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 P46454

[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_HAEIN
Primary accession number P46454
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on November 1, 1995 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 59)
Name and origin of the protein
Protein name L-lactate dehydrogenase [cytochrome]
Synonym EC 1.1.2.3
Gene name
Name: lldD
OrderedLocusNames: HI1739.1
From
Haemophilus influenzae [TaxID: 727] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; Pasteurellaceae; Haemophilus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
PubMed=7542800 [NCBI, ExPASy, EBI, Israel, Japan]
Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd.";
Science 269:496-512(1995).
[2]
 IDENTIFICATION.
Koonin E.V., Rudd K.E.;
Submitted (SEP-1995) to UniProtKB.
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
L42023; AAC23385.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T09429; T09429.
RefSeq NP_439882.1; -.
3D structure databases
HSSP P00175; 1KBI. [HSSP ENTRY / PDB]
ModBase P46454.
Enzyme and pathway databases
BioCyc HINF71421:HI_1739.1-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 P46454.
Genome annotation databases
GeneID 950543; -.
GenomeReviews L42023_GR; HI1739.1.
KEGG hin:HI1739.1; -.
NMPDR fig|71421.1.peg.1652; -.
TIGR HI1739.1; -.
Phylogenomic databases
HOGENOM P46454; -.
Other
ProtoNet P46454.
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   381  381     L-lactate dehydrogenase [cytochrome]. PRO_0000206339
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: 381 AA [This is the length of the unprocessed precursor] Molecular weight: 41965 Da [This is the MW of the unprocessed precursor] CRC64: E1BC62B0A1A6482D [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MIISSASDYR EAARRRVPPF MFHYADGGSY AEQTLARNVS DLENIALRQR VLKDMSELDT 

        70         80         90        100        110        120 
SIELFGEKLS MPTILAPVGA CGMYARRGEV QAAQAADNKG VPFTLSTVSI CPIEEVAPAI 

       130        140        150        160        170        180 
KRPMWFQLYV LKDRGFMKNA LERAKAAGCS TLVFTVDMPT PGARYRDMHS GMSGPYKEIR 

       190        200        210        220        230        240 
RVLQGFTHPF WAYDVGIKGK PHTLGNVSTY MGRQIGLDDY IGWLTENFDP SISWKDLEWI 

       250        260        270        280        290        300 
REFWEGPMVI KGILDPEDAK DAVRFGADGI VVSNHGGRQL DGVLSSARAL PPIADAVKGD 

       310        320        330        340        350        360 
IKIIADSGIR NGLDIVRMLA LGADATMLGR AFVYALGAEG RQGVENMLDI FKKEMHVAMT 

       370        380 
LTSNRTIADI KPEALVDLSK L
P46454 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 kr flag YPRC Korea Mirror sites: Australia Brazil Canada China Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!