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B8J9N1

- GLMU_ANAD2

UniProt

B8J9N1 - GLMU_ANAD2

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Protein
Bifunctional protein GlmU
Gene
glmU, A2cp1_4101
Organism
Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain By similarity.UniRule annotation

Catalytic activityi

Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate.UniRule annotation
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine.UniRule annotation

Cofactori

Binds 1 magnesium ion per subunit By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei27 – 271UDP-GlcNAc By similarity
Binding sitei82 – 821UDP-GlcNAc By similarity
Metal bindingi112 – 1121Magnesium By similarity
Binding sitei149 – 1491UDP-GlcNAc; via amide nitrogen By similarity
Binding sitei164 – 1641UDP-GlcNAc By similarity
Binding sitei179 – 1791UDP-GlcNAc By similarity
Metal bindingi235 – 2351Magnesium By similarity
Binding sitei235 – 2351UDP-GlcNAc By similarity
Binding sitei341 – 3411Acetyl-CoA; amide nitrogen By similarity
Binding sitei359 – 3591Acetyl-CoA By similarity
Active sitei371 – 3711Proton acceptor By similarity
Binding sitei374 – 3741Acetyl-CoA By similarity
Binding sitei385 – 3851Acetyl-CoA By similarity
Binding sitei413 – 4131Acetyl-CoA By similarity
Binding sitei431 – 4311Acetyl-CoA; via amide nitrogen By similarity
Binding sitei448 – 4481Acetyl-CoA By similarity

GO - Molecular functioni

  1. UDP-N-acetylglucosamine diphosphorylase activity Source: UniProtKB-HAMAP
  2. glucosamine-1-phosphate N-acetyltransferase activity Source: UniProtKB-HAMAP
  3. magnesium ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. UDP-N-acetylglucosamine biosynthetic process Source: UniProtKB-UniPathway
  2. cell morphogenesis Source: UniProtKB-HAMAP
  3. lipid A biosynthetic process Source: UniProtKB-UniPathway
  4. lipopolysaccharide biosynthetic process Source: InterPro
  5. peptidoglycan biosynthetic process Source: UniProtKB-HAMAP
  6. regulation of cell shape Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciADEH455488:GH35-4157-MONOMER.
UniPathwayiUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional protein GlmU
Including the following 2 domains:
UDP-N-acetylglucosamine pyrophosphorylase (EC:2.7.7.23)
Alternative name(s):
N-acetylglucosamine-1-phosphate uridyltransferase
Glucosamine-1-phosphate N-acetyltransferase (EC:2.3.1.157)
Gene namesi
Name:glmU
Ordered Locus Names:A2cp1_4101
OrganismiAnaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258)
Taxonomic identifieri455488 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter
ProteomesiUP000007089: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 488488Bifunctional protein GlmUUniRule annotation
PRO_1000186392Add
BLAST

Interactioni

Subunit structurei

Homotrimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi455488.A2cp1_4101.

Structurei

3D structure databases

ProteinModelPortaliB8J9N1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 237237Pyrophosphorylase By similarity
Add
BLAST
Regioni13 – 164UDP-GlcNAc binding By similarity
Regioni87 – 882UDP-GlcNAc binding By similarity
Regioni110 – 1123UDP-GlcNAc binding By similarity
Regioni238 – 25821Linker By similarity
Add
BLAST
Regioni259 – 488230N-acetyltransferase By similarity
Add
BLAST
Regioni394 – 3952Acetyl-CoA binding By similarity

Sequence similaritiesi

In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.
In the C-terminal section; belongs to the transferase hexapeptide repeat family.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1207.
HOGENOMiHOG000283476.
KOiK04042.
OMAiIGERAYI.
OrthoDBiEOG6Z6FQZ.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_01631. GlmU.
InterProiIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR025877. MobA-like_NTP_Trfase_dom.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF00132. Hexapep. 3 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.
TIGRFAMsiTIGR01173. glmU. 1 hit.
PROSITEiPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B8J9N1-1 [UniParc]FASTAAdd to Basket

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MPRTRTPLAA IVLAAGKGTR MKSNKAKVLH EVAGRPLAYY PVKRALELGA    50
SPVVVVVGHQ AEAVEAALSA ALPEAPLRFA VQEQQLGTAH AVLAAKRALR 100
GYRGPVLILS GDTPLLRAET LEAVVSAGRR ARAAVSLATM TLEVPRGYGR 150
VVRDARGRPA RIVEEKDATE AERAVREVNA GLYCVDAELL WKKLAKVGTA 200
NAQREFYLTD LVPMAAQAGG VAGVEVPAEE ASGVNDRVEL SRANRVMVGR 250
LAEAFMRAGV TIEDPARFDC DEGVEIGADA VIEPNVRLRG RTRVGARTRV 300
GVGAVITDGV LADGVTVNPY TVISEAQVAE GAILGPFSRL RPGADIGPEA 350
HVGNFVEVKK SRLGKGAKAN HLAYLGDAEI GAGANIGAGT ITCNYDGERK 400
NPTRIGEGAF IGSDSILVAP IEIGAGAYVA AGSTLTDPVP AGALALGRAR 450
QVTKEGWVAQ RQAEKQMKGT ATGPASARKG RPAARRAS 488
Length:488
Mass (Da):50,902
Last modified:March 3, 2009 - v1
Checksum:i889645503870632F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001359 Genomic DNA. Translation: ACL67419.1.
RefSeqiWP_015935139.1. NC_011891.1.
YP_002494485.1. NC_011891.1.

Genome annotation databases

EnsemblBacteriaiACL67419; ACL67419; A2cp1_4101.
GeneIDi7297526.
KEGGiacp:A2cp1_4101.
PATRICi20915156. VBIAnaDeh28364_4136.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001359 Genomic DNA. Translation: ACL67419.1 .
RefSeqi WP_015935139.1. NC_011891.1.
YP_002494485.1. NC_011891.1.

3D structure databases

ProteinModelPortali B8J9N1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 455488.A2cp1_4101.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACL67419 ; ACL67419 ; A2cp1_4101 .
GeneIDi 7297526.
KEGGi acp:A2cp1_4101.
PATRICi 20915156. VBIAnaDeh28364_4136.

Phylogenomic databases

eggNOGi COG1207.
HOGENOMi HOG000283476.
KOi K04042.
OMAi IGERAYI.
OrthoDBi EOG6Z6FQZ.

Enzyme and pathway databases

UniPathwayi UPA00113 ; UER00532 .
UPA00113 ; UER00533 .
UPA00973 .
BioCyci ADEH455488:GH35-4157-MONOMER.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
HAMAPi MF_01631. GlmU.
InterProi IPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR025877. MobA-like_NTP_Trfase_dom.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view ]
Pfami PF00132. Hexapep. 3 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view ]
SUPFAMi SSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.
TIGRFAMsi TIGR01173. glmU. 1 hit.
PROSITEi PS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1."
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Beliaev A.S., Richardson P.
    Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 2CP-1 / ATCC BAA-258.

Entry informationi

Entry nameiGLMU_ANAD2
AccessioniPrimary (citable) accession number: B8J9N1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: September 3, 2014
This is version 38 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, Multifunctional enzyme

Documents

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

External Data

Dasty 3

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