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UniProtKB/Swiss-Prot entry O75891


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

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Entry information
Entry name FTHFD_HUMAN
Primary accession number O75891
Secondary accession number Q68CS1
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on February 15, 2005 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 78)
Name and origin of the protein
Protein name 10-formyltetrahydrofolate dehydrogenase
Synonyms 10-FTHFDH
EC 1.5.1.6
Aldehyde dehydrogenase family 1 member L1
Gene name
Name: ALDH1L1
Synonyms: FTHFD
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Hong M.H., Lee Y., Kim J.W., Kang B.S., Choe I.S.;
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon carcinoma;
The German cDNA consortium;
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[3]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-307.
Ogg D.J., Stenmark P., Arrowsmith C., Edwards A., Ehn M., Graslund S., Hammarstrom M., Hallberg M., Kotenyova T., Nilsson-Ehle P., Nordlund P., Persson C., Sagemark J., Schuler H., Sundstrom M., Thorsell A., Weigelt J.;
"Crystal structure of human 10-formyltetrahydrofolate dehydrogenase.";
Submitted (JUL-2005) to the PDB data bank.
[4]
STRUCTURE BY NMR OF 303-405.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RSGI RUH-033, a PP-binding domain of 10-FTHFDH from human cDNA.";
Submitted (NOV-2005) to the PDB data bank.
[5]
VARIANT [LARGE SCALE ANALYSIS] VAL-511.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
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
AF052732; AAC35000.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR749807; CAH18667.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_036322.2; -.
UniGene Hs.434435
3D structure databases
PDB
2BW0; X-ray; 1.70 A; A=1-307.[ExPASy / RCSB / EBI]
2CFI; X-ray; 1.85 A; A=-.[ExPASy / RCSB / EBI]
2CQ8; NMR; -; A=303-401.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2BW0; -.
2CFI; -.
2CQ8; -.
SMR O75891; 406-902.
ModBase O75891.
PTM databases
PhosphoSite O75891; -.
Organism-specific databases
HGNC HGNC:3978; ALDH1L1.
GenAtlas ALDH1L1.
MIM 600249; gene. [NCBI / EBI]
PharmGKB PA28393; -.
GeneCards O75891.
Gene expression databases
ArrayExpress O75891; -.
CleanEx HS_ALDH1L1; -.
GermOnline ENSG00000144908; Homo sapiens.
Ontologies
GO
GO:0003824; Molecular function: catalytic activity (traceable author statement from ProtInc).
GO:0009258; Biological process: 10-formyltetrahydrofolate catabolic process (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR011407; 10_FTHF_DHase.
IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
IPR005793; Formyl_trans_C.
IPR002376; Formyl_transf_N.
IPR001555; GART_AS.
IPR006163; Phsphopanteth_bd.
IPR006162; Ppantne_S.
Graphical view of domain structure.
Gene3D G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
G3DSA:3.10.25.10; Formyl_trans_C; 1.
G3DSA:3.40.50.170; Formyl_transf_N; 1.
PANTHER PTHR11699; Aldehyde_dehyd; 1.
Pfam PF00171; Aldedh; 1.
PF02911; Formyl_trans_C; 1.
PF00551; Formyl_trans_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF036489; 10-FTHFDH; 1.
PROSITE PS50075; ACP_DOMAIN; 1.
PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PS00373; GART; 1.
PS00012; PHOSPHOPANTETHEINE; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).
BLOCKS O75891.
Genome annotation databases
Ensembl ENSG00000144908; Homo sapiens. [Contig view]
GeneID 10840; -.
KEGG hsa:10840; -.
NMPDR fig|9606.3.peg.23112; -.
Phylogenomic databases
HOVERGEN O75891; -.
Other
DrugBank DB00116; Tetrahydrofolic acid.
LinkHub O75891; -.
SOURCE ALDH1L1; Homo sapiens.
ProtoNet O75891.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; NADP; One-carbon metabolism; Oxidoreductase; Phosphopantetheine; Phosphoprotein; Polymorphism.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   902  902     10-formyltetrahydrofolate dehydrogenase. PRO_0000199419
DOMAIN   323   392  70     Acyl carrier. 
REGION   1   203  203     GART. 
REGION   417   902  486     Aldehyde dehydrogenase. 
ACT_SITE   106   106        Proton donor (By similarity). 
ACT_SITE   673   673        By similarity. 
ACT_SITE   707   707        By similarity. 
BINDING   354   354        Phosphopantetheine (covalent) (By similarity). 
SITE   142   142  1     Essential for catalytic activity (By similarity). 
MOD_RES   354   354        Phosphoserine (By similarity). 
VARIANT   511   511  1     A -> V (in a colorectal cancer sample; somatic mutation). VAR_036101 
CONFLICT   63    63        G -> A (in Ref. 1; AAC35000). 
CONFLICT   85    85        F -> S (in Ref. 1; AAC35000). 
CONFLICT   176   176        M -> V (in Ref. 1; AAC35000). 
CONFLICT   195   195        E -> K (in Ref. 1; AAC35000). 
CONFLICT   470   470        D -> G (in Ref. 1; AAC35000). 
CONFLICT   677   677        K -> E (in Ref. 1; AAC35000). 
CONFLICT   680   680        L -> F (in Ref. 1; AAC35000). 
CONFLICT   702   702        N -> S (in Ref. 1; AAC35000). 
STRAND   2     6  5      
HELIX   9    21  13      
STRAND   25    31  7      
HELIX   41    49  9      
STRAND   53    55  3      
HELIX   67    74  8      
STRAND   79    85  7      
HELIX   92    95  4      
STRAND   102   108  7      
TURN   110   113  4      
STRAND   114   116  3      
HELIX   118   124  7      
STRAND   128   136  9      
STRAND   139   142  4      
STRAND   146   153  8      
HELIX   160   166  7      
TURN   167   169  3      
HELIX   170   185  16      
HELIX   206   209  4      
HELIX   217   225  9      
TURN   226   231  6      
STRAND   234   237  4      
STRAND   240   249  10      
STRAND   258   261  4      
STRAND   270   273  4      
STRAND   276   280  5      
STRAND   286   293  8      
STRAND   299   301  3      
HELIX   302   304  3      
HELIX   320   334  15      
HELIX   347   351  5      
HELIX   356   367  12      
HELIX   375   380  6      
HELIX   384   397  14      
Sequence information
Length: 902 AA [This is the length of the unprocessed precursor] Molecular weight: 98829 Da [This is the MW of the unprocessed precursor] CRC64: D92CB2930617F7CF [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKIAVIGQSL FGQEVYCHLR KEGHEVVGVF TVPDKDGKAD PLGLEAEKDG VPVFKYSRWR 

        70         80         90        100        110        120 
AKGQALPDVV AKYQALGAEL NVLPFCSQFI PMEIISAPRH GSIIYHPSLL PRHRGASAIN 

       130        140        150        160        170        180 
WTLIHGDKKG GFSIFWADDG LDTGDLLLQK ECEVLPDDTV STLYNRFLFP EGIKGMVQAV 

       190        200        210        220        230        240 
RLIAEGKAPR LPQPEEGATY EGIQKKETAK INWDQPAEAI HNWIRGNDKV PGAWTEACEQ 

       250        260        270        280        290        300 
KLTFFNSTLN TSGLVPEGDA LPIPGAHRPG VVTKAGLILF GNDDKMLLVK NIQLEDGKMI 

       310        320        330        340        350        360 
LASNFFKGAA SSVLELTEAE LVTAEAVRSV WQRILPKVLE VEDSTDFFKS GAASVDVVRL 

       370        380        390        400        410        420 
VEEVKELCDG LELENEDVYM ASTFGDFIQL LVRKLRGDDE EGECSIDYVE MAVNKRTVRM 

       430        440        450        460        470        480 
PHQLFIGGEF VDAEGAKTSE TINPTDGSVI CQVSLAQVTD VDKAVAAAKD AFENGRWGKI 

       490        500        510        520        530        540 
SARDRGRLMY RLADLMEQHQ EELATIEALD AGAVYTLALK THVGMSIQTF RYFAGWCDKI 

       550        560        570        580        590        600 
QGSTIPINQA RPNRNLTLTR KEPVGVCGII IPWNYPLMML SWKTAACLAA GNTVVIKPAQ 

       610        620        630        640        650        660 
VTPLTALKFA ELTLKAGIPK GVVNVLPGSG SLVGQRLSDH PDVRKIGFTG STEVGKHIMK 

       670        680        690        700        710        720 
SCAISNVKKV SLELGGKSPL IIFADCDLNK AVQMGMSSVF FNKGENCIAA GRLFVEDSIH 

       730        740        750        760        770        780 
DEFVRRVVEE VRKMKVGNPL DRDTDHGPQN HHAHLVKLME YCQHGVKEGA TLVCGGNQVP 

       790        800        810        820        830        840 
RPGFFFEPTV FTDVEDHMFI AKEESFGPVM IISRFADGDL DAVLSRANAT EFGLASGVFT 

       850        860        870        880        890        900 
RDINKALYVS DKLQAGTVFV NTYNKTDVAA PFGGFKQSGF GKDLGEAALN EYLRVKTVTF 


EY 

O75891 in FASTA format

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