Q4QEW7 (Q4QEW7_LEIMA) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Dihydroorotate dehydrogenase EMBL CAJ03555.1
EC=1.3.3.1 EMBL CAJ03555.1

Gene names

Name:	DHODH EMBL CAJ03555.1
ORF Names:	LMJF_16_0530 EMBL CAJ03555.1

Organism

Leishmania major [Reference proteome]

Taxonomic identifier

5664 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Leishmaniinae › Leishmania › Leishmania › Leishmania major species complex

Protein attributes

Sequence length	320 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	FMN PDB 3GYE PDB 3GZ3 PDB 3MHU PDB 3MJY Flavoprotein PDB 3GYE PDB 3GZ3 PDB 3MHU PDB 3MJY Nucleotide-binding PDB 3GYE PDB 3GZ3 PDB 3MHU PDB 3MJY
Molecular function	Oxidoreductase EMBL CAJ03555.1
Technical term	3D-structure PDB 3TQ0 PDB 3TJX PDB 3GYE PDB 3GZ3 PDB 3TRO PDB 3MHU PDB 3MJY PDB 4EF8 PDB 4EF9 Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	UMP biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular_function	dihydroorotate oxidase activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Nucleotide binding	44 – 45	2	FMN PDB 3GYE PDB 3GZ3 PDB 3MHU PDB 3MJY
	Nucleotide binding	194 – 195	2	FMN PDB 3GYE PDB 3GZ3 PDB 3MHU PDB 3MJY
	Nucleotide binding	272 – 273	2	FMN PDB 3GYE PDB 3GZ3 PDB 3MHU PDB 3MJY
Sites
	Binding site	20	1	FMN PDB 3GYE PDB 3GZ3 PDB 3MHU PDB 3MJY
	Binding site	68	1	FMN PDB 3GYE PDB 3GZ3 PDB 3MHU PDB 3MJY
	Binding site	128	1	FMN PDB 3GYE PDB 3GZ3 PDB 3MHU PDB 3MJY
	Binding site	165	1	FMN PDB 3GYE PDB 3GZ3 PDB 3MHU PDB 3MJY
	Binding site	223	1	FMN; via amide nitrogen PDB 3GYE PDB 3GZ3 PDB 3MHU PDB 3MJY
	Binding site	251	1	FMN; via amide nitrogen PDB 3GYE PDB 3GZ3 PDB 3MHU PDB 3MJY

Sequences

	Sequence		Length	Mass (Da)
	Q4QEW7 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: FB13D0101F91577A	FASTA	320	34,662
	10 20 30 40 50 60 MSLQVNLLNN TFANPFMNAA GVMCTTTEEL VAMTESASGS LVSKSCTPAL REGNPTPRYQ 70 80 90 100 110 120 ALPLGSINSM GLPNNGFDFY LAYAAEQHDY GKKPLFLSMS GLSMRENVEM CKRLAAVATE 130 140 150 160 170 180 KGVILELNLS CPNVPGKPQV AYDFDAMRQC LTAVSEVYPH SFGVKMPPYF DFAHFDAAAE 190 200 210 220 230 240 ILNEFPKVQF ITCINSIGNG LVIDAETESV VIKPKQGFGG LGGRYVLPTA LANINAFYRR 250 260 270 280 290 300 CPGKLIFGCG GVYTGEDAFL HVLAGASMVQ VGTALQEEGP SIFERLTSEL LGVMAKKRYQ 310 320 TLDEFRGKVR TLDGTAESTR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome of the kinetoplastid parasite, Leishmania major." Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G., Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A., Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M., Bianchettin G. , Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E., Ciarloni L., Clayton C., Coulson R.M.R., Cronin A., Cruz A.K., Davies R.M., De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N., Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A., Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S., Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M., Masuy D., Matthews K., Michaeli S., Mottram J.C., Mueller-Auer S., Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M., Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E., Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C., Rutter S., Saunders D., Schaefer M., Schein J., Schwartz D.C., Seeger K., Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V., Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J., Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D., Barrell B.G., Myler P.J. Science 309:436-442(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MHOM/IL/81/Friedlin.
[2]	"Crystal Structure of Leishmania major Dihydroorotate dehydrogenase." Cordeiro A.T., Feliciano P.R., Nonato M.C. Submitted (APR-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH FMN.
[3]	"Leismania major dihydroorotate in complex with orotate." Cordeiro A.T., Feliciano P.R., Nonato M.C. Submitted (APR-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH FMN.
[4]	"Novel insights for dihydroorotate dehydrogenase class 1A inhibitors discovery." Cheleski J., Rocha J.R., Pinheiro M.P., Wiggers H.J., da Silva A.B., Nonato M.C., Montanari C.A. Eur. J. Med. Chem. 45:5899-5909(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-312 IN COMPLEX WITH FMN.
[5]	"Crystal Structure of Leishmania major dihydroorotate dehydrogenase mutant H174A." de Souza A.L., Nonato M.C., Pinheiro M.P. Submitted (AUG-2011) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS).
[6]	"Crystal Structure of Leishmania major dihydroorotate dehydrogenase mutant D171A." de Souza A.L., Pinheiro M.P., Nonato M.C. Submitted (SEP-2011) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS).
[7]	"Crystal structure of dihydroorotate dehydrogenase from Leishmania major." Cordeiro A.T., Feliciano P.R., Pinheiro M.P., Nonato M.C. Biochimie 94:1739-1748(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-312.
[8]	"Target sites for the design of anti-trypanosomatid drugs based on the structure of dihydroorotate." Pinheiro M.P., Emery F.D., Nonato M.C. Curr. Pharm. Des. 0:0-0(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

FR796412 Genomic DNA. Translation: CAJ03555.1.

RefSeq

XP_001682131.1. XM_001682079.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3GYE	X-ray	2.00	A/B	1-320	[»]
3GZ3	X-ray	1.90	A/B	1-320	[»]
3MHU	X-ray	1.85	A/B	1-312	[»]
3MJY	X-ray	1.96	A/B	1-312	[»]
3TJX	X-ray	1.64	A/B	1-320	[»]
3TQ0	X-ray	1.90	A/B	1-312	[»]
3TRO	X-ray	1.86	A/B	1-320	[»]
4EF8	X-ray	1.56	A/B	1-320	[»]
4EF9	X-ray	1.60	A/B	1-320	[»]

ProteinModelPortal

Q4QEW7.

SMR

Q4QEW7. Positions 1-313.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblProtists

LmjF.16.0530:mRNA; LmjF.16.0530:pep; LmjF.16.0530.

GeneID

5650598.

KEGG

lma:LMJF_16_0530.

Phylogenomic databases

HOGENOM

HOG000225104.

KO

K00226.

OMA

VSCPHAE.

ProtClustDB

CLSZ2439727.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

InterPro

IPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
[Graphical view]

Pfam

PF01180. DHO_dh. 1 hit.
[Graphical view]

PIRSF

PIRSF000164. DHO_oxidase. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q4QEW7.

Entry information

Entry name

Q4QEW7_LEIMA

Accession

Primary (citable) accession number: Q4QEW7

Entry history

Integrated into UniProtKB/TrEMBL:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	May 1, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)