P07805 (DCOR_TRYBB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Ornithine decarboxylase Short name=ODC EC=4.1.1.17
Organism	Trypanosoma brucei brucei
Taxonomic identifier	5702 [NCBI]
Taxonomic lineage	Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma

Protein attributes

Sequence length	423 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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.
Sequence caution	The sequence AAA30218.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Polyamine biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Decarboxylase Lyase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	polyamine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ornithine decarboxylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 423

423

Ornithine decarboxylase

PRO_0000149903

Sites

Active site

358

1

Proton donor; shared with dimeric partner

Amino acid modifications

Modified residue

67

1

N6-(pyridoxal phosphate)lysine

Secondary structure

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423

Helix Strand Turn

Details...

Helix

19 – 26

8

Beta strand

38 – 42

5

Helix

43 – 56

14

Beta strand

60 – 65

6

Helix

66 – 68

3

Helix

72 – 80

9

Beta strand

84 – 87

4

Helix

90 – 98

9

Helix

103 – 105

3

Beta strand

106 – 108

3

Helix

115 – 123

9

Beta strand

128 – 131

4

Helix

134 – 143

10

Beta strand

148 – 153

6

Helix

172 – 184

13

Beta strand

188 – 193

6

Helix

204 – 222

19

Beta strand

229 – 231

3

Beta strand

242 – 244

3

Helix

246 – 260

15

Beta strand

268 – 271

4

Helix

275 – 278

4

Helix

279 – 281

3

Beta strand

282 – 293

12

Beta strand

312 – 317

6

Turn

320 – 322

3

Helix

323 – 325

3

Helix

326 – 329

4

Beta strand

348 – 354

7

Beta strand

356 – 358

3

Beta strand

363 – 371

9

Beta strand

378 – 381

4

Beta strand

386 – 388

3

Helix

389 – 391

3

Helix

395 – 397

3

Beta strand

402 – 406

5

Helix

414 – 418

5

Sequences

	Sequence		Length	Mass (Da)
	P07805 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 924A5AA6C4CD2C36	FASTA	423	46,881
	10 20 30 40 50 60 MDIVVNDDLS CRFLEGFNTR DALCKKISMN TCDEGDPFFV ADLGDIVRKH ETWKKCLPRV 70 80 90 100 110 120 TPFYAVKCND DWRVLGTLAA LGTGFDCASN TEIQRVRGIG VPPEKIIYAN PCKQISHIRY 130 140 150 160 170 180 ARDSGVDVMT FDCVDELEKV AKTHPKAKMV LRISTDDSLA RCRLSVKFGA KVEDCRFILE 190 200 210 220 230 240 QAKKLNIDVT GVSFHVGSGS TDASTFAQAI SDSRFVFDMG TELGFNMHIL DIGGGFPGTR 250 260 270 280 290 300 DAPLKFEEIA GVINNALEKH FPPDLKLTIV AEPGRYYVAS AFTLAVNVIA KKVTPGVQTD 310 320 330 340 350 360 VGAHAESNAQ SFMYYVNDGV YGSFNCILYD HAVVRPLPQR EPIPNEKLYP SSVWGPTCDG 370 380 390 400 410 420 LDQIVERYYL PEMQVGEWLL FEDMGAYTVV GTSSFNGFQS PTIYYVVSGL PDHVVRELKS QKS

References

[1]	"Cloning and sequencing of the ornithine decarboxylase gene from Trypanosoma brucei. Implications for enzyme turnover and selective difluoromethylornithine inhibition." Phillips M.A., Coffino P., Wang C.C. J. Biol. Chem. 262:8721-8727(1987) [PubMed: 3036823] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"X-ray structure of ornithine decarboxylase from Trypanosoma brucei: the native structure and the structure in complex with alpha-difluoromethylornithine." Grishin N.V., Osterman A.L., Brooks H.B., Phillips M.A., Goldsmith E.J. Biochemistry 38:15174-15184(1999) [PubMed: 10563800] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[3]	"Altering the reaction specificity of eukaryotic ornithine decarboxylase." Jackson L.K., Brooks H.B., Osterman A.L., Goldsmith E.J., Phillips M.A. Biochemistry 39:11247-11257(2000) [PubMed: 10985770] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J02771 Genomic DNA. Translation: AAA30218.1. Different initiation.
J02771 Genomic DNA. Translation: AAA30219.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F3T	X-ray	2.00	A/B/C/D	1-423	[»]
1QU4	X-ray	2.90	A/B/C/D	1-423	[»]
1SZR	X-ray	2.15	A/B/C/D	1-423	[»]
2TOD	X-ray	2.00	A/B/C/D	1-423	[»]

ProteinModelPortal

P07805.

SMR

P07805. Positions 12-420.

DisProt

DP00051.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR009006. 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.
[Graphical view]

Gene3D

G3DSA:2.40.37.10. Ala_racemase/Decarboxylase_C. 1 hit.

Pfam

PF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]

PRINTS

PR01179. ODADCRBXLASE.
PR01182. ORNDCRBXLASE.

SUPFAM

SSF50621. Racem_decarbox_C. 1 hit.

PROSITE

PS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

DCOR_TRYBB

Accession

Primary (citable) accession number: P07805

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	May 30, 2000
Last modified:	May 31, 2011
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)