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

Phosphoribosylformylglycinamidine synthase

Gene

purL

Organism
Actinobacillus pleuropneumoniae serotype 7 (strain AP76)
Status
Unreviewed-Annotation score: -Protein inferred from homologyi

Functioni

Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate.UniRule annotationSAAS annotation

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.UniRule annotation

Catalytic activityi

ATP + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O = ADP + phosphate + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine + L-glutamate.UniRule annotationSAAS annotation

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 1 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 annotationSAAS annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Phosphoribosylformylglycinamidine synthase (purL)
  2. Phosphoribosylformylglycinamidine cyclo-ligase (purM)
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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei679ATP; via carbonyl oxygenUniRule annotation1
Metal bindingi680MagnesiumUniRule annotation1
Metal bindingi719MagnesiumUniRule annotation1
Metal bindingi723MagnesiumUniRule annotation1
Metal bindingi887MagnesiumUniRule annotation1
Binding sitei889ATPUniRule annotation1
Active sitei1138NucleophileUniRule annotation1
Active sitei1263UniRule annotation1
Active sitei1265UniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi308 – 319ATPUniRule annotationAdd BLAST12

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigaseUniRule annotationSAAS annotationImported
Biological processPurine biosynthesisUniRule annotationSAAS annotation
LigandATP-bindingUniRule annotationSAAS annotation, MagnesiumUniRule annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00074; UER00128

Protein family/group databases

MEROPSiC56.972

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoribosylformylglycinamidine synthaseUniRule annotation (EC:6.3.5.3UniRule annotation)
Short name:
FGAM synthaseUniRule annotation
Short name:
FGAMSUniRule annotation
Alternative name(s):
Formylglycinamide ribonucleotide amidotransferaseUniRule annotation
Short name:
FGAR amidotransferaseUniRule annotation
Short name:
FGAR-ATUniRule annotation
Gene namesi
Name:purLUniRule annotationImported
Ordered Locus Names:APP7_1743Imported
OrganismiActinobacillus pleuropneumoniae serotype 7 (strain AP76)Imported
Taxonomic identifieri537457 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeActinobacillus
Proteomesi
  • UP000001226 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

CytoplasmUniRule annotation

Interactioni

Subunit structurei

Monomer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB3H2S8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1045 – 1298Glutamine amidotransferase type-1InterPro annotationAdd BLAST254

Sequence similaritiesi

In the N-terminal section; belongs to the FGAMS family.UniRule annotationSAAS annotation

Keywords - Domaini

Glutamine amidotransferaseUniRule annotationSAAS annotation

Phylogenomic databases

HOGENOMiHOG000261359
KOiK01952
OMAiSLSANWM
OrthoDBiPOG091H021O

Family and domain databases

Gene3Di3.30.1330.10, 2 hits
3.40.50.880, 1 hit
3.90.650.10, 2 hits
HAMAPiMF_00419 PurL_1, 1 hit
InterProiView protein in InterPro
IPR029062 Class_I_gatase-like
IPR017926 GATASE
IPR010073 PRibForGlyAmidine_synth
IPR010918 PurM-like_C_dom
IPR036676 PurM-like_C_sf
IPR036921 PurM-like_N_sf
IPR036604 PurS-like_sf
PANTHERiPTHR10099:SF5 PTHR10099:SF5, 1 hit
PfamiView protein in Pfam
PF02769 AIRS_C, 2 hits
SUPFAMiSSF52317 SSF52317, 1 hit
SSF55326 SSF55326, 2 hits
SSF56042 SSF56042, 2 hits
SSF82697 SSF82697, 1 hit
TIGRFAMsiTIGR01735 FGAM_synt, 1 hit
PROSITEiView protein in PROSITE
PS51273 GATASE_TYPE_1, 1 hit

Sequencei

Sequence statusi: Complete.

B3H2S8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVQTFRGSP ALSEFRLNQF QTKFQQNALP VKSVYAEYVH FVDLNAELSA
60 70 80 90 100
AQTAEIKELL HYGPTLAEHE PVGFCLIVTP RIGTISSWSS KATDIAHNCG
110 120 130 140 150
LQAVNRIERG LAYYFEFSAE PTAAQIETLK GLLHDRMLET VLDNEAQAAN
160 170 180 190 200
LFAQQEPKPF TTVDILNGGR KALEEANVNL GLALADDEID YLVENFTALK
210 220 230 240 250
RNPNDIELYM FAQANSEHCR HKIFNADWTI DGQKQEKSLF KMIKNTFEKT
260 270 280 290 300
PDYVLSAYKD NAAVMEGSKV GRWFPDQDGQ YRAHQEDAHI LMKVETHNHP
310 320 330 340 350
TAISPFPGAA TGSGGEIRDE GATGRGAKPK AGLTGFSVSN LVIPNFEQPW
360 370 380 390 400
ENPLSKPHRI ASALDIMIEG PLGGAAFNNE FGRPALLGYF RTYEEKVNSF
410 420 430 440 450
AGEEVRGYHK PIMLAGGIGN IRAEHVQKGE IPVGAKLIVL GGPAMNIGLG
460 470 480 490 500
GGAASSMASG KSKEDLDFAS VQRENPEMER RCQEVIDRCW QLGEDNPILF
510 520 530 540 550
IHDVGAGGLS NAMPELVHDG DRGGKFDLRK ILCDEKGMSP LEIWCNESQE
560 570 580 590 600
RYVLAVSPEK LALFTELCER ERAPFAVIGE ATEEKHLTLK DDHFDNNPID
610 620 630 640 650
LPMNVLLGKT PKMHRDVSSK TVENQPLDSQ QIQLKEALHR VLRLPVVAEK
660 670 680 690 700
TFLITIGDRT VTGMVARDQM VGPWQIPVAD CAVTTASLDS YHGEAMSMGE
710 720 730 740 750
RAPVALLDFG ASARLAVAES ITNIAATNIG ELKRIKLSAN WMSAAGHEGE
760 770 780 790 800
DAGLYEAVKA VGEELCPALG ITIPVGKDSM SMRTTWEENG EQKSVTAPLS
810 820 830 840 850
LVISAFARVE DVRKTVTPQL RTDKGLSSLL LLDLGEGKNR LGATALAQVY
860 870 880 890 900
KQLGDKPADV VNVESLKNFF NAMQTLVAED KLLAYHDRSD GGLITTLAEM
910 920 930 940 950
TFAGNCGVEI DISALGDDDL AVLFNEELGA VIQVKDADLA RVREVLNAHN
960 970 980 990 1000
LLGLTKDLGT VHEDDRFVIS RGSLKLLNEK RSELRGIWAE LTHQMQRLRD
1010 1020 1030 1040 1050
NPECADQEFE TKKDPNNKGL STFLTYDVNE DITAPFINKG VKPTIAILRE
1060 1070 1080 1090 1100
QGVNSHYEMA AAFDRAGFNA IDVHMSDLMA GRRNLKDFNA LVACGGFSYG
1110 1120 1130 1140 1150
DVLGAGGGWA KSILFNPMLR EQFSQFFANP NTLALGVCNG CQMVSNLAEI
1160 1170 1180 1190 1200
IPGTENWPHF VRNKSERFEA RVGLVKINET NSHWFQGMAG SHMPIAVSHG
1210 1220 1230 1240 1250
EGQVEFKSAQ QLADLTAQKL VIAQYIDNNL QPTEVYPANP NGSVNGITAI
1260 1270 1280 1290
SNSDGRVAIM MPHPERVYRA VSNSWHPEDW TEDGAWMRLF RNARVVLG
Length:1,298
Mass (Da):142,534
Last modified:July 22, 2008 - v1
Checksum:iC52E931B0B9C035A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001091 Genomic DNA Translation: ACE62395.1
RefSeqiWP_005618154.1, NC_010939.1

Genome annotation databases

EnsemblBacteriaiACE62395; ACE62395; APP7_1743
KEGGiapa:APP7_1743

Similar proteinsi

Entry informationi

Entry nameiB3H2S8_ACTP7
AccessioniPrimary (citable) accession number: B3H2S8
Entry historyiIntegrated into UniProtKB/TrEMBL: July 22, 2008
Last sequence update: July 22, 2008
Last modified: June 20, 2018
This is version 79 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health