Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q8R0Y6

Entry ID Method Resolution Chain Position Source
AF-Q8R0Y6-F1 Predicted AlphaFoldDB

61 variants for Q8R0Y6

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388845765 6 I>M No EVA
rs3388849600 10 L>V No EVA
rs3388849537 18 Q>H No EVA
rs3388839412 19 L>Q No EVA
rs3388849558 37 G>R No EVA
rs3388845282 53 V>M No EVA
rs3397102579 77 G>A No EVA
rs3388838496 115 G>E No EVA
rs240169178 153 D>E No EVA
rs3396968076 166 R>H No EVA
rs3388809242 168 L>P No EVA
rs3388851144 187 T>A No EVA
rs3388845773 188 A>T No EVA
rs36794236 210 M>R No EVA
rs263119818 275 A>E No EVA
rs263119818 275 A>V No EVA
rs3397098740 277 L>V No EVA
rs3397098737 279 L>R No EVA
rs3388843099 305 F>Y No EVA
rs3397092690 309 S>T No EVA
rs3396883275 312 S>R No EVA
rs3396624254 313 A>P No EVA
rs3396784818 315 E>K No EVA
rs3388845346 353 A>T No EVA
rs3388849567 374 E>D No EVA
rs3388838573 395 L>* No EVA
rs36884257 400 G>D No EVA
rs239432715 414 K>N No EVA
rs3388827711 429 E>D No EVA
rs3388845814 464 A>V No EVA
rs3388847398 468 A>G No EVA
rs3388845274 540 I>N No EVA
rs3397092640 545 I>* No EVA
rs3397092682 582 W>C No EVA
rs3396618378 582 W>S No EVA
rs3397038155 583 K>R No EVA
rs3397027832 586 A>S No EVA
rs3388839596 586 A>V No EVA
rs3388843112 609 F>L No EVA
rs3388833945 621 G>C No EVA
rs3397038114 621 G>D No EVA
rs3388843285 629 S>Y No EVA
rs3388833900 645 K>N No EVA
rs3388847486 691 A>V No EVA
rs3388847467 702 N>K No EVA
rs3388827718 704 G>R No EVA
rs3388839626 713 L>I No EVA
rs3388847422 755 L>M No EVA
rs3388809180 769 G>R No EVA
rs37608620 774 C>Y No EVA
rs3388839459 785 F>L No EVA
rs37064932 790 V>I No EVA
rs3388849542 798 M>V No EVA
rs38748377 806 F>L No EVA
rs3388849605 817 D>V No EVA
rs3388845327 830 T>I No EVA
rs3388843134 849 V>F No EVA
rs3388839405 850 S>N No EVA
rs36602348 855 A>T No EVA
rs3388833875 887 A>T No EVA
rs3388839616 898 V>A No EVA

No associated diseases with Q8R0Y6

7 regional properties for Q8R0Y6

Type Name Position InterPro Accession
active_site Phosphoribosylglycinamide formyltransferase, active site 131 - 154 IPR001555
domain Formyl transferase, N-terminal 1 - 180 IPR002376
domain Formyl transferase, C-terminal 205 - 309 IPR005793
domain Phosphopantetheine binding ACP domain 318 - 395 IPR009081
domain Aldehyde dehydrogenase domain 430 - 898 IPR015590
conserved_site Aldehyde dehydrogenase, cysteine active site 700 - 711 IPR016160
conserved_site Aldehyde dehydrogenase, glutamic acid active site 672 - 679 IPR029510

Functions

Description
EC Number 1.5.1.6 With NAD(+) or NADP(+) as acceptor
Subcellular Localization
  • Cytoplasm, cytosol
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
protein-containing complex A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.

6 GO annotations of molecular function

Name Definition
aldehyde dehydrogenase (NAD+) activity Catalysis of the reaction: an aldehyde + NAD+ + H2O = an acid + NADH + H+.
aldehyde dehydrogenase (NADP+) activity Catalysis of the reaction: an aldehyde + NADP+ + H2O = an acid + NADPH + H+.
aldehyde dehydrogenase [NAD(P)+] activity Catalysis of the reaction: an aldehyde + NAD(P)+ + H2O = an acid + NAD(P)H + H+.
formyltetrahydrofolate dehydrogenase activity Catalysis of the reaction: 10-formyltetrahydrofolate + H(2)O + NADP(+) = (6S)-5,6,7,8-tetrahydrofolate + CO(2) + H(+) + NADPH.
hydroxymethyl-, formyl- and related transferase activity Catalysis of the transfer of a hydroxymethyl- or formyl group from one compound (donor) to another (acceptor).
protein-containing complex binding Binding to a macromolecular complex.

5 GO annotations of biological process

Name Definition
10-formyltetrahydrofolate catabolic process The chemical reactions and pathways resulting in the breakdown of 10-formyltetrahydrofolate, the formylated derivative of tetrahydrofolate.
biosynthetic process The chemical reactions and pathways resulting in the formation of substances; typically the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.
folic acid metabolic process The chemical reactions and pathways involving folic acid, pteroylglutamic acid. Folic acid is widely distributed as a member of the vitamin B complex and is essential for the synthesis of purine and pyrimidines.
NADPH regeneration A metabolic process that generates a pool of NADPH by the reduction of NADP+.
one-carbon metabolic process The chemical reactions and pathways involving the transfer of one-carbon units in various oxidation states.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P28037 Aldh1l1 Cytosolic 10-formyltetrahydrofolate dehydrogenase Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MKIAVIGQSL FGQEVYCQLR KEGHEVVGVF TIPDKDGKAD PLGLEAEKDG VPVFKFPRWR
70 80 90 100 110 120
ARGQALPEVV AKYQALGAEL NVLPFCSQFI PMEVINAPRH GSIIYHPSLL PRHRGASAIN
130 140 150 160 170 180
WTLIHGDKKG GFTIFWADDG LDTGDLLLQK ECDVLPDDTV STLYNRFLFP EGIKGMVQAV
190 200 210 220 230 240
RLIAEGTAPR RPQPEEGATY EGIQKKETAM INWDQPAEAI HNWIRGNDKV PGAWTEACGQ
250 260 270 280 290 300
KLTFFNSTLN TSGLVAQGEA LPIPGAHRPG LVTKAGLILF GNDDRMLLVK NIQLEDGKMM
310 320 330 340 350 360
PASQFFKGSA SSALELTEEE LATAEAVRSS WMRILPNVPE VEDSTDFFKS GAASVDVVRL
370 380 390 400 410 420
VEEVKELCDG LELENEDVYM ATTFGDFIQL LVRKLRGEDG ESECVINYVE KAVKKLTLQM
430 440 450 460 470 480
PYQLFIGGEF VDAEGAKTYS TINPTDGSVI CQVSLAQVSD VDKAVAAAKE AFENGLWGKI
490 500 510 520 530 540
NARDRGRLLY RLADLMEQHQ EELATIEALD AGAVYTLALK THVGMSIQTF RYFAGWCDKI
550 560 570 580 590 600
QGATIPINQA RPNRNLTLTK KEPVGVCGIV IPWNYPLMML SWKTAACLAA GNTVVIKPAQ
610 620 630 640 650 660
VTPLTALKFA ELTLKAGIPK GVVNILPGSG SLVGQRLSDH PDVRKIGFTG STEVGKHIMK
670 680 690 700 710 720
SCALSNVKKV SLELGGKSPL IIFADCDLNK AVQMGMSSVF FNKGENCIAA GRLFVEDSIH
730 740 750 760 770 780
DQFVQKVVEE VGKMKIGNPL DRDTNHGPQN HEAHLRKLVE YCQRGVKEGA TLVCGGNQVP
790 800 810 820 830 840
RPGFFFQPTV FTDVEDHMYI AKEESFGPIM IISRFADGDV DAVLSRANAT EFGLASGVFT
850 860 870 880 890 900
RDINKALYVS DKLQAGTVFV NTYNKTDVAA PFGGFKQSGF GKDLGEAALN EYLRIKTVTF
EY