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UniProtKB/Swiss-Prot entry Q5LNV2

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

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Entry information
Entry name FOLD1_SILPO
Primary accession number Q5LNV2
Secondary accession numbers None
Integrated into Swiss-Prot on December 12, 2006
Sequence was last modified on February 1, 2005 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 28)
Name and origin of the protein
Protein name Bifunctional protein folD 1/3
Synonyms None
Includes Methylenetetrahydrofolate dehydrogenase
     (EC 1.5.1.5)
Methenyltetrahydrofolate cyclohydrolase
     (EC 3.5.4.9)
Gene names
Name: folD1
OrderedLocusNames: SPO1559
and
Name: folD3
OrderedLocusNames: SPO3101
From
Silicibacter pomeroyi [TaxID: 89184] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; Rhodobacteraceae; Silicibacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
DOI=10.1038/nature03170; PubMed=15602564 [NCBI, ExPASy, EBI, Israel, Japan]
Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B., Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
"Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine environment.";
Nature 432:910-913(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
CP000031; AAV96336.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000031; AAV94846.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_166800.1; -.
YP_168304.1; -.
3D structure databases
ModBase Q5LNV2.
Enzyme and pathway databases
BioCyc SPOM246200:SPO_1559-MON; -.
SPOM246200:SPO_3101-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.
ProtoNet Q5LNV2.
Genome annotation databases
GeneID 3193798; -.
3194901; -.
GenomeReviews CP000031_GR; SPO1559.
CP000031_GR; SPO3101.
KEGG sil:SPO1559; -.
sil:SPO3101; -.
Phylogenomic databases
HOGENOM Q5LNV2; -.
Genome annotation databases
CMR Q5LNV2; SPO1559.
Other
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   296  296     Bifunctional protein folD 1/3. PRO_0000268501
Sequence information
Length: 296 AA [This is the length of the unprocessed precursor] Molecular weight: 30926 Da [This is the MW of the unprocessed precursor] CRC64: E8331BCC13CE786C [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAATVIDGKA FAARIRGQVA EHVAELKAGH GITPGLAVVL VGEDPASQVY VRSKGKQTVE 

        70         80         90        100        110        120 
VGMNSYEHKL DADTSEADLL ALIDRLNGDP DVHGILVQLP LPGHLDEDLV INAIDPAKDV 

       130        140        150        160        170        180 
DGFHISNVGL LGTGQKSMVP CTPLGCLMML RDHHGSLSGM DAVVIGRSNI VGKPMAQLLL 

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

       250        260        270        280        290 
TRLVGDVHYD SCAQVAGAIT PVPGGVGPMT IACLLANTLT ACTRANKLTE PDGLTP
Q5LNV2 in FASTA format

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