Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Trifunctional purine biosynthetic protein adenosine-3

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

Functioni

Catalytic activityi

10-formyltetrahydrofolate + N1-(5-phospho-D-ribosyl)glycinamide = tetrahydrofolate + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide.UniRule annotation
ATP + 2-(formamido)-N1-(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 + N1-(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

Keywordsi

Molecular functionLigaseUniRule annotation, Multifunctional enzymeUniRule annotation, TransferaseImported
Biological processPurine biosynthesisUniRule annotation
LigandATP-bindingPROSITE-ProRule 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

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28576

PTM / Processingi

Proteomic databases

PeptideAtlasiQ59HH3
PRIDEiQ59HH3

Expressioni

Gene expression databases

GenevisibleiQ59HH3 HS

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
3.90.600.10, 1 hit
3.90.650.10, 1 hit
HAMAPiMF_00741 AIRS, 1 hit
MF_00138 GARS, 1 hit
MF_01930 PurN, 1 hit
InterProiView protein in InterPro
IPR011761 ATP-grasp
IPR013815 ATP_grasp_subdomain_1
IPR002376 Formyl_transf_N
IPR036477 Formyl_transf_N_sf
IPR004607 GART
IPR001555 GART_AS
IPR016185 PreATP-grasp_dom_sf
IPR020561 PRibGlycinamid_synth_ATP-grasp
IPR000115 PRibGlycinamide_synth
IPR020560 PRibGlycinamide_synth_C-dom
IPR037123 PRibGlycinamide_synth_C_sf
IPR020559 PRibGlycinamide_synth_CS
IPR020562 PRibGlycinamide_synth_N
IPR010918 PurM-like_C_dom
IPR036676 PurM-like_C_sf
IPR016188 PurM-like_N
IPR036921 PurM-like_N_sf
IPR004733 PurM_cligase
IPR011054 Rudment_hybrid_motif
PANTHERiPTHR10520 PTHR10520, 1 hit
PfamiView protein in Pfam
PF00586 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
SMARTiView protein in SMART
SM01210 GARS_C, 1 hit
SUPFAMiSSF51246 SSF51246, 1 hit
SSF52440 SSF52440, 1 hit
SSF53328 SSF53328, 1 hit
SSF55326 SSF55326, 1 hit
SSF56042 SSF56042, 1 hit
TIGRFAMsiTIGR00877 purD, 1 hit
TIGR00878 purM, 1 hit
TIGR00639 PurN, 1 hit
PROSITEiView protein in PROSITE
PS50975 ATP_GRASP, 1 hit
PS00184 GARS, 1 hit
PS00373 GART, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiQ59HH3_HUMAN
AccessioniPrimary (citable) accession number: Q59HH3
Entry historyiIntegrated into UniProtKB/TrEMBL: April 26, 2005
Last sequence update: April 26, 2005
Last modified: March 28, 2018
This is version 105 of the entry and version 1 of the sequence. See 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.

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health