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P28037

- AL1L1_RAT

UniProt

P28037 - AL1L1_RAT

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Protein
Cytosolic 10-formyltetrahydrofolate dehydrogenase
Gene
Aldh1l1, Fthfd
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei106 – 1061Proton donor By similarity
Binding sitei142 – 1421Substrate By similarity
Sitei142 – 1421Essential for catalytic activity
Active sitei673 – 6731Proton acceptor Inferred
Active sitei707 – 7071Proton donor Inferred
Binding sitei757 – 7571NADP

Regions

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

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
Complete GO annotation...

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
Complete GO annotation...

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 dehydrogenase
PRO_0000199422Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PRIDEiP28037.

PTM databases

PhosphoSiteiP28037.

Expressioni

Gene expression databases

GenevestigatoriP28037.

Interactioni

Subunit structurei

Homotetramer.2 Publications

Protein-protein interaction databases

MINTiMINT-4565983.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP28037.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini323 – 39270Acyl carrier
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 203203GART
Add
BLAST
Regioni88 – 903Substrate binding By similarity
Regioni417 – 902486Aldehyde dehydrogenase
Add
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the GART family.
In the C-terminal section; belongs to the aldehyde dehydrogenase family. ALDH1L subfamily.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 522VP → RA in AAA70429. 1 Publication
Sequence conflicti283 – 2842DD → EH in AAA70429. 1 Publication
Sequence conflicti386 – 3861G → E in AAA70429. 1 Publication
Sequence conflicti411 – 4111K → R in AAA70429. 1 Publication
Sequence conflicti511 – 5111A → R in AAA70429. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 134 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 1 Publication undoubtedly results from the secondary neutral loss of pantetheine from the phosphodiester linked cofactor.

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

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