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Protein

Trifunctional purine biosynthetic protein adenosine-3

Gene
N/A
Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

10-formyltetrahydrofolate + N(1)-(5-phospho-D-ribosyl)glycinamide = tetrahydrofolate + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide.UniRule annotation
ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole.UniRule annotation
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide.UniRule annotation

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Phosphoribosylformylglycinamidine synthase (PFAS)
  2. Trifunctional purine biosynthetic protein adenosine-3, Trifunctional purine biosynthetic protein adenosine-3 (GART), Trifunctional purine biosynthetic protein adenosine-3 (GART)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Amidophosphoribosyltransferase (PPAT), Amidophosphoribosyltransferase (PPAT)
  2. Trifunctional purine biosynthetic protein adenosine-3, Trifunctional purine biosynthetic protein adenosine-3 (GART), Trifunctional purine biosynthetic protein adenosine-3 (GART)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route).UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Trifunctional purine biosynthetic protein adenosine-3, Trifunctional purine biosynthetic protein adenosine-3 (GART), Trifunctional purine biosynthetic protein adenosine-3 (GART)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route), the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotation, TransferaseImported

Keywords - Biological processi

Purine biosynthesisUniRule annotation

Keywords - Ligandi

ATP-bindingUniRule annotation, ManganeseUniRule annotation, Metal-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00074; UER00125.
UPA00074; UER00126.
UPA00074; UER00129.

Names & Taxonomyi

Protein namesi
Recommended name:
Trifunctional purine biosynthetic protein adenosine-3UniRule annotation
Including the following 3 domains:
Phosphoribosylamine--glycine ligaseUniRule annotation (EC:6.3.4.13UniRule annotation)
Alternative name(s):
Glycinamide ribonucleotide synthetaseUniRule annotation
Short name:
GARSUniRule annotation
Phosphoribosylglycinamide synthetaseUniRule annotation
Phosphoribosylformylglycinamidine cyclo-ligaseUniRule annotation (EC:6.3.3.1UniRule annotation)
Alternative name(s):
AIR synthaseUniRule annotation
Short name:
AIRSUniRule annotation
Phosphoribosyl-aminoimidazole synthetaseUniRule annotation
Phosphoribosylglycinamide formyltransferaseUniRule annotation (EC:2.1.2.2UniRule annotation)
Alternative name(s):
5'-phosphoribosylglycinamide transformylaseUniRule annotation
GAR transformylaseUniRule annotation
Short name:
GARTUniRule annotation
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei12 – 30HelicalSequence analysisAdd BLAST19

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28576.

PTM / Processingi

Proteomic databases

PaxDbiQ59HH3.
PeptideAtlasiQ59HH3.
PRIDEiQ59HH3.

Expressioni

Gene expression databases

GenevisibleiQ59HH3. HS.

Interactioni

Protein-protein interaction databases

MINTiMINT-5004954.
STRINGi9606.ENSP00000371236.

Structurei

3D structure databases

ProteinModelPortaliQ59HH3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini147 – 354ATP-graspInterPro annotationAdd BLAST208

Sequence similaritiesi

In the C-terminal section; belongs to the GART family.UniRule annotation
In the N-terminal section; belongs to the GARS family.UniRule annotation
In the central section; belongs to the AIR synthase family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helixSequence analysis

Phylogenomic databases

eggNOGiKOG0237. Eukaryota.
KOG3076. Eukaryota.
COG0150. LUCA.
COG0151. LUCA.
COG0299. LUCA.
HOGENOMiHOG000030315.
HOVERGENiHBG008333.

Family and domain databases

CDDicd08645. FMT_core_GART. 1 hit.
cd02196. PurM. 1 hit.
Gene3Di3.30.1330.10. 1 hit.
3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.170. 1 hit.
3.40.50.20. 1 hit.
3.90.600.10. 1 hit.
3.90.650.10. 1 hit.
HAMAPiMF_00741. AIRS. 1 hit.
MF_00138. GARS. 1 hit.
MF_01930. PurN. 1 hit.
InterProiIPR010918. AIR_synth_C_dom.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR002376. Formyl_transf_N.
IPR001555. GART_AS.
IPR016185. PreATP-grasp_dom.
IPR020561. PRibGlycinamid_synth_ATP-grasp.
IPR000115. PRibGlycinamide_synth.
IPR020560. PRibGlycinamide_synth_C-dom.
IPR020559. PRibGlycinamide_synth_CS.
IPR020562. PRibGlycinamide_synth_N.
IPR016188. PurM-like_N.
IPR004733. PurM_cligase.
IPR004607. PurN.
IPR011054. Rudment_hybrid_motif.
[Graphical view]
PfamiPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
PF01071. GARS_A. 1 hit.
PF02843. GARS_C. 1 hit.
PF02844. GARS_N. 1 hit.
[Graphical view]
SMARTiSM01210. GARS_C. 1 hit.
[Graphical view]
SUPFAMiSSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
SSF53328. SSF53328. 1 hit.
SSF56042. SSF56042. 1 hit.
TIGRFAMsiTIGR00877. purD. 1 hit.
TIGR00878. purM. 1 hit.
TIGR00639. PurN. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS00184. GARS. 1 hit.
PS00373. GART. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q59HH3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
RRRGRRARRA TRCLTHGFQA LSGFIFLWNF CFTDRTMAAR VLIIGSGGRE
60 70 80 90 100
HTLAWKLAQS HHVKQVLVAP GNAGTACSEK ISNTAISISD HTALAQFCKE
110 120 130 140 150
KKIEFVVVGP EAPLAAGIVG NLRSAGVQCF GPTAEAAQLE SSKRFAKEFM
160 170 180 190 200
DRHGIPTAQW KAFTKPEEAC SFILSADFPA LVVKASGLAA GKGVIVAKSK
210 220 230 240 250
EEACKAVQEI MQEKAFGAAG ETIVIEELLD GEEVSCLCFT DGKTVAPMPP
260 270 280 290 300
AQDHKRLLEG DGGPNTGGMG AYCPAPQVSN DLLLKIKDTV LQRTVDGMQQ
310 320 330 340 350
EGTPYTGILY AGIMLTKNGP KVLEFNCRFG DPECQVILPL LKSDLYEVIQ
360 370 380 390 400
STLDGLLCTS LPVWLENHTA LTVVMASKGY PGDYTKGVEI TGFPEAQALG
410 420 430 440 450
LEVFHAGTAL KNGKVVTHGG RVLAVTAIRE NLISALEEAK KGLAAIKFEG
460 470 480 490 500
AIYRKDIGFR AIAFLQQPRS LTYKESGVDI AAGNMLVKKI QPLAKATSRS
510 520 530 540 550
GCKVDLGGFA GLFDLKAAGF KDPLLASGTD GVGTKLKIAQ LCNKHDTIGQ
560 570 580 590 600
DLVAMCVNDI LAQGAEPLFF LDYFSCGKLD LSVTEAVVAG IAKACGKAGC
610 620 630 640 650
ALLGGETAEM PDMYPPGEYD LAGFAVGAME RDQKLPHLER ITEGDVVVGI
660 670 680 690 700
ASSGLHSNGF SLVRKIVAKS SLQYSSPAPD GCGDQTLGDL LLTPTRIYSH
710 720 730 740 750
SLLPVLRSGH VKAFAHITGG GLLENIPRVL PEKLGVDLDA QTWRIPRVFS
760 770 780 790 800
WLQQEGHLSE EEMARTFNCG VGAVLVVSKE QTEQILRDIQ QHKEEAWVIG
810 820 830 840 850
SVVARAEGSP RVKVKNLIES MQINGSVLKN GSLTNHFSFE KKKARVAVLI
860 870 880 890 900
SGTGSNLQAL IDSTREPNSS AQIDIVISNK AAVAGLDKAE RAGIPTRVIN
910 920 930 940 950
HKLYKNRVEF DSAIDLVLEE FSIDIVCLAG FMRILSGPFV QKWNGKMLNI
960 970 980 990 1000
HPSLLPSFKG SNAHEQALET GVTVTGCTVH FVAEDVDAGQ IILQEAVPVK
1010 1020 1030 1040
RGDTVATLSE RVKLAEHKIF PAALQLVASG TVQLGENGKI CWVKEE
Length:1,046
Mass (Da):112,138
Last modified:April 26, 2005 - v1
Checksum:iDF03CB4B83AE9EEA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei1Imported1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB208785 mRNA. Translation: BAD92022.1.
RefSeqiNP_001129478.1. NM_001136006.1.
UniGeneiHs.473648.

Genome annotation databases

GeneIDi2618.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB208785 mRNA. Translation: BAD92022.1.
RefSeqiNP_001129478.1. NM_001136006.1.
UniGeneiHs.473648.

3D structure databases

ProteinModelPortaliQ59HH3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-5004954.
STRINGi9606.ENSP00000371236.

Proteomic databases

PaxDbiQ59HH3.
PeptideAtlasiQ59HH3.
PRIDEiQ59HH3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2618.

Organism-specific databases

CTDi2618.
PharmGKBiPA28576.

Phylogenomic databases

eggNOGiKOG0237. Eukaryota.
KOG3076. Eukaryota.
COG0150. LUCA.
COG0151. LUCA.
COG0299. LUCA.
HOGENOMiHOG000030315.
HOVERGENiHBG008333.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00125.
UPA00074; UER00126.
UPA00074; UER00129.

Miscellaneous databases

GenomeRNAii2618.

Gene expression databases

GenevisibleiQ59HH3. HS.

Family and domain databases

CDDicd08645. FMT_core_GART. 1 hit.
cd02196. PurM. 1 hit.
Gene3Di3.30.1330.10. 1 hit.
3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.170. 1 hit.
3.40.50.20. 1 hit.
3.90.600.10. 1 hit.
3.90.650.10. 1 hit.
HAMAPiMF_00741. AIRS. 1 hit.
MF_00138. GARS. 1 hit.
MF_01930. PurN. 1 hit.
InterProiIPR010918. AIR_synth_C_dom.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR002376. Formyl_transf_N.
IPR001555. GART_AS.
IPR016185. PreATP-grasp_dom.
IPR020561. PRibGlycinamid_synth_ATP-grasp.
IPR000115. PRibGlycinamide_synth.
IPR020560. PRibGlycinamide_synth_C-dom.
IPR020559. PRibGlycinamide_synth_CS.
IPR020562. PRibGlycinamide_synth_N.
IPR016188. PurM-like_N.
IPR004733. PurM_cligase.
IPR004607. PurN.
IPR011054. Rudment_hybrid_motif.
[Graphical view]
PfamiPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
PF01071. GARS_A. 1 hit.
PF02843. GARS_C. 1 hit.
PF02844. GARS_N. 1 hit.
[Graphical view]
SMARTiSM01210. GARS_C. 1 hit.
[Graphical view]
SUPFAMiSSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
SSF53328. SSF53328. 1 hit.
SSF56042. SSF56042. 1 hit.
TIGRFAMsiTIGR00877. purD. 1 hit.
TIGR00878. purM. 1 hit.
TIGR00639. PurN. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS00184. GARS. 1 hit.
PS00373. GART. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiQ59HH3_HUMAN
AccessioniPrimary (citable) accession number: Q59HH3
Entry historyi
Integrated into UniProtKB/TrEMBL: April 26, 2005
Last sequence update: April 26, 2005
Last modified: October 5, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Multifunctional enzymeUniRule annotation

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.