ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q6G4R2


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name LLDD_BARHE
Primary accession number Q6G4R2
Secondary accession numbers None
Integrated into Swiss-Prot on January 10, 2006
Sequence was last modified on July 19, 2004 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 29)
Name and origin of the protein
Protein name L-lactate dehydrogenase [cytochrome]
Synonym EC 1.1.2.3
Gene name
Name: lldD
OrderedLocusNames: BH02710
From
Bartonella henselae (Rochalimaea henselae) [TaxID: 38323] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bartonellaceae; Bartonella.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 49882 / Houston 1;
DOI=10.1073/pnas.0305659101; PubMed=15210978 [NCBI, ExPASy, EBI, Israel, Japan]
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.;
"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae.";
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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
BX897699; CAF27083.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_033123.1; -.
3D structure databases
ModBase Q6G4R2.
Enzyme and pathway databases
BioCyc BHEN283166:BH02710-MON; -.
Ontologies
GO
GO:0004460; Molecular function: L-lactate dehydrogenase (cytochrome) activity (inferred from electronic annotation from HAMAP).
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).
BLOCKS Q6G4R2.
Genome annotation databases
GeneID 2865591; -.
GenomeReviews BX897699_GR; BH02710.
KEGG bhe:BH02710; -.
NMPDR fig|283166.1.peg.251; -.
Phylogenomic databases
HOGENOM Q6G4R2; -.
Genome annotation databases
CMR Q6G4R2; BH02710.
Other
ProtoNet Q6G4R2.
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   383  383     L-lactate dehydrogenase [cytochrome]. PRO_0000206331
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: 383 AA [This is the length of the unprocessed precursor] Molecular weight: 42129 Da [This is the MW of the unprocessed precursor] CRC64: CCEA4E2FEFB6AF1A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MIISSTLDYR KAAKRRLPPF LFHYIDGGAY AEETMRRNYA DLQALALRQR ILRGVGEVDL 

        70         80         90        100        110        120 
STKLFDQTLD LPIILAPVGL TGMYARRGEV QAARAAVAKG IPFTLSSVSV CPIAEVQKAV 

       130        140        150        160        170        180 
GSAFWFQLYV LKDRGFMRDV LERSWASGVR TLVFTVDMPV PGARYRDAHS GMSGSYAGLR 

       190        200        210        220        230        240 
RILQAFIHPH WAWNVGIMGR PHDLGNVSTY LQKKIALDDY IGWLGANFDP SIGWHDLQWI 

       250        260        270        280        290        300 
RDFWKGKMIL KGILDPEDAR EAIQFGADGI VVSNHGGRQL DGVLSTVRAL PAIAEAVKSD 

       310        320        330        340        350        360 
LTILVDSGVR SGLDVVRMIA QGADAVMIGR AFVYALAAAG EKGVAHLIDL FANEMRVAMT 

       370        380 
LTGVRAIKEI TRESLASPDV FEQ 

Q6G4R2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!