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Protein

Putative asparagine synthetase [glutamine-hydrolyzing]

Gene

asnB

Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate.

Pathwayi: L-asparagine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-asparagine from L-aspartate (L-Gln route).
Proteins known to be involved in this subpathway in this organism are:
  1. Putative asparagine synthetase [glutamine-hydrolyzing] (asnB)
This subpathway is part of the pathway L-asparagine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-asparagine from L-aspartate (L-Gln route), the pathway L-asparagine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei2For GATase activityBy similarity1
Binding sitei115GlutamineBy similarity1
Sitei384Important for beta-aspartyl-AMP intermediate formationBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi382 – 383ATPBy similarity2

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase
Biological processAmino-acid biosynthesis, Asparagine biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00134; UER00195.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative asparagine synthetase [glutamine-hydrolyzing] (EC:6.3.5.4)
Gene namesi
Name:asnB
Ordered Locus Names:BQ2027_MB2224
OrganismiMycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Taxonomic identifieri233413 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001419 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000569362 – 652Putative asparagine synthetase [glutamine-hydrolyzing]Add BLAST651

Expressioni

Inductioni

Induced in response to the thiol oxidant diamide.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP64248.
SMRiP64248.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 231Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd BLAST230

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni60 – 64Glutamine bindingBy similarity5
Regioni89 – 91Glutamine bindingBy similarity3

Sequence similaritiesi

Belongs to the asparagine synthetase family.Curated

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

HOGENOMiHOG000027495.
KOiK01953.
OMAiIEHSHQP.

Family and domain databases

CDDicd01991. Asn_Synthase_B_C. 1 hit.
cd00712. AsnB. 1 hit.
Gene3Di3.40.50.620. 1 hit.
3.60.20.10. 1 hit.
InterProiView protein in InterPro
IPR006426. Asn_synth_AEB.
IPR001962. Asn_synthase.
IPR033738. AsnB_N.
IPR017932. GATase_2_dom.
IPR029055. Ntn_hydrolases_N.
IPR014729. Rossmann-like_a/b/a_fold.
PfamiView protein in Pfam
PF00733. Asn_synthase. 1 hit.
PF13537. GATase_7. 1 hit.
PIRSFiPIRSF001589. Asn_synthetase_glu-h. 1 hit.
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR01536. asn_synth_AEB. 1 hit.
PROSITEiView protein in PROSITE
PS51278. GATASE_TYPE_2. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P64248-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCGLLAFVAA PAGAAGPEGA DAASAIARAS HLMRHRGPDE SGTWHAVDGA
60 70 80 90 100
SGGVVFGFNR LSIIDIAHSH QPLRWGPPEA PDRYVLVFNG EIYNYLELRD
110 120 130 140 150
ELRTQHGAVF ATDGDGEAIL AGYHHWGTEV LQRLRGMFAF ALWDTVTREL
160 170 180 190 200
FCARDPFGIK PLFIATGAGG TAVASEKKCL LDLVELVGFD TEIDHRALQH
210 220 230 240 250
YTVLQYVPEP ETLHRGVRRL ESGCFARIRA DQLAPVITRY FVPRFAASPI
260 270 280 290 300
TNDNDQARYD EITAVLEDSV AKHMRADVTV GAFLSGGIDS TAIAALAIRH
310 320 330 340 350
NPRLITFTTG FEREGFSEID VAVASAEAIG ARHIAKVVSA DEFVAALPEI
360 370 380 390 400
VWYLDEPVAD PALVPLFFVA REARKHVKVV LSGEGADELF GGYTIYREPL
410 420 430 440 450
SLRPFDYLPK PLRRSMGKVS KPLPEGMRGK SLLHRGSLTL EERYYGNARS
460 470 480 490 500
FSGAQLREVL PGFRPDWTHT DVTAPVYAES AGWDPVARMQ HIDLFTWLRG
510 520 530 540 550
DILVKADKIT MANSLELRVP FLDPEVFAVA SRLPAGAKIT RTTTKYALRR
560 570 580 590 600
ALEPIVPAHV LHRPKLGFPV PIRHWLRAGE LLEWAYATVG SSQAGHLVDI
610 620 630 640 650
AAVYRMLDEH RCGSSDHSRR LWTMLIFMLW HAIFVEHSVV PQISEPQYPV

QL
Length:652
Mass (Da):72,150
Last modified:October 11, 2004 - v1
Checksum:iC4624495A845F790
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
LT708304 Genomic DNA. Translation: SIU00832.1.
RefSeqiNP_855873.1. NC_002945.3.
WP_003411413.1. NC_002945.4.

Genome annotation databases

EnsemblBacteriaiCDO43478; CDO43478; Mb2224.
KEGGimbo:Mb2224.
PATRICifig|233413.5.peg.2440.

Similar proteinsi

Entry informationi

Entry nameiASNH_MYCBO
AccessioniPrimary (citable) accession number: P64248
Secondary accession number(s): A0A1R3Y0J6, Q10374, X2BKF1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: August 30, 2017
This is version 84 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families