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Database: UniProt
Entry: A0A0M9A5K4_9HYME
LinkDB: A0A0M9A5K4_9HYME
Original site: A0A0M9A5K4_9HYME 
ID   A0A0M9A5K4_9HYME        Unreviewed;       470 AA.
AC   A0A0M9A5K4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=ornithine decarboxylase {ECO:0000256|ARBA:ARBA00034138};
DE            EC=4.1.1.17 {ECO:0000256|ARBA:ARBA00034138};
GN   ORFNames=WN51_11650 {ECO:0000313|EMBL:KOX76319.1};
OS   Melipona quadrifasciata.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Melipona.
OX   NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX76319.1, ECO:0000313|Proteomes:UP000053105};
RN   [1] {ECO:0000313|EMBL:KOX76319.1, ECO:0000313|Proteomes:UP000053105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0111107301 {ECO:0000313|EMBL:KOX76319.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KOX76319.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Melipona quadrifasciata.";
RL   Submitted (JUL-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}.
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DR   EMBL; KQ435750; KOX76319.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M9A5K4; -.
DR   STRING; 166423.A0A0M9A5K4; -.
DR   OrthoDB; 48358at2759; -.
DR   Proteomes; UP000053105; 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: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   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:UP000053105}.
FT   DOMAIN          42..275
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          276..374
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   ACT_SITE        347
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         65
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   470 AA;  51685 MW;  E295B5B15D44F9BD CRC64;
     MKVTNLDERI HVLDSASNVM TVIKDIALSG LQEEAFYVLD IGDIVCKHQI WKEKMPRVSP
     YYAVKCNDNL IVIEVLAALG IGFDCASKSE INKVLSVGVD SSRIIFANPA KPASHIRHAA
     AVGVDAMTAD NESELHKIKK LHPSAKVVIR IRCDAEVAQC QLGMKFGCDP IYEAPNLLRL
     ARVLGLNVIG ISFHVGSGCR DPPVFYRAIR ESKILFDLAT DLGFKPYLLD IGGGYPGDKG
     TSIDKIANVI NEALDEFFNT DAVHIIAEPG RFYVASAFTL ATSIHSKRSV RGDENSPNSV
     THNMYYINDG VYGSFNCLLY DHQHVTPIPL KKGCGKIYPS SIWGPTCDGL DQVVENIMLH
     DMELGDWIIF ENMGAYTLPV ASPFNGFPVP KVHIVADENI WHLLKDALPL TEDHFVIGNT
     PANLRLGLGI SGTDTNAWRN SNIELTSSEI LADVTNPPTA YIYDYLEVDL
//
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