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P28037

- AL1L1_RAT

UniProt

P28037 - AL1L1_RAT

Protein

Cytosolic 10-formyltetrahydrofolate dehydrogenase

Gene

Aldh1l1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 3 (21 Mar 2012)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    10-formyltetrahydrofolate + NADP+ + H2O = tetrahydrofolate + CO2 + NADPH.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei106 – 1061Proton donorBy similarity
    Binding sitei142 – 1421SubstrateBy similarity
    Sitei142 – 1421Essential for catalytic activity
    Active sitei673 – 6731Proton acceptorCurated
    Active sitei707 – 7071Proton donorCurated
    Binding sitei757 – 7571NADP2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi571 – 5733NADP2 Publications
    Nucleotide bindingi597 – 6004NADP2 Publications
    Nucleotide bindingi630 – 6356NADP2 Publications
    Nucleotide bindingi650 – 6512NADP2 Publications
    Nucleotide bindingi804 – 8063NADP2 Publications

    GO - Molecular functioni

    1. aldehyde dehydrogenase (NADP+) activity Source: UniProtKB
    2. aldehyde dehydrogenase [NAD(P)+] activity Source: RGD
    3. formyltetrahydrofolate dehydrogenase activity Source: RGD
    4. hydroxymethyl-, formyl- and related transferase activity Source: InterPro
    5. methyltransferase activity Source: InterPro
    6. protein complex binding Source: RGD

    GO - Biological processi

    1. 10-formyltetrahydrofolate catabolic process Source: InterPro
    2. one-carbon metabolic process Source: UniProtKB-KW
    3. tetrahydrofolate biosynthetic process Source: RGD

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    One-carbon metabolism

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BRENDAi1.5.1.6. 5301.
    SABIO-RKP28037.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytosolic 10-formyltetrahydrofolate dehydrogenase (EC:1.5.1.6)
    Short name:
    10-FTHFDH
    Short name:
    FDH
    Alternative name(s):
    Aldehyde dehydrogenase family 1 member L1
    FBP-CI
    Gene namesi
    Name:Aldh1l1
    Synonyms:Fthfd
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi621294. Aldh1l1.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytosol Source: RGD
    2. protein complex Source: RGD

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi142 – 1421D → A, N, E or Q: Loss of hydrolase activity. 1 Publication
    Mutagenesisi673 – 6731E → A: Loss of aldehyde dehydrogenase activity. 1 Publication
    Mutagenesisi707 – 7071C → A: Loss of dehydrogenase activity. No effect on hydrolase activity and NADP binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 902902Cytosolic 10-formyltetrahydrofolate dehydrogenasePRO_0000199422Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei38 – 381N6-succinyllysineBy similarity
    Modified residuei354 – 3541O-(pantetheine 4'-phosphoryl)serine; alternateCurated
    Modified residuei354 – 3541Phosphoserine; alternate1 Publication
    Modified residuei767 – 7671N6-succinyllysineBy similarity

    Keywords - PTMi

    Phosphopantetheine, Phosphoprotein

    Proteomic databases

    PRIDEiP28037.

    PTM databases

    PhosphoSiteiP28037.

    Expressioni

    Gene expression databases

    GenevestigatoriP28037.

    Interactioni

    Subunit structurei

    Homotetramer.3 Publications

    Protein-protein interaction databases

    MINTiMINT-4565983.

    Structurei

    Secondary structure

    1
    902
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 76
    Helixi10 – 2112
    Beta strandi25 – 306
    Helixi41 – 499
    Beta strandi59 – 613
    Helixi67 – 748
    Beta strandi79 – 857
    Helixi92 – 954
    Beta strandi96 – 983
    Beta strandi102 – 1087
    Turni110 – 1134
    Beta strandi114 – 1163
    Helixi118 – 1247
    Beta strandi128 – 1369
    Beta strandi139 – 1424
    Beta strandi146 – 1538
    Helixi160 – 1667
    Helixi168 – 18518
    Helixi206 – 2094
    Beta strandi213 – 2153
    Helixi217 – 2259
    Turni226 – 2316
    Beta strandi233 – 2375
    Beta strandi240 – 24910
    Beta strandi258 – 2603
    Beta strandi271 – 2733
    Beta strandi276 – 2805
    Beta strandi286 – 2949
    Beta strandi299 – 3013
    Helixi302 – 3043
    Beta strandi409 – 4135
    Beta strandi416 – 4205
    Beta strandi423 – 4264
    Beta strandi429 – 4313
    Helixi434 – 4363
    Beta strandi438 – 4425
    Turni444 – 4463
    Beta strandi449 – 4546
    Helixi458 – 47316
    Helixi476 – 4783
    Helixi482 – 49817
    Helixi500 – 51112
    Helixi515 – 5206
    Turni521 – 5233
    Helixi524 – 53613
    Helixi537 – 5393
    Beta strandi542 – 5454
    Beta strandi553 – 56311
    Beta strandi566 – 5705
    Beta strandi573 – 5753
    Helixi576 – 58914
    Beta strandi593 – 5975
    Helixi604 – 61512
    Beta strandi622 – 6254
    Helixi630 – 63910
    Beta strandi645 – 6506
    Helixi652 – 66413
    Beta strandi669 – 6735
    Beta strandi678 – 6825
    Helixi688 – 70013
    Helixi701 – 7044
    Beta strandi710 – 7167
    Helixi717 – 73115
    Helixi752 – 76716
    Beta strandi771 – 7744
    Beta strandi780 – 7834
    Beta strandi789 – 7935
    Helixi799 – 8013
    Beta strandi807 – 8159
    Helixi821 – 8277
    Beta strandi830 – 8345
    Beta strandi837 – 8393
    Helixi843 – 85210
    Beta strandi855 – 8617
    Helixi876 – 8783
    Beta strandi879 – 8813
    Helixi885 – 8906
    Beta strandi893 – 90210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1S3IX-ray2.30A1-310[»]
    2O2PX-ray1.70A/B/C/D397-902[»]
    2O2QX-ray2.00A/B/C/D397-902[»]
    2O2RX-ray2.20A/B/C/D397-902[»]
    3RHJX-ray1.89A/B/C/D397-902[»]
    3RHLX-ray2.00A/B/C/D397-902[»]
    3RHMX-ray2.38A/B/C/D397-902[»]
    3RHOX-ray2.26A/B/C/D397-902[»]
    3RHPX-ray2.50A/B/C/D397-902[»]
    3RHQX-ray2.10A/B/C/D397-902[»]
    3RHRX-ray2.30A/B/C/D397-902[»]
    4GNZX-ray2.30A/B/C/D397-902[»]
    4GO0X-ray3.38A/B/C/D397-902[»]
    4GO2X-ray2.28A/B/C/D397-902[»]
    ProteinModelPortaliP28037.
    SMRiP28037. Positions 1-402, 405-902.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP28037.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini323 – 39270Acyl carrierPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 203203GARTAdd
    BLAST
    Regioni88 – 903Substrate bindingBy similarity
    Regioni417 – 902486Aldehyde dehydrogenaseAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the GART family.Curated
    In the C-terminal section; belongs to the aldehyde dehydrogenase family. ALDH1L subfamily.Curated
    Contains 1 acyl carrier domain.PROSITE-ProRule annotation

    Phylogenomic databases

    HOVERGENiHBG051668.
    KOiK00289.

    Family and domain databases

    Gene3Di1.10.1200.10. 1 hit.
    3.10.25.10. 1 hit.
    3.40.309.10. 1 hit.
    3.40.50.170. 1 hit.
    3.40.605.10. 1 hit.
    InterProiIPR011407. 10_FTHF_DH.
    IPR009081. Acyl_carrier_prot-like.
    IPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016160. Ald_DH_CS_CYS.
    IPR029510. Ald_DH_CS_GLU.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    IPR005793. Formyl_trans_C.
    IPR002376. Formyl_transf_N.
    IPR011034. Formyl_transferase_C-like.
    IPR001555. GART_AS.
    [Graphical view]
    PfamiPF00171. Aldedh. 1 hit.
    PF02911. Formyl_trans_C. 1 hit.
    PF00551. Formyl_trans_N. 1 hit.
    PF00550. PP-binding. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036489. 10-FTHFDH. 1 hit.
    SUPFAMiSSF47336. SSF47336. 1 hit.
    SSF50486. SSF50486. 1 hit.
    SSF53328. SSF53328. 1 hit.
    SSF53720. SSF53720. 1 hit.
    PROSITEiPS50075. ACP_DOMAIN. 1 hit.
    PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
    PS00373. GART. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P28037-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKIAVIGQSL FGQEVYCQLR KEGHEVVGVF TIPDKDGKAD PLGLEAEKDG    50
    VPVFKFPRWR ARGQALPEVV AKYQALGAEL NVLPFCSQFI PMEVINAPRH 100
    GSIIYHPSLL PRHRGASAIN WTLIHGDKKG GFTIFWADDG LDTGDLLLQK 150
    ECEVLPDDTV STLYNRFLFP EGIKGMVQAV RLIAEGTAPR CPQSEEGATY 200
    EGIQKKETAK INWDQPAEAI HNWIRGNDKV PGAWTEACGQ KLTFFNSTLN 250
    TSGLSTQGEA LPIPGAHRPG VVTKAGLILF GNDDRMLLVK NIQLEDGKMM 300
    PASQFFKGSA SSDLELTEAE LATAEAVRSS WMRILPNVPE VEDSTDFFKS 350
    GAASVDVVRL VEEVKELCDG LELENEDVYM ATTFRGFIQL LVRKLRGEDD 400
    ESECVINYVE KAVNKLTLQM PYQLFIGGEF VDAEGSKTYN TINPTDGSVI 450
    CQVSLAQVSD VDKAVAAAKE AFENGLWGKI NARDRGRLLY RLADVMEQHQ 500
    EELATIEALD AGAVYTLALK THVGMSIQTF RYFAGWCDKI QGATIPINQA 550
    RPNRNLTLTK KEPVGVCGIV IPWNYPLMML SWKTAACLAA GNTVVIKPAQ 600
    VTPLTALKFA ELTLKAGIPK GVVNILPGSG SLVGQRLSDH PDVRKIGFTG 650
    STEVGKHIMK SCALSNVKKV SLELGGKSPL IIFADCDLNK AVQMGMSSVF 700
    FNKGENCIAA GRLFVEESIH NQFVQKVVEE VEKMKIGNPL ERDTNHGPQN 750
    HEAHLRKLVE YCQRGVKEGA TLVCGGNQVP RPGFFFQPTV FTDVEDHMYI 800
    AKEESFGPIM IISRFADGDV DAVLSRANAT EFGLASGVFT RDINKALYVS 850
    DKLQAGTVFI NTYNKTDVAA PFGGFKQSGF GKDLGEAALN EYLRIKTVTF 900
    EY 902
    Length:902
    Mass (Da):98,874
    Last modified:March 21, 2012 - v3
    Checksum:i562A8CBD73D6474A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti51 – 522VP → RA in AAA70429. (PubMed:1848231)Curated
    Sequence conflicti283 – 2842DD → EH in AAA70429. (PubMed:1848231)Curated
    Sequence conflicti386 – 3861G → E in AAA70429. (PubMed:1848231)Curated
    Sequence conflicti411 – 4111K → R in AAA70429. (PubMed:1848231)Curated
    Sequence conflicti511 – 5111A → R in AAA70429. (PubMed:1848231)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59861 mRNA. Translation: AAA70429.1.
    BC089101 mRNA. Translation: AAH89101.1.
    PIRiA23709. A60560.
    RefSeqiNP_071992.1. NM_022547.1.
    UniGeneiRn.2328.

    Genome annotation databases

    GeneIDi64392.
    KEGGirno:64392.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59861 mRNA. Translation: AAA70429.1 .
    BC089101 mRNA. Translation: AAH89101.1 .
    PIRi A23709. A60560.
    RefSeqi NP_071992.1. NM_022547.1.
    UniGenei Rn.2328.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1S3I X-ray 2.30 A 1-310 [» ]
    2O2P X-ray 1.70 A/B/C/D 397-902 [» ]
    2O2Q X-ray 2.00 A/B/C/D 397-902 [» ]
    2O2R X-ray 2.20 A/B/C/D 397-902 [» ]
    3RHJ X-ray 1.89 A/B/C/D 397-902 [» ]
    3RHL X-ray 2.00 A/B/C/D 397-902 [» ]
    3RHM X-ray 2.38 A/B/C/D 397-902 [» ]
    3RHO X-ray 2.26 A/B/C/D 397-902 [» ]
    3RHP X-ray 2.50 A/B/C/D 397-902 [» ]
    3RHQ X-ray 2.10 A/B/C/D 397-902 [» ]
    3RHR X-ray 2.30 A/B/C/D 397-902 [» ]
    4GNZ X-ray 2.30 A/B/C/D 397-902 [» ]
    4GO0 X-ray 3.38 A/B/C/D 397-902 [» ]
    4GO2 X-ray 2.28 A/B/C/D 397-902 [» ]
    ProteinModelPortali P28037.
    SMRi P28037. Positions 1-402, 405-902.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-4565983.

    PTM databases

    PhosphoSitei P28037.

    Proteomic databases

    PRIDEi P28037.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 64392.
    KEGGi rno:64392.

    Organism-specific databases

    CTDi 10840.
    RGDi 621294. Aldh1l1.

    Phylogenomic databases

    HOVERGENi HBG051668.
    KOi K00289.

    Enzyme and pathway databases

    BRENDAi 1.5.1.6. 5301.
    SABIO-RK P28037.

    Miscellaneous databases

    EvolutionaryTracei P28037.
    NextBioi 613150.

    Gene expression databases

    Genevestigatori P28037.

    Family and domain databases

    Gene3Di 1.10.1200.10. 1 hit.
    3.10.25.10. 1 hit.
    3.40.309.10. 1 hit.
    3.40.50.170. 1 hit.
    3.40.605.10. 1 hit.
    InterProi IPR011407. 10_FTHF_DH.
    IPR009081. Acyl_carrier_prot-like.
    IPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016160. Ald_DH_CS_CYS.
    IPR029510. Ald_DH_CS_GLU.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    IPR005793. Formyl_trans_C.
    IPR002376. Formyl_transf_N.
    IPR011034. Formyl_transferase_C-like.
    IPR001555. GART_AS.
    [Graphical view ]
    Pfami PF00171. Aldedh. 1 hit.
    PF02911. Formyl_trans_C. 1 hit.
    PF00551. Formyl_trans_N. 1 hit.
    PF00550. PP-binding. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036489. 10-FTHFDH. 1 hit.
    SUPFAMi SSF47336. SSF47336. 1 hit.
    SSF50486. SSF50486. 1 hit.
    SSF53328. SSF53328. 1 hit.
    SSF53720. SSF53720. 1 hit.
    PROSITEi PS50075. ACP_DOMAIN. 1 hit.
    PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
    PS00373. GART. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of cDNA clones for rat liver 10-formyltetrahydrofolate dehydrogenase."
      Cook R.J., Lloyd R.S., Wagner C.
      J. Biol. Chem. 266:4965-4973(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Strain: Sprague-Dawley.
      Tissue: Liver.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Ovary.
    3. "Aspartate 142 is involved in both hydrolase and dehydrogenase catalytic centers of 10-formyltetrahydrofolate dehydrogenase."
      Krupenko S.A., Wagner C.
      J. Biol. Chem. 274:35777-35784(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF N-TERMINUS, MUTAGENESIS OF ASP-142.
    4. "Resolution of rat liver 10-formyltetrahydrofolate dehydrogenase/hydrolase activities."
      Case G.L., Kaisaki P.J., Steele R.D.
      J. Biol. Chem. 263:10204-10207(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    5. "Cysteine 707 is involved in the dehydrogenase activity site of rat 10-formyltetrahydrofolate dehydrogenase."
      Krupenko S.A., Wagner C., Cook R.J.
      J. Biol. Chem. 270:519-522(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-707, FUNCTION, SUBUNIT.
    6. "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS."
      Moser K., White F.M.
      J. Proteome Res. 5:98-104(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "The crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase: mechanism of hydrolysis and its interplay with the dehydrogenase domain."
      Chumanevich A.A., Krupenko S.A., Davies C.
      J. Biol. Chem. 279:14355-14364(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-309, CATALYTIC ACTIVITY.
    8. "Crystal structures of the carboxyl terminal domain of rat 10-formyltetrahydrofolate dehydrogenase: implications for the catalytic mechanism of aldehyde dehydrogenases."
      Tsybovsky Y., Donato H., Krupenko N.I., Davies C., Krupenko S.A.
      Biochemistry 46:2917-2929(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 397-902 IN COMPLEX WITH NADP, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-673, ACTIVE SITE.
    9. "Conserved catalytic residues of the ALDH1L1 aldehyde dehydrogenase domain control binding and discharging of the coenzyme."
      Tsybovsky Y., Krupenko S.A.
      J. Biol. Chem. 286:23357-23367(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 397-902 IN COMPLEX WITH NADP, ACTIVE SITE, SUBUNIT.

    Entry informationi

    Entry nameiAL1L1_RAT
    AccessioniPrimary (citable) accession number: P28037
    Secondary accession number(s): Q5HZB2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: March 21, 2012
    Last modified: October 1, 2014
    This is version 135 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    The phosphoserine observed at Ser-354 in PubMed:16396499 undoubtedly results from the secondary neutral loss of pantetheine from the phosphodiester linked cofactor.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3