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P27116 (DCOR_LEIDO) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ornithine decarboxylase

Short name=ODC
EC=4.1.1.17
OrganismLeishmania donovani
Taxonomic identifier5661 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmania

Protein attributes

Sequence length707 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

L-ornithine = putrescine + CO2.

Cofactor

Pyridoxal phosphate.

Pathway

Amine and polyamine biosynthesis; putrescine biosynthesis via L-ornithine pathway; putrescine from L-ornithine: step 1/1.

Sequence similarities

Belongs to the Orn/Lys/Arg decarboxylase class-II family.

Ontologies

Keywords
   Biological processPolyamine biosynthesis
   LigandPyridoxal phosphate
   Molecular functionDecarboxylase
Lyase
Gene Ontology (GO)
   Biological processpolyamine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionornithine decarboxylase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 707707Ornithine decarboxylase
PRO_0000149901

Sites

Active site6341Proton donor; shared with dimeric partner By similarity

Amino acid modifications

Modified residue2881N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P27116 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: EBDF14F791EC572D

FASTA70777,397
        10         20         30         40         50         60 
MGDHDVALCH VSRYNHANYW AFVPLPTVSD DTGCDSLHHD SASERIRMAP PASASKAGAA 

        70         80         90        100        110        120 
EERLHPYERR LLDQYQIHLQ PANRNPLSRA DSAAGREETA QTPAQVQMVP VVAVADSTSD 

       130        140        150        160        170        180 
QHASVASSQD LVDLFFLEGS QAVDGLCFSP YPIYGWRTAE ERRAAVCEVF KTYNVVTRLP 

       190        200        210        220        230        240 
ASPAALAAAQ RRYSRHRHSA IAPINKSAIE TREQYWRRLS NLYTQKGVKD AASAADAAAT 

       250        260        270        280        290        300 
TATNGAVPAA PAYEPEDPFY IIDLGRVVEQ MARWRHELPM VRPYFAVKSN PQPAVLEVLS 

       310        320        330        340        350        360 
ALGAGFDCAS KEEIHMVLGR QLVASPDDII FANPCKQLGD LREAQACGVT YVTVDNPLEM 

       370        380        390        400        410        420 
EKISRLMPSA HAIIRIKTND SKAQCSFSTK FGAPLEDVEG LLEAARQFNV TVCGVSFHVG 

       430        440        450        460        470        480 
SGNDDQSAYV SAVRDAYQVF QQAVQYGFKC TILDIGGGFP GTEVVEGSGN TSFEAIARTI 

       490        500        510        520        530        540 
RPVLAELFGG GDVTIISEPG RYFTAASHAL LMNVFASRTL RLSDVEVSRQ AFQSVVSMDE 

       550        560        570        580        590        600 
PEEYQYYVND GLYHSFNCIL FDHAHPTLLL LNDGDGADGV ESGTEAAAVC SEEEGETSLS 

       610        620        630        640        650        660 
GPLANDPLFM SAWDRRRSFA RRPLRITTIF GPTCDSMDCI LKKQPFPEMK LGDWLLVPDM 

       670        680        690        700 
GSYTTAAAGF FNGFATRRLE WVSSVDLCAR PRPVYTREGN TLRCVSE 

« Hide

References

[1]"Amplification and molecular cloning of the ornithine decarboxylase gene of Leishmania donovani."
Hanson S.S., Adelman J., Ullman B.
J. Biol. Chem. 267:2350-2359(1992) [PubMed: 1339439] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M81192 Genomic DNA. Translation: AAA29259.1.
PIRA42322.

3D structure databases

ProteinModelPortalP27116.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR009006. Ala_racemase/Decarboxylase_C.
IPR022643. De-COase2_C.
IPR022657. De-COase2_CS.
IPR022644. De-COase2_N.
IPR022653. De-COase2_pyr-phos_BS.
IPR000183. Orn/DAP/Arg_de-COase.
IPR002433. Orn_de-COase.
[Graphical view]
Gene3DG3DSA:2.40.37.10. Ala_racemase/Decarboxylase_C. 2 hits.
PfamPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSPR01179. ODADCRBXLASE.
PR01182. ORNDCRBXLASE.
SUPFAMSSF50621. Racem_decarbox_C. 1 hit.
PROSITEPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDCOR_LEIDO
AccessionPrimary (citable) accession number: P27116
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: September 21, 2011
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families