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UniProtKB/Swiss-Prot entry Q1AXT3

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

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Entry information
Entry name FOLD1_RUBXD
Primary accession number Q1AXT3
Secondary accession numbers None
Integrated into Swiss-Prot on December 12, 2006
Sequence was last modified on July 11, 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: Rxyl_0827
From
Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129) [TaxID: 266117] [HAMAP proteome]
Taxonomy Bacteria; Actinobacteria; Rubrobacteridae; Rubrobacterales; Rubrobacterineae; Rubrobacteraceae; Rubrobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S., Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
"Complete sequence of Rubrobacter xylanophilus DSM 9941.";
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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
CP000386; ABG03795.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_643607.1; -.
3D structure databases
ModBase Q1AXT3.
Enzyme and pathway databases
BioCyc RXYL266117:RXYL_0827-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; FALSE_NEG.
Genome annotation databases
GeneID 4117079; -.
GenomeReviews CP000386_GR; Rxyl_0827.
KEGG rxy:Rxyl_0827; -.
NMPDR fig|266117.6.peg.753; -.
Phylogenomic databases
HOGENOM Q1AXT3; -.
Genome annotation databases
CMR Q1AXT3; Rxyl_0827.
Other
ProtoNet Q1AXT3.
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   284  284     Bifunctional protein folD 1. PRO_0000268485
Sequence information
Length: 284 AA [This is the length of the unprocessed precursor] Molecular weight: 29977 Da [This is the MW of the unprocessed precursor] CRC64: E077D503AF9AD8DD [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MARLLDGRSV AAQIRAEVAE GVSELKRRGV PVRLDVILAG EDPASVTYVS NKRRDCAEVG 

        70         80         90        100        110        120 
IESRLHAFPA DVPQKELLAL VERLNGDPEV SGFFIQLPLP GGVDPLPLLS AIDPSKDVDG 

       130        140        150        160        170        180 
LSPQSAGRLA VGLPSLLPCT PHGVIQLLRR SGVGLEGREA VVVGRSNLVG KPLALLLLRE 

       190        200        210        220        230        240 
NATVTVCHSR TRDLAGVTRR AEVLVVAAGR RGMVGAEHVR EGAVVVDVGI HRAEDGGLTG 

       250        260        270        280 
DVRQEEVAAR AAALTPVPGG VGPMTRAMLL YNTLEAARLR EERA
Q1AXT3 in FASTA format

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