Reviewed, UniProtKB/Swiss-Prot P27116 (DCOR_LEIDO)

Names and origin

Protein names	Recommended name:     Ornithine decarboxylase       Short name=ODC     EC=4.1.1.17
Organism	Leishmania donovani
Taxonomic identifier	5661 [NCBI]
Taxonomic lineage	Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Leishmania

Protein attributes

Sequence length	707 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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 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 – 707	707	Ornithine decarboxylase		PRO_0000149901
Sites
	Active site	634	1	Proton donor; shared with dimeric partner By similarity
Amino acid modifications
	Modified residue	288	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P27116-1 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: EBDF14F791EC572D	FASTA	707	77,397
	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

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].

Cross-references

Sequence databases
EMBLGenBankDDBJ	M81192 Genomic DNA. Translation: AAA29259.1.
PIR	A42322.
3D structure databases
HSSP	HSSP built from PDB template 7ODC based on UniProtKB P00860.
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.1.1.17. 882.
Family and domain databases
InterPro	IPR000183. De-COase2. IPR002433. Orn_de-COase. [Graphical view]
Pfam	PF02784. Orn_Arg_deC_N. 1 hit. PF00278. Orn_DAP_Arg_deC. 1 hit. [Graphical view]
PRINTS	PR01179. ODADCRBXLASE. PR01182. ORNDCRBXLASE.
PROSITE	PS00878. ODR_DC_2_1. 1 hit. PS00879. ODR_DC_2_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DCOR_LEIDO

Accession

Primary (citable) accession number: P27116

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	June 16, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)