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UniProtKB/Swiss-Prot entry Q12627


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

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Entry information
Entry name DLD1_KLULA
Primary accession number Q12627
Secondary accession number Q6CMJ7
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on September 27, 2004 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 59)
Name and origin of the protein
Protein name D-lactate dehydrogenase [cytochrome], mitochondrial [Precursor]
Synonyms EC 1.1.2.4
D-lactate ferricytochrome C oxidoreductase
D-LCR
Gene name
Name: DLD1
Synonyms: DLD
OrderedLocusNames: KLLA0E19789g
From
Kluyveromyces lactis (Yeast) (Candida sphaerica) [TaxID: 28985] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37;
DOI=10.1007/BF00282752; PubMed=7969031 [NCBI, ExPASy, EBI, Israel, Japan]
Lodi T., O'Connor D., Goffrini P., Ferrero I.;
"Carbon catabolite repression in Kluyveromyces lactis: isolation and characterization of the KIDLD gene encoding the mitochondrial enzyme D-lactate ferricytochrome c oxidoreductase.";
Mol. Gen. Genet. 244:622-629(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37;
DOI=10.1038/nature02579; PubMed=15229592 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(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
X71628; CAA50635.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR382125; CAG99929.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S51528; S51528.
RefSeq XP_454842.1; -.
3D structure databases
ModBase Q12627.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.
Family and domain databases
InterPro IPR016167; FAD-bd_2_sub1.
IPR016168; FAD-linked_Oxase_FAD-bd_sub2.
IPR004113; FAD-linked_oxidase_C.
IPR006094; Oxid_FAD_bind_N.
Graphical view of domain structure.
Gene3D G3DSA:3.30.43.10; FAD-binding_2_sub1; 1.
G3DSA:3.30.465.20; FAD-linked_oxidase_FAD-bd_sub2; 1.
Pfam PF02913; FAD-oxidase_C; 1.
PF01565; FAD_binding_4; 1.
Pfam graphical view of domain structure.
PROSITE PS51387; FAD_PCMH; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q12627.
Genome annotation databases
GeneID 2894285; -.
KEGG kla:KLLA0E19789g; -.
Phylogenomic databases
HOGENOM Q12627; -.
Other
ProtoNet Q12627.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Transit peptide; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1     ?        Mitochondrion. 
CHAIN   ?   576        D-lactate dehydrogenase [cytochrome], mitochondrial. PRO_0000020427
DOMAIN   139   320  182     FAD-binding PCMH-type. 
CONFLICT   539   539        E -> Q (in Ref. 1; CAA50635). 
CONFLICT   564   564        D -> DKIF (in Ref. 1; CAA50635). 
Sequence information
Length: 576 AA [This is the length of the unprocessed precursor] Molecular weight: 63097 Da [This is the MW of the unprocessed precursor] CRC64: 629615C88758545F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MFRFVGRSGF ALRGSLQLRK DVLRSRTTAV AKRHYSSSNG NNGGGFSSAI LSVLGGSLIG 

        70         80         90        100        110        120 
GGFVAYALGS QFEKEKSVSD LSIARLEDLD SPEYCDKETF AKALVELKDV LENDPENFTV 

       130        140        150        160        170        180 
AKDDLDAHSD TYFNSHHAEA NQRPEIVLYP RNTEDVSKLL KICHKYSIPV IPFSGGTSLE 

       190        200        210        220        230        240 
GHFLPTRPGS CVVLDISKYL NKIIQLNKED LDVVVQGGVP WEELNEYLND HGLLFGCDPG 

       250        260        270        280        290        300 
PGAQIAGCIA NSCSGTNAYR YGTMKENVVN ITMCMADGTI VKTKRRPRKS SAGYNLNGLI 

       310        320        330        340        350        360 
IGSEGTLGIV TEATIKCHVR STFETVAVVP FPTVSDAASC SSHLIQAGIQ LNAMELLDDN 

       370        380        390        400        410        420 
MMKIINQSGA TSKDNWVESP TLFFKIGGRS EQIIQEVIKE VEKIASQHNN TKFEFATDED 

       430        440        450        460        470        480 
SKLELWEARK VALWSTIDTG RKTNPDANIW TTDVAVPISK FADVINATKE EMNASGLLTS 

       490        500        510        520        530        540 
LVGHAGDGNF HAFIIYNTEQ RKTAETIVEN MVKRAIDAEG TCTGEHGVGI GKRDYLLEEV 

       550        560        570 
GEDTVAVMRK LKLALDPKRI LNPDKIFKID PNDHQH 

Q12627 in FASTA format

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