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A1KR65

- GLMU_NEIMF

UniProt

A1KR65 - GLMU_NEIMF

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Protein

Bifunctional protein GlmU

Gene

glmU

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.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

Mg2+UniRule annotationNote: Binds 1 Mg(2+) ion per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei25 – 251UDP-GlcNAcUniRule annotation
Binding sitei75 – 751UDP-GlcNAcUniRule annotation
Metal bindingi104 – 1041MagnesiumUniRule annotation
Binding sitei138 – 1381UDP-GlcNAc; via amide nitrogenUniRule annotation
Binding sitei153 – 1531UDP-GlcNAcUniRule annotation
Binding sitei168 – 1681UDP-GlcNAcUniRule annotation
Metal bindingi226 – 2261MagnesiumUniRule annotation
Binding sitei226 – 2261UDP-GlcNAcUniRule annotation
Binding sitei332 – 3321Acetyl-CoA; amide nitrogenUniRule annotation
Binding sitei350 – 3501Acetyl-CoAUniRule annotation
Active sitei362 – 3621Proton acceptorUniRule annotation
Binding sitei365 – 3651Acetyl-CoAUniRule annotation
Binding sitei376 – 3761Acetyl-CoAUniRule annotation
Binding sitei404 – 4041Acetyl-CoAUniRule annotation
Binding sitei422 – 4221Acetyl-CoA; via amide nitrogenUniRule annotation
Binding sitei439 – 4391Acetyl-CoAUniRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. cell morphogenesis Source: UniProtKB-HAMAP
  2. cell wall organization Source: UniProtKB-KW
  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
  7. UDP-N-acetylglucosamine biosynthetic process Source: UniProtKB-UniPathway
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 GlmUUniRule annotation
Including the following 2 domains:
UDP-N-acetylglucosamine pyrophosphorylaseUniRule annotation (EC:2.7.7.23UniRule annotation)
Alternative name(s):
N-acetylglucosamine-1-phosphate uridyltransferaseUniRule annotation
Glucosamine-1-phosphate N-acetyltransferaseUniRule annotation (EC:2.3.1.157UniRule annotation)
Gene namesi
Name:glmUUniRule annotation
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 UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 456456Bifunctional protein GlmUPRO_1000056175Add
BLAST

Interactioni

Subunit structurei

Homotrimer.UniRule annotation

Protein-protein interaction databases

STRINGi272831.NMC0015.

Structurei

3D structure databases

ProteinModelPortaliA1KR65.
SMRiA1KR65. Positions 5-450.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 228228PyrophosphorylaseUniRule annotationAdd
BLAST
Regioni11 – 144UDP-GlcNAc bindingUniRule annotation
Regioni80 – 812UDP-GlcNAc bindingUniRule annotation
Regioni102 – 1043UDP-GlcNAc bindingUniRule annotation
Regioni229 – 24921LinkerUniRule annotationAdd
BLAST
Regioni250 – 456207N-acetyltransferaseUniRule annotationAdd
BLAST
Regioni385 – 3862Acetyl-CoA bindingUniRule annotation

Sequence similaritiesi

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

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

« Hide

        10         20         30         40         50
MPQNTLNIVI LAAGKGTRMY SKMPKVLHRI GGKPMLGRVI DTAAALNPQN
60 70 80 90 100
ICVVIGHGKD QVLNAVKRDV VWVEQTEQLG TGHAVKTALP HLSAEGRTLV
110 120 130 140 150
LYGDVPLIDV KTLKTLLEAA GNEVGLLTDV PADPTGLGRI IRDGNGSVTA
160 170 180 190 200
IVEEKDADAA QKAVKEINTG ILVLPNAKLE NWLNSLSSNN AQGEYYLTDL
210 220 230 240 250
IAKAVADGIK VHPVQVHTSY LAAGVNNKLQ LAELERIFQT EQAQELLKAG
260 270 280 290 300
VTLSDPARFD LRGRLKHGQD VVIDVNCIFE GEVEIGDNVE IGANCVIKNA
310 320 330 340 350
KIGANSKIAP FSHLEDCEVG ENNRIGPYAR LRPQAKLAAD VHIGNFVEIK
360 370 380 390 400
NAAIGKGTKA NHLTYIGDAE VGSKTNFGAG TIIANYDGVH KHKTVIGNEV
410 420 430 440 450
RIGSNCVLVA PVTLGNKVTT GAGSAITRNV EDGKLALARA RQTVIEGWVR

PEKDKQ
Length:456
Mass (Da):48,683
Last modified:February 6, 2007 - v1
Checksum:iD5A1494FBDD3F59B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 65 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