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A1KR65

- GLMU_NEIMF

UniProt

A1KR65 - GLMU_NEIMF

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Protein
Bifunctional protein GlmU
Gene
glmU, NMC0015
Organism
Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18)
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 sitei25 – 251UDP-GlcNAc By similarity
Binding sitei75 – 751UDP-GlcNAc By similarity
Metal bindingi104 – 1041Magnesium By similarity
Binding sitei138 – 1381UDP-GlcNAc; via amide nitrogen By similarity
Binding sitei153 – 1531UDP-GlcNAc By similarity
Binding sitei168 – 1681UDP-GlcNAc By similarity
Metal bindingi226 – 2261Magnesium By similarity
Binding sitei226 – 2261UDP-GlcNAc By similarity
Binding sitei332 – 3321Acetyl-CoA; amide nitrogen By similarity
Binding sitei350 – 3501Acetyl-CoA By similarity
Active sitei362 – 3621Proton acceptor By similarity
Binding sitei365 – 3651Acetyl-CoA By similarity
Binding sitei376 – 3761Acetyl-CoA By similarity
Binding sitei404 – 4041Acetyl-CoA By similarity
Binding sitei422 – 4221Acetyl-CoA; via amide nitrogen By similarity
Binding sitei439 – 4391Acetyl-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

BioCyciNMEN272831:GJDX-15-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:NMC0015
OrganismiNeisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18)
Taxonomic identifieri272831 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
ProteomesiUP000002286: 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 – 456456Bifunctional protein GlmUUniRule annotation
PRO_1000056175Add
BLAST

Interactioni

Subunit structurei

Homotrimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi272831.NMC0015.

Structurei

3D structure databases

ProteinModelPortaliA1KR65.
SMRiA1KR65. Positions 5-450.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 228228Pyrophosphorylase By similarity
Add
BLAST
Regioni11 – 144UDP-GlcNAc binding By similarity
Regioni80 – 812UDP-GlcNAc binding By similarity
Regioni102 – 1043UDP-GlcNAc binding By similarity
Regioni229 – 24921Linker By similarity
Add
BLAST
Regioni250 – 456207N-acetyltransferase By similarity
Add
BLAST
Regioni385 – 3862Acetyl-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.
OMAiDCVTNQD.
OrthoDBiEOG6Z6FQZ.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_01631. GlmU.
InterProiIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR025877. MobA-like_NTP_Trfase_dom.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF00132. Hexapep. 2 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.
TIGRFAMsiTIGR01173. glmU. 1 hit.

Sequencei

Sequence statusi: Complete.

A1KR65-1 [UniParc]FASTAAdd to Basket

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MPQNTLNIVI LAAGKGTRMY SKMPKVLHRI GGKPMLGRVI DTAAALNPQN    50
ICVVIGHGKD QVLNAVKRDV VWVEQTEQLG TGHAVKTALP HLSAEGRTLV 100
LYGDVPLIDV KTLKTLLEAA GNEVGLLTDV PADPTGLGRI IRDGNGSVTA 150
IVEEKDADAA QKAVKEINTG ILVLPNAKLE NWLNSLSSNN AQGEYYLTDL 200
IAKAVADGIK VHPVQVHTSY LAAGVNNKLQ LAELERIFQT EQAQELLKAG 250
VTLSDPARFD LRGRLKHGQD VVIDVNCIFE GEVEIGDNVE IGANCVIKNA 300
KIGANSKIAP FSHLEDCEVG ENNRIGPYAR LRPQAKLAAD VHIGNFVEIK 350
NAAIGKGTKA NHLTYIGDAE VGSKTNFGAG TIIANYDGVH KHKTVIGNEV 400
RIGSNCVLVA PVTLGNKVTT GAGSAITRNV EDGKLALARA RQTVIEGWVR 450
PEKDKQ 456
Length:456
Mass (Da):48,683
Last modified:February 6, 2007 - v1
Checksum:iD5A1494FBDD3F59B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM421808 Genomic DNA. Translation: CAM09341.1.
RefSeqiYP_974160.1. NC_008767.1.

Genome annotation databases

EnsemblBacteriaiCAM09341; CAM09341; NMC0015.
GeneIDi4676123.
KEGGinmc:NMC0015.
PATRICi20349497. VBINeiMen17609_0022.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM421808 Genomic DNA. Translation: CAM09341.1 .
RefSeqi YP_974160.1. NC_008767.1.

3D structure databases

ProteinModelPortali A1KR65.
SMRi A1KR65. Positions 5-450.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272831.NMC0015.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAM09341 ; CAM09341 ; NMC0015 .
GeneIDi 4676123.
KEGGi nmc:NMC0015.
PATRICi 20349497. VBINeiMen17609_0022.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00113 ; UER00532 .
UPA00113 ; UER00533 .
UPA00973 .
BioCyci NMEN272831:GJDX-15-MONOMER.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
HAMAPi MF_01631. GlmU.
InterProi IPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR025877. MobA-like_NTP_Trfase_dom.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view ]
Pfami PF00132. Hexapep. 2 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view ]
SUPFAMi SSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.
TIGRFAMsi TIGR01173. glmU. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700532 / DSM 15464 / FAM18.

Entry informationi

Entry nameiGLMU_NEIMF
AccessioniPrimary (citable) accession number: A1KR65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: June 11, 2014
This is version 62 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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