ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q987T6


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name FOLD2_RHILO
Primary accession number Q987T6
Secondary accession numbers None
Integrated into Swiss-Prot on December 12, 2006
Sequence was last modified on October 1, 2001 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 34)
Name and origin of the protein
Protein name Bifunctional protein folD 2
Synonyms None
Includes Methylenetetrahydrofolate dehydrogenase
     (EC 1.5.1.5)
Methenyltetrahydrofolate cyclohydrolase
     (EC 3.5.4.9)
Gene name
Name: folD2
OrderedLocusNames: mll6921
From
Rhizobium loti (Mesorhizobium loti) [TaxID: 381] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Phyllobacteriaceae; Mesorhizobium.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MAFF303099;
DOI=10.1093/dnares/7.6.331; PubMed=11214968 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.;
"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti.";
DNA Res. 7:331-338(2000).
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
BA000012; BAB53114.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_107328.1; -.
3D structure databases
HSSP P11586; 1A4I. [HSSP ENTRY / PDB]
ModBase Q987T6.
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; FALSE_NEG.
PS00767; THF_DHG_CYH_2; 1.
ProtoNet Q987T6.
Genome annotation databases
GeneID 1229983; -.
GenomeReviews BA000012_GR; mll6921.
KEGG mlo:mll6921; -.
NMPDR fig|266835.1.peg.5429; -.
Phylogenomic databases
HOGENOM Q987T6; -.
Genome annotation databases
CMR Q987T6; mll6921.
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   306  306     Bifunctional protein folD 2. PRO_0000268464
Sequence information
Length: 306 AA [This is the length of the unprocessed precursor] Molecular weight: 32228 Da [This is the MW of the unprocessed precursor] CRC64: FD73239C914E5450 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSLPDDSRYL KGGPVAQRII AAVREDAAIA KAEGFPPKLI SITVGDTDAV DVYVRNQRAK 

        70         80         90        100        110        120 
AQLAGIDFEE RRFPATITSG ELEAAIHGLN ADPRVTGIII QRPVPAHISV KTLQAAVHPL 

       130        140        150        160        170        180 
KDVEGMHPAS IGNIVYNQLD LAPCTAAASV ELLKETGLDL KGLEVVVVGH SEIVGKPIAF 

       190        200        210        220        230        240 
LLMSEGATVT VCHHLTRSVA AHARRADALF VAVGKPRLIK ADMVKPGAAV IDIGINSEIG 

       250        260        270        280        290        300 
PDGTSRIVGD VDTDSVKDVA SWITPVPGGV GPITVAILLR NTMVALSRQR ALYEATYGTA 


DRLAAE 

Q987T6 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!