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UniProtKB/Swiss-Prot entry Q167Y9

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

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Entry information
Entry name FOLD1_ROSDO
Primary accession number Q167Y9
Secondary accession numbers None
Integrated into Swiss-Prot on December 12, 2006
Sequence was last modified on July 25, 2006 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 20)
Name and origin of the protein
Protein name Bifunctional protein folD 1
Synonyms None
Includes Methylenetetrahydrofolate dehydrogenase
     (EC 1.5.1.5)
Methenyltetrahydrofolate cyclohydrolase
     (EC 3.5.4.9)
Gene name
Name: folD1
OrderedLocusNames: RD1_2105
From
Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp. (strain OCh 114)) (Roseobacter denitrificans) [TaxID: 375451] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; Rhodobacteraceae; Roseobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.01390-06; PubMed=17098896 [NCBI, ExPASy, EBI, Israel, Japan]
Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H., Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K., O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T., Touchman J.W.;
"The complete genome sequence of Roseobacter denitrificans reveals a mixotrophic rather than photosynthetic metabolism.";
J. Bacteriol. 189:683-690(2007).
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
CP000362; ABG31704.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_682390.1; -.
3D structure databases
ModBase Q167Y9.
Enzyme and pathway databases
BioCyc RDEN375451:RD1_2105-MON; -.
Ontologies
GO
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0004477; Molecular function: methenyltetrahydrofolate cyclohydrolase activity (inferred from electronic annotation from HAMAP).
GO:0004488; Molecular function: methylenetetrahydrofolate dehydrogenase (NADP+) activity (inferred from electronic annotation from HAMAP).
GO:0009396; Biological process: folic acid and derivative biosynthetic process (inferred from electronic annotation from InterPro).
GO:0000105; Biological process: histidine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0009086; Biological process: methionine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0006730; Biological process: one-carbon compound metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006164; Biological process: purine nucleotide biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_01576; -; 1.
PBIL [Tree]
InterPro IPR016040; NAD(P)-bd.
IPR000672; THF_DHase/CycOHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF00763; THF_DHG_CYH; 1.
PF02882; THF_DHG_CYH_C; 1.
Pfam graphical view of domain structure.
PRINTS PR00085; THFDHDRGNASE.
ProDom PD002300; THFDhg/Cyc_hydro; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00766; THF_DHG_CYH_1; 1.
PS00767; THF_DHG_CYH_2; 1.
Genome annotation databases
GeneID 4196651; -.
GenomeReviews CP000362_GR; RD1_2105.
KEGG rde:RD1_2105; -.
NMPDR fig|375451.6.peg.1965; -.
Phylogenomic databases
HOGENOM Q167Y9; -.
Genome annotation databases
CMR Q167Y9; RD1_2105.
Other
ProtoNet Q167Y9.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis; Hydrolase; Methionine biosynthesis; Multifunctional enzyme; NADP; One-carbon metabolism; Oxidoreductase; Purine biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   300  300     Bifunctional protein folD 1. PRO_0000268482
Sequence information
Length: 300 AA [This is the length of the unprocessed precursor] Molecular weight: 31313 Da [This is the MW of the unprocessed precursor] CRC64: ED4ED50BBF8BFDD1 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSATLIDGKA FAARVRAQVA EHVTRLKADH GITPGLAVVL VGQDPASQVY VRSKGKQTTE 

        70         80         90        100        110        120 
VGMKSVEHKL DADTSETDLL AVVDQLNKDP DIHGILVQLP LPGHLDEDLV INSIAPEKDV 

       130        140        150        160        170        180 
DGFHISNVGL LGTGQKSMVP CTPLGCLMML RDYHGSLLGM DAVVVGRSNI VGKPMAQLLL 

       190        200        210        220        230        240 
GDSCTVTIAH SRTKDLADVV RRADIVVAAV GRPEMVPGDW IKPGATVIDV GINRLDAPEK 

       250        260        270        280        290        300 
GEGKTRLVGD VDFDSCAAVA GAITPVPGGV GPMTIACLLA NTVTACCRAN GLEEPEGLTA
Q167Y9 in FASTA format

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