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Protein

GMP synthase [glutamine-hydrolyzing]

Gene

gua1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

ATP + XMP + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate.

Pathwayi: GMP biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes GMP from XMP (L-Gln route).
Proteins known to be involved in this subpathway in this organism are:
  1. GMP synthase [glutamine-hydrolyzing] (gua1)
This subpathway is part of the pathway GMP biosynthesis, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes GMP from XMP (L-Gln route), the pathway GMP biosynthesis and in Purine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei96 – 961For GATase activityBy similarity
Active sitei189 – 1891For GATase activityBy similarity
Active sitei191 – 1911For GATase activityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi244 – 2507ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

GMP biosynthesis, Purine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-73817. Purine ribonucleoside monophosphate biosynthesis.
UniPathwayiUPA00189; UER00296.

Protein family/group databases

MEROPSiC26.957.

Names & Taxonomyi

Protein namesi
Recommended name:
GMP synthase [glutamine-hydrolyzing] (EC:6.3.5.2)
Alternative name(s):
GMP synthetase
Glutamine amidotransferase
Gene namesi
Name:gua1
ORF Names:SPAP7G5.02c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAP7G5.02c.
PomBaseiSPAP7G5.02c.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 539539GMP synthase [glutamine-hydrolyzing]PRO_0000286154Add
BLAST

Proteomic databases

MaxQBiQ9P772.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

MINTiMINT-4704784.

Structurei

3D structure databases

ProteinModelPortaliQ9P772.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 215196Glutamine amidotransferase type-1Add
BLAST
Domaini216 – 413198GMPS ATP-PPaseAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

HOGENOMiHOG000223964.
InParanoidiQ9P772.
KOiK01951.
OMAiMSHGDSV.
OrthoDBiEOG7J70QG.
PhylomeDBiQ9P772.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.40.50.880. 1 hit.
HAMAPiMF_00344. GMP_synthase.
InterProiIPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR001674. GMP_synth_C.
IPR004739. GMP_synth_N.
IPR022955. GMP_synthase.
IPR025777. GMPS_ATP_PPase_dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00117. GATase. 1 hit.
PF00958. GMP_synt_C. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR00884. guaA_Cterm. 1 hit.
TIGR00888. guaA_Nterm. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
PS51553. GMPS_ATP_PPASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9P772-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSTEVPGEV STSVSSYFDT ILILDFGSQY SHLIARRLRE IHVYAELLPC
60 70 80 90 100
TQKIEALPFK PIGVILSGGP YSVYDDIAPH VDPAVFELGV PVLGICYGMQ
110 120 130 140 150
EIAWLNGRCV EPGIEREYGP ATVSMEPEIK TEVFKSFFNS MPKEFEVWMS
160 170 180 190 200
HGDRLSALPN GYETIGRTKN SPFAVIAHVT KPIIGLQFHP EVTHTPLGLQ
210 220 230 240 250
LIKNFAIEIC HAKPNWSMEN FVDKEILRIR KMIGPSDHVI GAVSGGVDST
260 270 280 290 300
VASKVLKEAI GDRFHAIMVD NGLLRLNEAE IVRETLNKHL GIQLTVVDAS
310 320 330 340 350
EEFIGKLKGV TDPEKKRKII GNTFIHVFER EAERIVKETN GKVEYLLQGT
360 370 380 390 400
LYPDVIESIS FKGPSQTIKT HHNVGGLLKD MKLKLIEPLR ELFKDEVRAL
410 420 430 440 450
GELLGIEHSL VWRHPFPGPG LGIRILGEVN AAQLEIARKA DHIFITEIRN
460 470 480 490 500
HGYYDKISQA FAALLPVKAV GVMGDKRTHE QVIALRAITT SDFMTADWYD
510 520 530
GFSIKFLKLV SSRICNEVSG VNRVLYDISS KPPATVEME
Length:539
Mass (Da):60,044
Last modified:October 1, 2000 - v1
Checksum:iF83A1C4575F71723
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB88269.1.
RefSeqiNP_594312.1. NM_001019735.2.

Genome annotation databases

EnsemblFungiiSPAP7G5.02c.1; SPAP7G5.02c.1:pep; SPAP7G5.02c.
GeneIDi2542573.
KEGGispo:SPAP7G5.02c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB88269.1.
RefSeqiNP_594312.1. NM_001019735.2.

3D structure databases

ProteinModelPortaliQ9P772.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4704784.

Protein family/group databases

MEROPSiC26.957.

Proteomic databases

MaxQBiQ9P772.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAP7G5.02c.1; SPAP7G5.02c.1:pep; SPAP7G5.02c.
GeneIDi2542573.
KEGGispo:SPAP7G5.02c.

Organism-specific databases

EuPathDBiFungiDB:SPAP7G5.02c.
PomBaseiSPAP7G5.02c.

Phylogenomic databases

HOGENOMiHOG000223964.
InParanoidiQ9P772.
KOiK01951.
OMAiMSHGDSV.
OrthoDBiEOG7J70QG.
PhylomeDBiQ9P772.

Enzyme and pathway databases

UniPathwayiUPA00189; UER00296.
ReactomeiR-SPO-73817. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

PROiQ9P772.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.40.50.880. 1 hit.
HAMAPiMF_00344. GMP_synthase.
InterProiIPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR001674. GMP_synth_C.
IPR004739. GMP_synth_N.
IPR022955. GMP_synthase.
IPR025777. GMPS_ATP_PPase_dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00117. GATase. 1 hit.
PF00958. GMP_synt_C. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR00884. guaA_Cterm. 1 hit.
TIGR00888. guaA_Nterm. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
PS51553. GMPS_ATP_PPASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiGUAA_SCHPO
AccessioniPrimary (citable) accession number: Q9P772
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

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.