKC NDSKAVVKTL AVLGAGFDCA SKTEIQLVQS IGVPPERIIY ANPCKQVSQI
KHAASSGVQM MTFDSEVELM KVARAHPKAK LVLRITTDDS KAVCRLSVKF GATLKASRLL
LERAKELDLV IIGVSFHVGS GCTDPETFVQ AISDARCVFD MGAELGFNMY LLDIGGGFPG
SEDVKLKFEE ITSVINPALD KYFPLDSGIN IIAEPGRYYV ASAFTLAVTI IAKKIVLKEQ
TGSDDEDDAN DKTLMYYVND GVYGSFNCIL YDHAHVKPVL QKRPKPDDSC YSCSIWGPTC
DGLDRIVERF NMPELQVGDW ILFENMGAYT VAAASTFNGF QRPTIHYVMS RPAWQLMQQI
KEQGFLAEVE EQDVASLPLS CAWESGIEYP ATCASASINV
//
