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
//