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UniProtKB/Swiss-Prot entry P33232

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

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Entry information
Entry name LLDD_ECOLI
Primary accession number P33232
Secondary accession number Q2M7R9
Integrated into Swiss-Prot on February 1, 1994
Sequence was last modified on February 1, 1994 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 73)
Name and origin of the protein
Protein name L-lactate dehydrogenase [cytochrome]
Synonym EC 1.1.2.3
Gene name
Name: lldD
Synonyms: lctD
OrderedLocusNames: b3605, JW3580
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=8407843 [NCBI, ExPASy, EBI, Israel, Japan]
Dong J.M., Taylor J.S., Latour D.J., Iuchi S., Lin E.C.C.;
"Three overlapping lct genes involved in L-lactate utilization by Escherichia coli.";
J. Bacteriol. 175:6671-6678(1993).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1093/nar/22.13.2576; PubMed=8041620 [NCBI, ExPASy, EBI, Israel, Japan]
Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
"Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes.";
Nucleic Acids Res. 22:2576-2586(1994).
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
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
L13970; AAA03585.1; -; Unassigned_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00039; AAB18582.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76629.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77687.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C49904; C49904.
RefSeq AP_004186.1; -.
NP_418062.1; -.
3D structure databases
HSSP P05414; 1GOX. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase P33232.
Protein-protein interaction databases
DIP DIP:10108N; -.
IntAct P33232; -.
Enzyme and pathway databases
BioCyc EcoCyc:L-LACTDEHYDROGFMN-MON; -.
MetaCyc:L-LACTDEHYDROGFMN-MON; -.
Organism-specific databases
EchoBASE EB1906; -.
EcoGene EG11963; lldD.
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:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
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).
ProtoNet P33232.
Genome annotation databases
GeneID 948121; -.
GenomeReviews U00096_GR; b3605.
AP009048_GR; JW3580.
KEGG ecj:JW3580; -.
eco:b3605; -.
Phylogenomic databases
HOGENOM P33232; -.
Genome annotation databases
CMR P33232; b3605.
Other
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_0000206335
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: 42728 Da [This is the MW of the unprocessed precursor] CRC64: CA0D8E308713BF83 [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 MPVALAPVGL 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
P33232 in FASTA format

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