P49725 (DCOR_PANRE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ornithine decarboxylase
Short name=ODC
EC=4.1.1.17

Gene names

Name:

ODC

Organism

Panagrellus redivivus

Taxonomic identifier

6233 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Panagrolaimoidea › Panagrolaimidae › Panagrellus

Protein attributes

Sequence length	435 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the Orn/Lys/Arg decarboxylase class-II family.

Ontologies

Keywords
Biological process	Polyamine biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Decarboxylase Lyase
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 – 435	435	Ornithine decarboxylase		PRO_0000149902
Sites
	Active site	368	1	Proton donor; shared with dimeric partner By similarity
Amino acid modifications
	Modified residue	76	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P49725 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: BBB093C1EF7FEFA4	FASTA	435	47,111
	10 20 30 40 50 60 MTLTGCVDYY EIIAGTKVAV CRNAIDNKTV ATAIAATRTV NGNDDPFVVM NVSTIMAKVI 70 80 90 100 110 120 QWQRTMPRVA PCYAVKCNDD KVLLRTLADL GMGFDCASKA EIEKVIGLVG PEKIVYANPC 130 140 150 160 170 180 KTRGFIAHAE AAGVKRMTFD SVEELTKIKQ NHADPSLILR ISVSDPTAQC QLGIKFGCDP 190 200 210 220 230 240 ETVAPKLLRK AADMGMNVIG ISFHVGSGCN EPATFRTALE YARGLFDLGI SLGLSMTLLD 250 260 270 280 290 300 IGGGFPGVDT AHISLDACAA VINPALEELF PLDSCPDVEV IAEPGRYFAC AAVSVTTNVI 310 320 330 340 350 360 ASVKVPASRI TEKADDVNRD GYMYYMNDGV YGSFNCKLFD HYQPRGMPLA EHDADEPRFP 370 380 390 400 410 420 VCVWGPTCDG LDQVEESSVM PRLYEGDWLY YPDMGAYTSV AASTFNGFDK PKTYYFIDEA 430 TLGSIVRKAD SAPRG

References

[1]	"Molecular cloning and characterization of ornithine decarboxylase cDNA of the nematode Panagrellus redivivus." von Besser H., Niemann G., Domdey B., Walter R.D. Biochem. J. 308:635-640(1995) [PubMed: 7772052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X82199 mRNA. Translation: CAA57683.1. X95719 Genomic DNA. Translation: CAA65024.1.
PIR	S52784. S55347.
3D structure databases
ProteinModelPortal	P49725.
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_PANRE

Accession

Primary (citable) accession number: P49725

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	September 21, 2011
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)