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P28037

- AL1L1_RAT

UniProt

P28037 - AL1L1_RAT

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Protein

Cytosolic 10-formyltetrahydrofolate dehydrogenase

Gene

Aldh1l1

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 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
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 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.
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.
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

        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)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.
InParanoidi P28037.
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: October 29, 2014
This is version 136 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