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Protein

Bifunctional protein GlmU

Gene

glmU

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 annotation1 Publication

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 Mg2+ ion per subunit.UniRule annotation

Pathwayi: UDP-N-acetyl-alpha-D-glucosamine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Bifunctional protein GlmU (glmU)
This subpathway is part of the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II), the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis and in Nucleotide-sugar biosynthesis.

Pathwayi: UDP-N-acetyl-alpha-D-glucosamine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Bifunctional protein GlmU (glmU)
This subpathway is part of the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate, the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis and in Nucleotide-sugar biosynthesis.

Pathwayi: LPS lipid A biosynthesis

This protein is involved in the pathway LPS lipid A biosynthesis, which is part of Bacterial outer membrane biogenesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway LPS lipid A biosynthesis and in Bacterial outer membrane biogenesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei25UDP-GlcNAcUniRule annotation1
Binding sitei76UDP-GlcNAcUniRule annotation1 Publication1
Metal bindingi105MagnesiumUniRule annotation1
Binding sitei140UDP-GlcNAc; via amide nitrogenUniRule annotation1 Publication1
Binding sitei154UDP-GlcNAcUniRule annotation1 Publication1
Binding sitei169UDP-GlcNAcUniRule annotation1 Publication1
Metal bindingi227MagnesiumUniRule annotation1
Binding sitei227UDP-GlcNAcUniRule annotation1
Binding sitei333UDP-GlcNAcUniRule annotation1
Binding sitei351UDP-GlcNAcUniRule annotation1
Active sitei363Proton acceptorUniRule annotation1
Binding sitei366UDP-GlcNAcUniRule annotation1
Binding sitei377UDP-GlcNAcUniRule annotation1
Binding sitei380Acetyl-CoA; via amide nitrogenUniRule annotationBy similarity1
Binding sitei405Acetyl-CoAUniRule annotation1
Binding sitei423Acetyl-CoA; via amide nitrogenUniRule annotation1
Binding sitei440Acetyl-CoAUniRule annotation1

GO - Molecular functioni

GO - Biological processi

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

BRENDAi2.7.7.23. 2529.
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:HI_0642
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
Proteomesi
  • UP000000579 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi25K → A: No pyrophosphorylase activity. 1 Publication1
Mutagenesisi76Q → A: No pyrophosphorylase activity. 1 Publication1
Mutagenesisi103Y → A: Reduces the pyrophosphorylase activity. 1 Publication1
Mutagenesisi105D → A: No pyrophosphorylase activity. 1 Publication1
Mutagenesisi223V → A: Reduces slightly the pyrophosphorylase activity. 1 Publication1
Mutagenesisi224E → A: Reduces the pyrophosphorylase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000687031 – 456Bifunctional protein GlmUAdd BLAST456

Proteomic databases

PRIDEiP43889.

Interactioni

Subunit structurei

Homotrimer.UniRule annotation3 Publications

Protein-protein interaction databases

STRINGi71421.HI0642.

Chemistry databases

BindingDBiP43889.

Structurei

Secondary structure

1456
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 11Combined sources6
Helixi17 – 19Combined sources3
Beta strandi21 – 23Combined sources3
Helixi25 – 27Combined sources3
Beta strandi28 – 30Combined sources3
Helixi35 – 45Combined sources11
Beta strandi51 – 55Combined sources5
Helixi59 – 65Combined sources7
Turni66 – 68Combined sources3
Beta strandi72 – 75Combined sources4
Helixi82 – 89Combined sources8
Helixi90 – 92Combined sources3
Beta strandi97 – 103Combined sources7
Helixi111 – 120Combined sources10
Beta strandi125 – 132Combined sources8
Beta strandi141 – 145Combined sources5
Beta strandi148 – 153Combined sources6
Turni155 – 157Combined sources3
Helixi160 – 163Combined sources4
Beta strandi167 – 176Combined sources10
Helixi177 – 184Combined sources8
Helixi198 – 200Combined sources3
Helixi201 – 207Combined sources7
Beta strandi212 – 216Combined sources5
Helixi221 – 223Combined sources3
Helixi229 – 249Combined sources21
Beta strandi253 – 255Combined sources3
Helixi257 – 259Combined sources3
Beta strandi260 – 268Combined sources9
Beta strandi276 – 286Combined sources11
Beta strandi297 – 303Combined sources7
Beta strandi314 – 320Combined sources7
Beta strandi328 – 332Combined sources5
Beta strandi336 – 338Combined sources3
Beta strandi343 – 352Combined sources10
Beta strandi360 – 372Combined sources13
Beta strandi383 – 386Combined sources4
Beta strandi388 – 391Combined sources4
Beta strandi395 – 397Combined sources3
Beta strandi408 – 415Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V0HX-ray1.79A1-456[»]
2V0IX-ray1.89A1-456[»]
2V0JX-ray2.00A1-456[»]
2V0KX-ray2.30A1-456[»]
2V0LX-ray2.20A1-456[»]
2VD4X-ray1.90A1-456[»]
2W0VX-ray1.99A1-456[»]
2W0WX-ray2.59A1-456[»]
4E1KX-ray2.00A1-456[»]
4KNRX-ray2.10A1-456[»]
4KNXX-ray1.90A1-456[»]
4KPXX-ray2.21A1-456[»]
4KPZX-ray2.09A1-456[»]
4KQLX-ray2.31A1-456[»]
ProteinModelPortaliP43889.
SMRiP43889.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43889.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 229PyrophosphorylaseUniRule annotationAdd BLAST229
Regioni11 – 14UDP-GlcNAc bindingUniRule annotation3 Publications4
Regioni81 – 82UDP-GlcNAc bindingUniRule annotation2 Publications2
Regioni103 – 105UDP-GlcNAc bindingUniRule annotation3 Publications3
Regioni230 – 250LinkerUniRule annotationAdd BLAST21
Regioni251 – 456N-acetyltransferaseUniRule annotationAdd BLAST206
Regioni386 – 387Acetyl-CoA bindingUniRule annotation2

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105CAJ. Bacteria.
COG1207. LUCA.
KOiK04042.
OMAiFAHARPK.
PhylomeDBiP43889.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_01631. GlmU. 1 hit.
InterProiIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep.
IPR018357. Hexapep_transf_CS.
IPR025877. MobA-like_NTP_Trfase.
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.

P43889-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKKALSAVI LAAGKGTRMY SDLPKVLHTI AGKPMVKHVI DTAHQLGSEN
60 70 80 90 100
IHLIYGHGGD LMRTHLANEQ VNWVLQTEQL GTAHAVQQAA PFFKDNENIV
110 120 130 140 150
VLYGDAPLIT KETLEKLIEA KPENGIALLT VNLDNPTGYG RIIRENGNVV
160 170 180 190 200
AIVEQKDANA EQLNIKEVNT GVMVSDGASF KKWLARVGNN NAQGEYYLTD
210 220 230 240 250
LIALANQDNC QVVAVQATDV MEVEGANNRL QLAALERYFQ NKQASKLLLE
260 270 280 290 300
GVMIYDPARF DLRGTLEHGK DVEIDVNVII EGNVKLGDRV KIGTGCVLKN
310 320 330 340 350
VVIGNDVEIK PYSVLEDSIV GEKAAIGPFS RLRPGAELAA ETHVGNFVEI
360 370 380 390 400
KKSTVGKGSK VNHLTYVGDS EIGSNCNIGA GVITCNYDGA NKFKTIIGDD
410 420 430 440 450
VFVGSDTQLV APVKVANGAT IGAGTTITRD VGENELVITR VAQRHIQGWQ

RPIKKK
Length:456
Mass (Da):49,287
Last modified:November 1, 1995 - v1
Checksum:i93B76552A8F9BD36
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22302.1.
PIRiG64083.
RefSeqiNP_438802.1. NC_000907.1.
WP_005694502.1. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC22302; AAC22302; HI_0642.
GeneIDi949691.
KEGGihin:HI0642.
PATRICi20189891. VBIHaeInf48452_0670.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22302.1.
PIRiG64083.
RefSeqiNP_438802.1. NC_000907.1.
WP_005694502.1. NC_000907.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V0HX-ray1.79A1-456[»]
2V0IX-ray1.89A1-456[»]
2V0JX-ray2.00A1-456[»]
2V0KX-ray2.30A1-456[»]
2V0LX-ray2.20A1-456[»]
2VD4X-ray1.90A1-456[»]
2W0VX-ray1.99A1-456[»]
2W0WX-ray2.59A1-456[»]
4E1KX-ray2.00A1-456[»]
4KNRX-ray2.10A1-456[»]
4KNXX-ray1.90A1-456[»]
4KPXX-ray2.21A1-456[»]
4KPZX-ray2.09A1-456[»]
4KQLX-ray2.31A1-456[»]
ProteinModelPortaliP43889.
SMRiP43889.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi71421.HI0642.

Chemistry databases

BindingDBiP43889.

Proteomic databases

PRIDEiP43889.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC22302; AAC22302; HI_0642.
GeneIDi949691.
KEGGihin:HI0642.
PATRICi20189891. VBIHaeInf48452_0670.

Phylogenomic databases

eggNOGiENOG4105CAJ. Bacteria.
COG1207. LUCA.
KOiK04042.
OMAiFAHARPK.
PhylomeDBiP43889.

Enzyme and pathway databases

UniPathwayiUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.
BRENDAi2.7.7.23. 2529.

Miscellaneous databases

EvolutionaryTraceiP43889.
PROiP43889.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_01631. GlmU. 1 hit.
InterProiIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep.
IPR018357. Hexapep_transf_CS.
IPR025877. MobA-like_NTP_Trfase.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiGLMU_HAEIN
AccessioniPrimary (citable) accession number: P43889
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 124 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

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Haemophilus influenzae
    Haemophilus influenzae (strain Rd): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.