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Protein

GMP synthase [glutamine-hydrolyzing]

Gene

guaA

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the synthesis of GMP from XMP.1 Publication

Catalytic activityi

ATP + XMP + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate.1 Publication

Kineticsi

kcat is 2.3 sec(-1) for XMP. kcat is 2.39 sec(-1) for ATP. kcat is 3.05 sec(-1) for glutamine.

  1. KM=1.24 mM for glutamine1 Publication
  2. KM=27 µM for ATP1 Publication
  1. Vmax=2.49 µmol/min/mg enzyme toward XMP (at 40 degrees Celsius)1 Publication
  2. Vmax=2.58 µmol/min/mg enzyme toward ATP (at 40 degrees Celsius)1 Publication
  3. Vmax=3.30 µmol/min/mg enzyme toward glutamine (at 40 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 7.5.1 Publication

Temperature dependencei

Optimum temperature is 40 degrees Celsius.1 Publication

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] (guaA), GMP synthase [glutamine-hydrolyzing] (guaA)
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 sitei93 – 931NucleophileBy similarity
Active sitei179 – 1791By similarity
Active sitei181 – 1811By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi233 – 2397ATPBy similarity

GO - Molecular functioni

GO - Biological processi

  • glutamine metabolic process Source: UniProtKB-HAMAP
  • GMP biosynthetic process Source: GO_Central
  • growth Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

GMP biosynthesis, Purine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00189; UER00296.

Protein family/group databases

MEROPSiC26.A07.

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:guaA
Ordered Locus Names:Rv3396c
ORF Names:MTCY78.32
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv3396c.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: MTBBASE
  • cytosol Source: GO_Central
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 525524GMP synthase [glutamine-hydrolyzing]PRO_0000140149Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylvalineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP9WMS7.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi83332.Rv3396c.

Structurei

3D structure databases

ProteinModelPortaliP9WMS7.
SMRiP9WMS7. Positions 17-525.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 205190Glutamine amidotransferase type-1Add
BLAST
Domaini206 – 399194GMPS ATP-PPaseAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiENOG4105CM0. Bacteria.
COG0518. LUCA.
COG0519. LUCA.
KOiK01951.
OMAiMSHGDSV.
PhylomeDBiP9WMS7.

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.
IPR022310. NAD/GMP_synthase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00117. GATase. 1 hit.
PF00958. GMP_synt_C. 1 hit.
PF02540. NAD_synthase. 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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P9WMS7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVQPADIDVP ETPARPVLVV DFGAQYAQLI ARRVREARVF SEVIPHTASI
60 70 80 90 100
EEIRARQPVA LVLSGGPASV YADGAPKLDP ALLDLGVPVL GICYGFQAMA
110 120 130 140 150
QALGGIVAHT GTREYGRTEL KVLGGKLHSD LPEVQPVWMS HGDAVTAAPD
160 170 180 190 200
GFDVVASSAG APVAAFEAFD RRLAGVQYHP EVMHTPHGQQ VLSRFLHDFA
210 220 230 240 250
GLGAQWTPAN IANALIEQVR TQIGDGHAIC GLSGGVDSAV AAALVQRAIG
260 270 280 290 300
DRLTCVFVDH GLLRAGERAQ VQRDFVAATG ANLVTVDAAE TFLEALSGVS
310 320 330 340 350
APEGKRKIIG RQFIRAFEGA VRDVLDGKTA EFLVQGTLYP DVVESGGGSG
360 370 380 390 400
TANIKSHHNV GGLPDDLKFT LVEPLRLLFK DEVRAVGREL GLPEEIVARQ
410 420 430 440 450
PFPGPGLGIR IVGEVTAKRL DTLRHADSIV REELTAAGLD NQIWQCPVVL
460 470 480 490 500
LADVRSVGVQ GDGRTYGHPI VLRPVSSEDA MTADWTRVPY EVLERISTRI
510 520
TNEVAEVNRV VLDITSKPPA TIEWE
Length:525
Mass (Da):56,060
Last modified:April 16, 2014 - v1
Checksum:iDFBE06100BA16FAF
GO

Mass spectrometryi

Molecular mass is 55928 Da from positions 2 - 525. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP46218.1.
PIRiA70735.
RefSeqiNP_217913.1. NC_000962.3.
WP_003417952.1. NC_000962.3.

Genome annotation databases

EnsemblBacteriaiCCP46218; CCP46218; Rv3396c.
GeneIDi887412.
KEGGimtu:Rv3396c.
mtv:RVBD_3396c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP46218.1.
PIRiA70735.
RefSeqiNP_217913.1. NC_000962.3.
WP_003417952.1. NC_000962.3.

3D structure databases

ProteinModelPortaliP9WMS7.
SMRiP9WMS7. Positions 17-525.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv3396c.

Protein family/group databases

MEROPSiC26.A07.

Proteomic databases

PaxDbiP9WMS7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP46218; CCP46218; Rv3396c.
GeneIDi887412.
KEGGimtu:Rv3396c.
mtv:RVBD_3396c.

Organism-specific databases

TubercuListiRv3396c.

Phylogenomic databases

eggNOGiENOG4105CM0. Bacteria.
COG0518. LUCA.
COG0519. LUCA.
KOiK01951.
OMAiMSHGDSV.
PhylomeDBiP9WMS7.

Enzyme and pathway databases

UniPathwayiUPA00189; UER00296.

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.
IPR022310. NAD/GMP_synthase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00117. GATase. 1 hit.
PF00958. GMP_synt_C. 1 hit.
PF02540. NAD_synthase. 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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.
  3. "Biochemical characterization of recombinant guaA-encoded guanosine monophosphate synthetase (EC 6.3.5.2) from Mycobacterium tuberculosis H37Rv strain."
    Franco T.M., Rostirolla D.C., Ducati R.G., Lorenzini D.M., Basso L.A., Santos D.S.
    Arch. Biochem. Biophys. 517:1-11(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MASS SPECTROMETRY.
    Strain: ATCC 25618 / H37Rv.

Entry informationi

Entry nameiGUAA_MYCTU
AccessioniPrimary (citable) accession number: P9WMS7
Secondary accession number(s): L0TCE7, P0A5A1, Q50729
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: June 8, 2016
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.