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UniProtKB/Swiss-Prot entry Q8FCB1

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LLDD_ECOL6
Primary accession number Q8FCB1
Secondary accession numbers None
Integrated into Swiss-Prot on January 10, 2006
Sequence was last modified on March 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 40)
Name and origin of the protein
Protein name L-lactate dehydrogenase [cytochrome]
Synonym EC 1.1.2.3
Gene name
Name: lldD
OrderedLocusNames: c4427
From
Escherichia coli O6 [TaxID: 217992] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
DOI=10.1073/pnas.252529799; PubMed=12471157 [NCBI, ExPASy, EBI, Israel, Japan]
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE014075; AAN82863.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_756289.1; -.
3D structure databases
HSSP P05414; 1GOX. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase Q8FCB1.
Ontologies
GO
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0010181; Molecular function: FMN binding (inferred from electronic annotation from InterPro).
GO:0004460; Molecular function: L-lactate dehydrogenase (cytochrome) activity (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_01559; -; 1.
PBIL [Tree]
InterPro IPR013785; Aldolase_TIM.
IPR012133; Alpha_OHA_DHase_FMN.
IPR008259; FMN_hydac_DHase_AS.
IPR000262; FMN_OHA_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
Pfam PF01070; FMN_dh; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000138; Al-hdrx_acd_dh; 1.
PROSITE PS00557; FMN_HYDROXY_ACID_DH_1; 1.
PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 1038129; -.
GenomeReviews AE014075_GR; c4427.
KEGG ecc:c4427; -.
Phylogenomic databases
HOGENOM Q8FCB1; -.
Genome annotation databases
CMR Q8FCB1; c4427.
Other
ProtoNet Q8FCB1.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Flavoprotein; FMN; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   396  396     L-lactate dehydrogenase [cytochrome]. PRO_0000206337
DOMAIN   1   380  380     FMN hydroxy acid dehydrogenase. 
NP_BIND   306   330  25     FMN (By similarity). 
ACT_SITE   275   275        Proton acceptor (By similarity). 
BINDING   24    24        Substrate (Potential). 
BINDING   106   106        FMN (By similarity). 
BINDING   127   127        FMN (By similarity). 
BINDING   129   129        Substrate (By similarity). 
BINDING   155   155        FMN (By similarity). 
BINDING   164   164        Substrate (By similarity). 
BINDING   251   251        FMN (By similarity). 
BINDING   278   278        Substrate (Potential). 
Sequence information
Length: 396 AA [This is the length of the unprocessed precursor] Molecular weight: 42714 Da [This is the MW of the unprocessed precursor] CRC64: ED12F511FF74A181 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MIISAASDYR AAAQRILPPF LFHYMDGGAY SEYTLRRNVE DLSEVALRQR ILKNMSDLSL 

        70         80         90        100        110        120 
ETTLFNEKLS MPVALGPVGL CGMYARRGEV QAAKAADAHG IPFTLSTVSV CPIEEVAPAI 

       130        140        150        160        170        180 
KRPMWFQLYV LRDRGFMRNA LERAKAAGCS TLVFTVDMPT PGARYRDAHS GMSGPNAAMR 

       190        200        210        220        230        240 
RYLQAVTHPQ WAWDVGLNGR PHDLGNISAY LGKPTGLEDY IGWLGNNFDP SISWKDLEWI 

       250        260        270        280        290        300 
RDFWDGPMVI KGILDPEDAR DAVRFGADGI VVSNHGGRQL DGVLSSARAL PAIADAVKGD 

       310        320        330        340        350        360 
IAILADSGIR NGLDVVRMIA LGADTVLLGR AFLYALATAG QAGVANLLNL IEKEMKVAMT 

       370        380        390 
LTGAKSISEI TQDSLVQGLG KELPAALAPM AKGNAA
Q8FCB1 in FASTA format

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