Reviewed, UniProtKB/Swiss-Prot Q0TFN1 (MQO_ECOL5)

Names and origin

Protein names

Recommended name:
    Probable malate:quinone oxidoreductase
    EC=1.1.99.16
Alternative name(s):
    Malate dehydrogenase [acceptor]
    MQO

Gene names

Name:	mqo
Ordered Locus Names:	ECP_2252

Organism

Escherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

362663 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	548 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	(S)-malate + acceptor = oxaloacetate + reduced acceptor.
Cofactor	FAD By similarity.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle.
Sequence similarities	Belongs to the MQO family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: HAMAP
Molecular function	malate dehydrogenase (acceptor) activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 548	548	Probable malate:quinone oxidoreductase		PRO_0000325496

Sequences

	Sequence		Length	Mass (Da)
	Q0TFN1-1 [UniParc]. Last modified March 18, 2008. Version 2. Checksum: 206AE9AD24ADF538	FASTA	548	60,232
	10 20 30 40 50 60 MKKVTAMLFS MAVGLNAVSM AAKAKASEEQ ETDVLLIGGG IMSATLGTYL RELEPEWSMT 70 80 90 100 110 120 MVERLEGVAQ ESSNGWNNAG TGHSALMELN YTPQNADGSI SIEKAVAINE AFQISRQFWA 130 140 150 160 170 180 HQVERGVLRT PRSFINTVPH MSFVWGEDNV NFLRARYAAL QQSSLFRGMR YSEDHAQIKE 190 200 210 220 230 240 WAPLVMEGRD PQQKVAATRT EIGTDVNYGE ITRQLIASLQ KKSNFSLQLS SEVRALKRND 250 260 270 280 290 300 DNSWTVTVAD LKNGTAQNIR AKFVFIGAGG AALKLLQESG IPEAKDYAGF PVGGQFLVSE 310 320 330 340 350 360 NPDVVNHHLA KVYGKASVGA PPMSVPHIDT RVLDGKRVVL FGPFATFSTK FLKNGSLWDL 370 380 390 400 410 420 MSSTTTSNVM PMMHVGLDNF DLVKYLVSQV MLSEEDRFEA LKEYYPQAKK EDWRLWQAGQ 430 440 450 460 470 480 RVQIIKRDAD KGGVLRLGTE VVSDQQGTIA ALLGASPGAS TAAPIMLNLL EKVFGDRVSS 490 500 510 520 530 540 PQWQATLKAI VPSYGRKLNG DVAATERELQ YTSEVLGLKY DKPQAADSTP KPQLKPQLVQ KEVADIAL

References

[1]

"Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536." Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J. Mol. Microbiol. 61:584-595(2006) [PubMed: 16879640] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000247 Genomic DNA. Translation: ABG70248.1. Different initiation.
RefSeq	YP_670149.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4190123.
GenomeReviews	Gene locus ECP_2252 in contig CP000247_GR.
KEGG	ecp:ECP_2252.
NMPDR	fig|340197.3.peg.274.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0TFN1.
Enzyme and pathway databases
BioCyc	ECOL362663:ECP_2252-MON.
Family and domain databases
HAMAP	MF_00212. [Tree]
InterPro	IPR006231. Malate_quinone_OxRdtase. [Graphical view]
Pfam	PF06039. Mqo. 1 hit. [Graphical view]
TIGRFAMs	TIGR01320. mal_quin_oxido. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MQO_ECOL5

Accession

Primary (citable) accession number: Q0TFN1

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	March 18, 2008
Last modified:	November 4, 2008
This is version 21 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)