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A1WNW9

- A1WNW9_VEREI

UniProt

A1WNW9 - A1WNW9_VEREI

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Protein

Phosphoribosylformylglycinamidine synthase

Gene

purL

Organism
Verminephrobacter eiseniae (strain EF01-2)
Status
Unreviewed - Annotation score: 3 out of 5- 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 annotation

Catalytic activityi

ATP + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O = ADP + phosphate + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate.UniRule annotationSAAS annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei684 – 6841ATP; via carbonyl oxygenUniRule annotation
Metal bindingi685 – 6851MagnesiumUniRule annotation
Metal bindingi724 – 7241MagnesiumUniRule annotation
Metal bindingi728 – 7281MagnesiumUniRule annotation
Metal bindingi895 – 8951MagnesiumUniRule annotation
Binding sitei897 – 8971ATPUniRule annotation
Active sitei1177 – 11771NucleophileUniRule annotation
Active sitei1298 – 12981UniRule annotation
Active sitei1300 – 13001UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi317 – 32812ATPUniRule annotationAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. metal ion binding Source: UniProtKB-KW
  3. phosphoribosylformylglycinamidine synthase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
  2. glutamine metabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotationSAAS annotation

Keywords - Biological processi

Purine biosynthesisUniRule annotationSAAS annotation

Keywords - Ligandi

ATP-bindingUniRule annotationSAAS annotation, MagnesiumUniRule annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation, Nucleotide-binding

Enzyme and pathway databases

BioCyciVEIS391735:GHY5-3653-MONOMER.
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
Gene namesi
Name:purLUniRule annotation
Ordered Locus Names:Veis_3609Imported
OrganismiVerminephrobacter eiseniae (strain EF01-2)Imported
Taxonomic identifieri391735 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeVerminephrobacter
ProteomesiUP000000374: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi391735.Veis_3609.

Structurei

3D structure databases

ProteinModelPortaliA1WNW9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1084 – 1316233Glutamine amidotransferase type-1UniRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 glutamine amidotransferase type-1 domain.UniRule annotation
Contains glutamine amidotransferase type-1 domain.SAAS annotation
In the N-terminal section; belongs to the FGAMS family.UniRule annotation

Keywords - Domaini

Glutamine amidotransferaseUniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiCOG0046.
HOGENOMiHOG000261359.
KOiK01952.
OMAiMSPREIW.
OrthoDBiEOG6FNHHR.

Family and domain databases

Gene3Di3.30.1330.10. 2 hits.
3.40.50.880. 1 hit.
3.90.650.10. 1 hit.
InterProiIPR010918. AIR_synth_C_dom.
IPR000728. AIR_synth_N_dom.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR010073. PRibForGlyAmidine_synth.
IPR016188. PurM_N-like.
[Graphical view]
PfamiPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 2 hits.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
SSF55326. SSF55326. 2 hits.
SSF56042. SSF56042. 3 hits.
TIGRFAMsiTIGR01735. FGAM_synt. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A1WNW9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTTLAGGNAL SPFRARQLQS ALADIHPGIT GIAARFVHLV LTDTAPAPAQ
60 70 80 90 100
QQRLAALLRY GDPYAGPVDG CAIIVTPRLG TLSPWASKAT DIARNCGLAV
110 120 130 140 150
RHLERSTEYR IRLRAGRLTD AERDRIAALL HDRMTESVLF DPAGLAALFT
160 170 180 190 200
ALPPARMEHV DVLGAGLAAL AAANTRLGLA LADQEMEYLV SAFTGLARNP
210 220 230 240 250
TEVELMMFAQ ANSEHCRHKI FNARFAIDGV AQEPSLFDMI RHTHQRAPGH
260 270 280 290 300
TLVAYSDNAA VMQGHLVEQF AAKMTDGADP SCAHTYAYSY QKSSSTEHLL
310 320 330 340 350
MKVETHNHPT AISPWPGAAT GAGGEIRDEG ATGRGARPRA GLTGFSVSRL
360 370 380 390 400
WGSQIGRPGH IASALQIMLE GPLGAAAFNN EFGRPNLAGY FREYEQRVGC
410 420 430 440 450
GADAVVRGYH KPIMLAGGLG VIDAALVRKI AFPAGTLLVQ LGGPGMRIGM
460 470 480 490 500
GGGAASSMAT GSNAAGLDFD SVQRGNPEIQ RRAQEVINHC AAQGAANPIL
510 520 530 540 550
AIHDVGAGGL SNALPELIHD AGRGARLDLR AVPLEDSGMS AMEIWSNESQ
560 570 580 590 600
ERYVLAIAPE SLAQLRSFCE RERCPLAVLG SATEERQLVL HDSAATAADQ
610 620 630 640 650
QLPVNLPMGV LLGQPPRMQR NASSLRRRFV PLDLSGLPLH KAVTDVLAHP
660 670 680 690 700
TVASKRFLVS IGDRTVGGLV HRDQMVGPWQ VPVADCAITL ADYQGFAGAA
710 720 730 740 750
MAIGERTPLA ALDAPASGRM AVAEAITNLL AAPIELARVK LSANWMAACG
760 770 780 790 800
EPGEDAALYA TVEAVGLELC PALGLAIPVG KDSLSMRTQW REGAGQTTVS
810 820 830 840 850
SPVSLIVSAF AALTDVRGSL TPQLDATEAE TTLVLIDLGR GRNRMGASIL
860 870 880 890 900
GQTLEQSGCP EKDGVPDLDA PQDLLALVDA VNALRAQGRL LAYHDRSDGG
910 920 930 940 950
LLATVAEMAF AGQVGVALNV DLLVTEGDGI GDSRMDTGDA KNWAGQVHAR
960 970 980 990 1000
REERTLEALF SEELGVVLQV RTAERNEVMQ TLRAHGLARW SHFIGSTRPA
1010 1020 1030 1040 1050
GPRVLQVWRD AQPVFSAPLA DLQRAWDTVS WKICRQRDNP DSADAEHAAA
1060 1070 1080 1090 1100
GDPTDPGLHL HLQPTFDAPE PPAAPGLRLA RPRVAILREQ GVNSHVEMAY
1110 1120 1130 1140 1150
AFTEAGFAAC DVHMTDLQTG RVRLADFKGL VACGGFSYGD TLGAGIGWAR
1160 1170 1180 1190 1200
SISFNPALAA QFQGFFARGD TFGLGVCNGC QMFAELADII PGAQYWPRFT
1210 1220 1230 1240 1250
TNQSQRFESR LSLVQVTESP SLFLQGMAGS RLPVPVAHGE GYADFRQRGD
1260 1270 1280 1290 1300
AAQAIAALRF VDNHGAVTER YPFNPNGSPG GLTGVTTADG RFTALMPHPE
1310 1320 1330
RVFRNIQMSW TPGERSALSP WMRLWRNARR WVG
Length:1,333
Mass (Da):142,090
Last modified:February 6, 2007 - v1
Checksum:iB763C28198478E9C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000542 Genomic DNA. Translation: ABM59326.1.
RefSeqiWP_011811317.1. NC_008786.1.
YP_998344.1. NC_008786.1.

Genome annotation databases

EnsemblBacteriaiABM59326; ABM59326; Veis_3609.
GeneIDi4692772.
KEGGivei:Veis_3609.
PATRICi24021031. VBIVerEis120356_3893.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000542 Genomic DNA. Translation: ABM59326.1 .
RefSeqi WP_011811317.1. NC_008786.1.
YP_998344.1. NC_008786.1.

3D structure databases

ProteinModelPortali A1WNW9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 391735.Veis_3609.

Protein family/group databases

MEROPSi C56.972.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABM59326 ; ABM59326 ; Veis_3609 .
GeneIDi 4692772.
KEGGi vei:Veis_3609.
PATRICi 24021031. VBIVerEis120356_3893.

Phylogenomic databases

eggNOGi COG0046.
HOGENOMi HOG000261359.
KOi K01952.
OMAi MSPREIW.
OrthoDBi EOG6FNHHR.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00128 .
BioCyci VEIS391735:GHY5-3653-MONOMER.

Family and domain databases

Gene3Di 3.30.1330.10. 2 hits.
3.40.50.880. 1 hit.
3.90.650.10. 1 hit.
InterProi IPR010918. AIR_synth_C_dom.
IPR000728. AIR_synth_N_dom.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR010073. PRibForGlyAmidine_synth.
IPR016188. PurM_N-like.
[Graphical view ]
Pfami PF00586. AIRS. 1 hit.
PF02769. AIRS_C. 2 hits.
[Graphical view ]
SUPFAMi SSF52317. SSF52317. 1 hit.
SSF55326. SSF55326. 2 hits.
SSF56042. SSF56042. 3 hits.
TIGRFAMsi TIGR01735. FGAM_synt. 1 hit.
PROSITEi PS51273. GATASE_TYPE_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.
    , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
    Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: EF01-2Imported.

Entry informationi

Entry nameiA1WNW9_VEREI
AccessioniPrimary (citable) accession number: A1WNW9
Entry historyi
Integrated into UniProtKB/TrEMBL: February 6, 2007
Last sequence update: February 6, 2007
Last modified: October 29, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Miscellaneous

In Gram-negative bacteria and most eukaryotes, FGAM synthase is only formed by PurL, a single polypeptide of 140 kDa (large PurL). However in Gram-positive bacteria and archaebacteria, phosphoribosylformylglycinamidine synthase is composed of three separate proteins: PurL (small PurL), PurQ and PurS.UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3