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Protein

Ornithine decarboxylase

Gene
N/A
Organism
Trypanosoma brucei brucei
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-ornithine = putrescine + CO2.

Cofactori

Pathwayi: putrescine biosynthesis via L-ornithine pathway

This protein is involved in step 1 of the subpathway that synthesizes putrescine from L-ornithine.
Proteins known to be involved in this subpathway in this organism are:
  1. Ornithine decarboxylase
This subpathway is part of the pathway putrescine biosynthesis via L-ornithine pathway, which is itself part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes putrescine from L-ornithine, the pathway putrescine biosynthesis via L-ornithine pathway and in Amine and polyamine biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei358Proton donor; shared with dimeric partner1

GO - Molecular functioni

  • ornithine decarboxylase activity Source: GeneDB

GO - Biological processi

  • polyamine biosynthetic process Source: GeneDB
  • putrescine biosynthetic process from ornithine Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Polyamine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi4.1.1.17. 6519.
SABIO-RKP07805.
UniPathwayiUPA00535; UER00288.

Names & Taxonomyi

Protein namesi
Recommended name:
Ornithine decarboxylase (EC:4.1.1.17)
Short name:
ODC
OrganismiTrypanosoma brucei brucei
Taxonomic identifieri5702 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001499031 – 423Ornithine decarboxylaseAdd BLAST423

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei67N6-(pyridoxal phosphate)lysine1

Proteomic databases

PRIDEiP07805.

Structurei

Secondary structure

1423
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi19 – 26Combined sources8
Beta strandi38 – 42Combined sources5
Helixi43 – 56Combined sources14
Beta strandi60 – 65Combined sources6
Helixi66 – 68Combined sources3
Helixi72 – 80Combined sources9
Beta strandi84 – 87Combined sources4
Helixi90 – 98Combined sources9
Helixi103 – 105Combined sources3
Beta strandi106 – 108Combined sources3
Helixi115 – 123Combined sources9
Beta strandi128 – 131Combined sources4
Helixi134 – 143Combined sources10
Beta strandi148 – 153Combined sources6
Beta strandi166 – 168Combined sources3
Helixi172 – 184Combined sources13
Beta strandi188 – 193Combined sources6
Helixi204 – 222Combined sources19
Beta strandi229 – 231Combined sources3
Beta strandi239 – 241Combined sources3
Beta strandi242 – 244Combined sources3
Helixi246 – 260Combined sources15
Beta strandi268 – 271Combined sources4
Helixi275 – 278Combined sources4
Helixi279 – 281Combined sources3
Beta strandi282 – 293Combined sources12
Beta strandi312 – 317Combined sources6
Turni320 – 322Combined sources3
Helixi323 – 325Combined sources3
Helixi326 – 329Combined sources4
Beta strandi337 – 340Combined sources4
Beta strandi348 – 354Combined sources7
Beta strandi356 – 358Combined sources3
Beta strandi363 – 371Combined sources9
Beta strandi378 – 381Combined sources4
Beta strandi386 – 388Combined sources3
Helixi389 – 391Combined sources3
Helixi395 – 397Combined sources3
Beta strandi402 – 406Combined sources5
Helixi414 – 418Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F3TX-ray2.00A/B/C/D1-423[»]
1QU4X-ray2.90A/B/C/D21-423[»]
1SZRX-ray2.15A/B/C/D1-423[»]
2TODX-ray2.00A/B/C/D21-423[»]
DisProtiDP00051.
ProteinModelPortaliP07805.
SMRiP07805.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07805.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
InterProiIPR009006. Ala_racemase/Decarboxylase_C.
IPR022643. De-COase2_C.
IPR022644. De-COase2_N.
IPR022653. De-COase2_pyr-phos_BS.
IPR000183. Orn/DAP/Arg_de-COase.
IPR002433. Orn_de-COase.
IPR029066. PLP-binding_barrel.
[Graphical view]
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSiPR01179. ODADCRBXLASE.
PR01182. ORNDCRBXLASE.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07805-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDIVVNDDLS CRFLEGFNTR DALCKKISMN TCDEGDPFFV ADLGDIVRKH
60 70 80 90 100
ETWKKCLPRV TPFYAVKCND DWRVLGTLAA LGTGFDCASN TEIQRVRGIG
110 120 130 140 150
VPPEKIIYAN PCKQISHIRY ARDSGVDVMT FDCVDELEKV AKTHPKAKMV
160 170 180 190 200
LRISTDDSLA RCRLSVKFGA KVEDCRFILE QAKKLNIDVT GVSFHVGSGS
210 220 230 240 250
TDASTFAQAI SDSRFVFDMG TELGFNMHIL DIGGGFPGTR DAPLKFEEIA
260 270 280 290 300
GVINNALEKH FPPDLKLTIV AEPGRYYVAS AFTLAVNVIA KKVTPGVQTD
310 320 330 340 350
VGAHAESNAQ SFMYYVNDGV YGSFNCILYD HAVVRPLPQR EPIPNEKLYP
360 370 380 390 400
SSVWGPTCDG LDQIVERYYL PEMQVGEWLL FEDMGAYTVV GTSSFNGFQS
410 420
PTIYYVVSGL PDHVVRELKS QKS
Length:423
Mass (Da):46,881
Last modified:May 30, 2000 - v2
Checksum:i924A5AA6C4CD2C36
GO

Sequence cautioni

The sequence AAA30218 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02771 Genomic DNA. Translation: AAA30218.1. Different initiation.
J02771 Genomic DNA. Translation: AAA30219.1.

Genome annotation databases

GeneDBiTb927.11.13730:pep.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02771 Genomic DNA. Translation: AAA30218.1. Different initiation.
J02771 Genomic DNA. Translation: AAA30219.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F3TX-ray2.00A/B/C/D1-423[»]
1QU4X-ray2.90A/B/C/D21-423[»]
1SZRX-ray2.15A/B/C/D1-423[»]
2TODX-ray2.00A/B/C/D21-423[»]
DisProtiDP00051.
ProteinModelPortaliP07805.
SMRiP07805.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP07805.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneDBiTb927.11.13730:pep.

Enzyme and pathway databases

UniPathwayiUPA00535; UER00288.
BRENDAi4.1.1.17. 6519.
SABIO-RKP07805.

Miscellaneous databases

EvolutionaryTraceiP07805.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
InterProiIPR009006. Ala_racemase/Decarboxylase_C.
IPR022643. De-COase2_C.
IPR022644. De-COase2_N.
IPR022653. De-COase2_pyr-phos_BS.
IPR000183. Orn/DAP/Arg_de-COase.
IPR002433. Orn_de-COase.
IPR029066. PLP-binding_barrel.
[Graphical view]
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSiPR01179. ODADCRBXLASE.
PR01182. ORNDCRBXLASE.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDCOR_TRYBB
AccessioniPrimary (citable) accession number: P07805
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: May 30, 2000
Last modified: November 2, 2016
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.