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Database: UniProt
Entry: DCOR_HAEIN
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ID   DCOR_HAEIN              Reviewed;         720 AA.
AC   P44317;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Ornithine decarboxylase;
DE            EC=4.1.1.17;
GN   Name=speF; OrderedLocusNames=HI_0591;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC       {ECO:0000305}.
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DR   EMBL; L42023; AAC22248.1; -; Genomic_DNA.
DR   PIR; F64079; F64079.
DR   RefSeq; NP_438749.1; NC_000907.1.
DR   AlphaFoldDB; P44317; -.
DR   SMR; P44317; -.
DR   STRING; 71421.HI_0591; -.
DR   EnsemblBacteria; AAC22248; AAC22248; HI_0591.
DR   KEGG; hin:HI_0591; -.
DR   PATRIC; fig|71421.8.peg.614; -.
DR   eggNOG; COG1982; Bacteria.
DR   HOGENOM; CLU_014292_3_0_6; -.
DR   OrthoDB; 9761189at2; -.
DR   PhylomeDB; P44317; -.
DR   BioCyc; HINF71421:G1GJ1-603-MONOMER; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR   GO; GO:0004586; F:ornithine decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd00615; Orn_deC_like; 1.
DR   Gene3D; 3.40.50.220; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.90.100.10; Orn/Lys/Arg decarboxylase, C-terminal domain; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR027568; ODC_inducible.
DR   InterPro; IPR005308; OKR_de-COase_N.
DR   InterPro; IPR011193; Orn/lys/arg_de-COase.
DR   InterPro; IPR000310; Orn/Lys/Arg_deCO2ase_major_dom.
DR   InterPro; IPR027464; Ornithine_deCO2ase_N.
DR   InterPro; IPR008286; Prn/Lys/Arg_de-COase_C.
DR   InterPro; IPR036633; Prn/Lys/Arg_de-COase_C_sf.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR04301; ODC_inducible; 1.
DR   PANTHER; PTHR45229:SF3; BIODEGRADATIVE ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR45229; CONSTITUTIVE ORNITHINE DECARBOXYLASE; 1.
DR   Pfam; PF01276; OKR_DC_1; 1.
DR   Pfam; PF03711; OKR_DC_1_C; 1.
DR   Pfam; PF03709; OKR_DC_1_N; 1.
DR   PIRSF; PIRSF009393; Orn_decarb; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF55904; Ornithine decarboxylase C-terminal domain; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00703; OKR_DC_1; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..720
FT                   /note="Ornithine decarboxylase"
FT                   /id="PRO_0000201136"
FT   MOD_RES         354
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   720 AA;  82027 MW;  9F89EFD178752F5F CRC64;
     MPNLKIAYSP KVEQYFSTNR ELVEIAKTDF TDVAAIVLSS SDVGEYLDRI KATKFDVPVF
     IVQTDEQQVD PKFYDSIYHI QDLNGYDIKL YSRQIETAAK LYEEKMLPPF FKMLSEYVEM
     GNIAFDCPGH QGGQYYRKHP AGRFLYDFYG ENIFRSDICN ADVKLGDLLI HEGAACDAQK
     YAAQVFNADK TYFVLNGTSS SNKVALNAVL APGDLVLFDR NNHKSNHHGA LIQAGATPIY
     LETARNPFGF IGGIDSHCFE EDYLKSLIKE VAPEKLNQKR PFRLAVIQLG TYDGTIYNAR
     QVVDKIGHLC DYILFDSAWV GYEQFIPMMK DCSPLLLELN ENDPGILVTQ SVHKQQAGFS
     QTSQIHKKDK HIKGQDRYVN HKRFNNAFML HASTSPFYPL FATLDVNAKI QGSEAGRRLW
     HECVKVGIEA RKLVLNHCEL IRPFIPTTIK GKKWQDYDTE EIATNLEFFK FHPTDTWHKF
     EGYADEQYFV DPCKFLLTTP GISLETGEYE EFGVPATILA NYLRENGIIP EKCDLNSILF
     LLTPAETITK MQTLVAQIAL FEKHIKQDSL LKYVLPTVYK NNEDRYKGYT IRQLCQEMHD
     LYVSRNVKQL QKDLFRKATL PEYVLNPHDA NIELIRNKVE LVPLTDIVGR VAAEGALPYP
     PGVLCVVPGE KWSTTAHQYF LALEEGINTL PGFAPEIQGV YLQKDPDGRT RAYGYVLTDY
//
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