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Database: UniProt
Entry: A0A1E1F0E1_9SPHN
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ID   A0A1E1F0E1_9SPHN        Unreviewed;       397 AA.
AC   A0A1E1F0E1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=ornithine decarboxylase {ECO:0000256|ARBA:ARBA00034138};
DE            EC=4.1.1.17 {ECO:0000256|ARBA:ARBA00034138};
GN   ORFNames=SCLO_1009430 {ECO:0000313|EMBL:BAV63983.1};
OS   Sphingobium cloacae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=120107 {ECO:0000313|EMBL:BAV63983.1, ECO:0000313|Proteomes:UP000218272};
RN   [1] {ECO:0000313|EMBL:BAV63983.1, ECO:0000313|Proteomes:UP000218272}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10874 {ECO:0000313|EMBL:BAV63983.1,
RC   ECO:0000313|Proteomes:UP000218272};
RA   Ootsuka M., Nishizawa T., Ohta H.;
RT   "Complete Genome Sequence of the Nonylphenol-Degrading Bacterium
RT   Sphingobium cloacae JCM 10874T.";
RL   Submitted (OCT-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; AP017655; BAV63983.1; -; Genomic_DNA.
DR   RefSeq; WP_066517515.1; NZ_AP017655.1.
DR   AlphaFoldDB; A0A1E1F0E1; -.
DR   KEGG; sclo:SCLO_1009430; -.
DR   OrthoDB; 9802147at2; -.
DR   Proteomes; UP000218272; Chromosome.
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; 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   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   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218272}.
FT   DOMAIN          32..262
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          266..347
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   ACT_SITE        323
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         48
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   397 AA;  43171 MW;  09BEEB7054024897 CRC64;
     MHKHHSALGV ATTLKPAAPV TLIRPQAAAR AARFFAEKFP GRSLYAVKAN PSPDLIRTLF
     DGGITHFDVA SIAEVRLVAE TLGNQAKLCF MHPVKAEEAI AEAYRVHGVR TFSLDTMDEL
     EKIMRATGNA ADLELCVRLR VSSEHSELSL ASKFGAELSE TRELLMATRQ AADALGICFH
     VGSQAMSPQA YSDAIERVRA AIVDAAVTVD IIDVGGGFPS VYPGMEPPAL EAYFDAIHRG
     FESLPISYSA ELWCEPGRAL SAEYSSVIVR VERRRGTELY INDGAYGALF DAAHVGWRFP
     VDLLRDEESG AQMTGFSFYG PTCDDMDHMV GPFLLPDDVQ AGDYIEIGML GAYGAAMRTG
     FNGFTSETVV EVEDEPMATL YADRVPPRRR ATVIKIG
//
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