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Protein

Cytosolic 10-formyltetrahydrofolate dehydrogenase

Gene

Aldh1l1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei106Proton donorBy similarity1
Binding sitei142SubstrateBy similarity1
Sitei142Essential for catalytic activity1
Active sitei673Proton acceptorCurated1
Active sitei707Proton donorCurated1
Binding sitei757NADP2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi571 – 573NADP2 Publications3
Nucleotide bindingi597 – 600NADP2 Publications4
Nucleotide bindingi630 – 635NADP2 Publications6
Nucleotide bindingi650 – 651NADP2 Publications2
Nucleotide bindingi804 – 806NADP2 Publications3

GO - Molecular functioni

  • 4-trimethylammoniobutyraldehyde dehydrogenase activity Source: GO_Central
  • aldehyde dehydrogenase (NADP+) activity Source: UniProtKB
  • aldehyde dehydrogenase [NAD(P)+] activity Source: RGD
  • aminobutyraldehyde dehydrogenase activity Source: GO_Central
  • formyltetrahydrofolate dehydrogenase activity Source: RGD
  • hydroxymethyl-, formyl- and related transferase activity Source: InterPro
  • protein complex binding Source: RGD

GO - Biological processi

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
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621294. Aldh1l1.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytosol Source: RGD
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi142D → A, N, E or Q: Loss of hydrolase activity. 1 Publication1
Mutagenesisi673E → A: Loss of aldehyde dehydrogenase activity. 1 Publication1
Mutagenesisi707C → A: Loss of dehydrogenase activity. No effect on hydrolase activity and NADP binding. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3414419.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001994221 – 902Cytosolic 10-formyltetrahydrofolate dehydrogenaseAdd BLAST902

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei9PhosphoserineBy similarity1
Modified residuei38N6-succinyllysineBy similarity1
Modified residuei354O-(pantetheine 4'-phosphoryl)serine; alternateCurated1
Modified residuei354Phosphoserine; alternateCombined sources1
Modified residuei629PhosphoserineBy similarity1
Modified residuei631PhosphoserineBy similarity1
Modified residuei767N6-succinyllysineBy similarity1
Modified residuei825PhosphoserineBy similarity1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PeptideAtlasiP28037.
PRIDEiP28037.

PTM databases

iPTMnetiP28037.
PhosphoSitePlusiP28037.

Interactioni

Subunit structurei

Homotetramer.3 Publications

GO - Molecular functioni

  • protein complex binding Source: RGD

Protein-protein interaction databases

MINTiMINT-4565983.

Structurei

Secondary structure

1902
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 7Combined sources6
Helixi10 – 21Combined sources12
Beta strandi25 – 30Combined sources6
Helixi41 – 49Combined sources9
Beta strandi59 – 61Combined sources3
Helixi67 – 74Combined sources8
Beta strandi79 – 85Combined sources7
Helixi92 – 95Combined sources4
Beta strandi96 – 98Combined sources3
Beta strandi102 – 108Combined sources7
Turni110 – 113Combined sources4
Beta strandi114 – 116Combined sources3
Helixi118 – 124Combined sources7
Beta strandi128 – 136Combined sources9
Beta strandi139 – 142Combined sources4
Beta strandi146 – 153Combined sources8
Helixi160 – 166Combined sources7
Helixi168 – 185Combined sources18
Helixi206 – 209Combined sources4
Beta strandi213 – 215Combined sources3
Helixi217 – 225Combined sources9
Turni226 – 231Combined sources6
Beta strandi233 – 237Combined sources5
Beta strandi240 – 249Combined sources10
Beta strandi258 – 260Combined sources3
Beta strandi271 – 273Combined sources3
Beta strandi276 – 280Combined sources5
Beta strandi286 – 294Combined sources9
Beta strandi299 – 301Combined sources3
Helixi302 – 304Combined sources3
Beta strandi409 – 413Combined sources5
Beta strandi416 – 420Combined sources5
Beta strandi423 – 426Combined sources4
Beta strandi429 – 431Combined sources3
Helixi434 – 436Combined sources3
Beta strandi438 – 442Combined sources5
Turni444 – 446Combined sources3
Beta strandi449 – 454Combined sources6
Helixi458 – 473Combined sources16
Helixi476 – 478Combined sources3
Helixi482 – 498Combined sources17
Helixi500 – 511Combined sources12
Helixi515 – 520Combined sources6
Turni521 – 523Combined sources3
Helixi524 – 536Combined sources13
Helixi537 – 539Combined sources3
Beta strandi542 – 545Combined sources4
Beta strandi553 – 563Combined sources11
Beta strandi566 – 570Combined sources5
Beta strandi573 – 575Combined sources3
Helixi576 – 589Combined sources14
Beta strandi593 – 597Combined sources5
Helixi604 – 615Combined sources12
Beta strandi622 – 625Combined sources4
Helixi630 – 639Combined sources10
Beta strandi645 – 650Combined sources6
Helixi652 – 664Combined sources13
Beta strandi669 – 673Combined sources5
Beta strandi678 – 682Combined sources5
Helixi688 – 700Combined sources13
Helixi701 – 704Combined sources4
Beta strandi710 – 716Combined sources7
Helixi717 – 731Combined sources15
Helixi752 – 767Combined sources16
Beta strandi771 – 774Combined sources4
Beta strandi780 – 783Combined sources4
Beta strandi789 – 793Combined sources5
Helixi799 – 801Combined sources3
Beta strandi807 – 815Combined sources9
Helixi821 – 827Combined sources7
Beta strandi830 – 834Combined sources5
Beta strandi837 – 839Combined sources3
Helixi843 – 852Combined sources10
Beta strandi855 – 861Combined sources7
Helixi876 – 878Combined sources3
Beta strandi879 – 881Combined sources3
Helixi885 – 890Combined sources6
Beta strandi893 – 902Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28037.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini323 – 392Acyl carrierPROSITE-ProRule annotationAdd BLAST70

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 203GARTAdd BLAST203
Regioni88 – 90Substrate bindingBy similarity3
Regioni417 – 902Aldehyde dehydrogenaseAdd BLAST486

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.
InParanoidiP28037.
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.
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.
IPR009081. PP-bd_ACP.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
PF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 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

        10         20         30         40         50
MKIAVIGQSL FGQEVYCQLR KEGHEVVGVF TIPDKDGKAD PLGLEAEKDG
60 70 80 90 100
VPVFKFPRWR ARGQALPEVV AKYQALGAEL NVLPFCSQFI PMEVINAPRH
110 120 130 140 150
GSIIYHPSLL PRHRGASAIN WTLIHGDKKG GFTIFWADDG LDTGDLLLQK
160 170 180 190 200
ECEVLPDDTV STLYNRFLFP EGIKGMVQAV RLIAEGTAPR CPQSEEGATY
210 220 230 240 250
EGIQKKETAK INWDQPAEAI HNWIRGNDKV PGAWTEACGQ KLTFFNSTLN
260 270 280 290 300
TSGLSTQGEA LPIPGAHRPG VVTKAGLILF GNDDRMLLVK NIQLEDGKMM
310 320 330 340 350
PASQFFKGSA SSDLELTEAE LATAEAVRSS WMRILPNVPE VEDSTDFFKS
360 370 380 390 400
GAASVDVVRL VEEVKELCDG LELENEDVYM ATTFRGFIQL LVRKLRGEDD
410 420 430 440 450
ESECVINYVE KAVNKLTLQM PYQLFIGGEF VDAEGSKTYN TINPTDGSVI
460 470 480 490 500
CQVSLAQVSD VDKAVAAAKE AFENGLWGKI NARDRGRLLY RLADVMEQHQ
510 520 530 540 550
EELATIEALD AGAVYTLALK THVGMSIQTF RYFAGWCDKI QGATIPINQA
560 570 580 590 600
RPNRNLTLTK KEPVGVCGIV IPWNYPLMML SWKTAACLAA GNTVVIKPAQ
610 620 630 640 650
VTPLTALKFA ELTLKAGIPK GVVNILPGSG SLVGQRLSDH PDVRKIGFTG
660 670 680 690 700
STEVGKHIMK SCALSNVKKV SLELGGKSPL IIFADCDLNK AVQMGMSSVF
710 720 730 740 750
FNKGENCIAA GRLFVEESIH NQFVQKVVEE VEKMKIGNPL ERDTNHGPQN
760 770 780 790 800
HEAHLRKLVE YCQRGVKEGA TLVCGGNQVP RPGFFFQPTV FTDVEDHMYI
810 820 830 840 850
AKEESFGPIM IISRFADGDV DAVLSRANAT EFGLASGVFT RDINKALYVS
860 870 880 890 900
DKLQAGTVFI NTYNKTDVAA PFGGFKQSGF GKDLGEAALN EYLRIKTVTF

EY
Length:902
Mass (Da):98,874
Last modified:March 21, 2012 - v3
Checksum:i562A8CBD73D6474A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti51 – 52VP → RA in AAA70429 (PubMed:1848231).Curated2
Sequence conflicti283 – 284DD → EH in AAA70429 (PubMed:1848231).Curated2
Sequence conflicti386G → E in AAA70429 (PubMed:1848231).Curated1
Sequence conflicti411K → R in AAA70429 (PubMed:1848231).Curated1
Sequence conflicti511A → R in AAA70429 (PubMed:1848231).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
M59861 mRNA. Translation: AAA70429.1.
BC089101 mRNA. Translation: AAH89101.1.
PIRiA23709. A60560.
RefSeqiNP_071992.1. NM_022547.1.
UniGeneiRn.2328.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4565983.

Chemistry databases

ChEMBLiCHEMBL3414419.

PTM databases

iPTMnetiP28037.
PhosphoSitePlusiP28037.

Proteomic databases

PeptideAtlasiP28037.
PRIDEiP28037.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64392.
KEGGirno:64392.

Organism-specific databases

CTDi10840.
RGDi621294. Aldh1l1.

Phylogenomic databases

HOVERGENiHBG051668.
InParanoidiP28037.
KOiK00289.

Enzyme and pathway databases

BRENDAi1.5.1.6. 5301.
SABIO-RKP28037.

Miscellaneous databases

EvolutionaryTraceiP28037.
PROiP28037.

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.
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.
IPR009081. PP-bd_ACP.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
PF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 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]
ProtoNetiSearch...

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: November 2, 2016
This is version 153 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.