Gene HP1222 from Helicobacter pylori 26695: D-lactate dehydrogenase (dld)
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Member of NCBI Protein Clusters
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CLSK872525(See COMBREX Page ) (See NCBI page)
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NCBI Entrez GeneID
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898825
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UniProtKB accession
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RefSeq Protein accession
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NP_208014.1 (PROVISIONAL)
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Gene Symbol(s)
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- symbol: HP1222
- locus tag: HP1222
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Organism
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Helicobacter pylori 26695 (NCBI TaxID: 85962)
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Initiate the grant application process for experimentally validating this gene (Important notice about COMBREX grants.)
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Contribute a predicted function for this gene (free text, GO terms, or EC number) (info). Be sure to
check the list of current predicted functions in the section immediately below beforehand.
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Nominate this gene for the Gold Standard Gene Database (if you believe it has been experimentally
validated) (info).
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Post a comment about this gene to appear on this page (info).
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Functional Status
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blue (function predicted, no experimental evidence)
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Source of prediction
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NCBI Protein Clusters info
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BLASTP hits to experimentally validated proteins
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This gene does not have a BLAST match to any experimentally validated gene with an E value below 1e-5
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GO terms
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BP:
GO:0055114 : oxidation reduction : IEA
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MF:
GO:0003824 : catalytic activity : IEA
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MF:
GO:0009055 : electron carrier activity : IEA
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MF:
GO:0050660 : FAD binding : IEA
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MF:
GO:0051536 : iron-sulfur cluster binding : IEA
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MF:
GO:0016491 : oxidoreductase activity : IEA
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Domain Structure from CDD
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- GlpC: Fe-S oxidoreductase [Energy production and conversion]
- FAD_binding_4: FAD binding domain. This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyses the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyses the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan..... (More)
- GlcD: FAD/FMN-containing dehydrogenases [Energy production and conversion]
See domain structure on NCBI Conserved Domain Database
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Domain structure from Pfam
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See domain structure on Pfam Database
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The table at right lists genes that may be "functionally linked to" (i.e., participate in a common biological process, or form a protein complex with) the subject gene of this page,
as determined by two sequence-independent methods, including phylogenetic profiling and operon membership (determined by OperonDB).
(Info.)
These linkages may also be viewed graphically using the program VisANT, by clicking on the headers of the table.
Note: VisANT requires Java. To install the latest version of Java, see www.java.com
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| | HP1220 | ABC transporter, ATP-binding protein (yhcG) | | | | HP1221 | hypothetical protein | | | | HP0509 | glycolate oxidase subunit (glcD) | | |
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Metabolic Annotation from Palsson Lab
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Metabolic Reaction: LDH_D1
- Name
- D-lactate dehydrogenase
- Formula
- lac-DASH-D[c] + mqn6[c] <=> mql6[c] + pyr[c]
- Pathway
- Respiratory chain
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