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Q7V8F2

- GLMU_PROMM

UniProt

Q7V8F2 - GLMU_PROMM

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Protein
Bifunctional protein GlmU
Gene
glmU, PMT_0400
Organism
Prochlorococcus marinus (strain MIT 9313)
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 sitei21 – 211UDP-GlcNAc By similarity
Binding sitei73 – 731UDP-GlcNAc By similarity
Metal bindingi103 – 1031Magnesium By similarity
Binding sitei140 – 1401UDP-GlcNAc; via amide nitrogen By similarity
Binding sitei155 – 1551UDP-GlcNAc By similarity
Binding sitei170 – 1701UDP-GlcNAc By similarity
Metal bindingi224 – 2241Magnesium By similarity
Binding sitei224 – 2241UDP-GlcNAc By similarity
Binding sitei329 – 3291Acetyl-CoA; amide nitrogen By similarity
Binding sitei347 – 3471Acetyl-CoA By similarity
Active sitei359 – 3591Proton acceptor By similarity
Binding sitei362 – 3621Acetyl-CoA By similarity
Binding sitei373 – 3731Acetyl-CoA By similarity
Binding sitei419 – 4191Acetyl-CoA; via amide nitrogen By similarity
Binding sitei436 – 4361Acetyl-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

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:PMT_0400
OrganismiProchlorococcus marinus (strain MIT 9313)
Taxonomic identifieri74547 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000001423: 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 – 446446Bifunctional protein GlmUUniRule annotation
PRO_0000233816Add
BLAST

Interactioni

Subunit structurei

Homotrimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi74547.PMT0400.

Structurei

3D structure databases

ProteinModelPortaliQ7V8F2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 226226Pyrophosphorylase By similarity
Add
BLAST
Regioni7 – 104UDP-GlcNAc binding By similarity
Regioni78 – 792UDP-GlcNAc binding By similarity
Regioni227 – 24721Linker By similarity
Add
BLAST
Regioni248 – 446199N-acetyltransferase By similarity
Add
BLAST
Regioni382 – 3832Acetyl-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.
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. 4 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.

Q7V8F2-1 [UniParc]FASTAAdd to Basket

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MLAVAILAAG KGTRMKSCLP KVLQPLAGST LVERVLTSCS GLQPQRRLLI    50
VGHQAQEVQQ QLTDWQGLEF VVQQPQNGTG HAVQQVLPVL EGFDGELLVL 100
NGDVPLLRPS TIEHLVNEHR SSGADVTLLT ARLADPTGYG RVFSDQQGRV 150
SSIVEHRDCS DEQRHNNLTN AGIYCFNWKK LAAVLPQLCS DNDQGELYLT 200
DTVALLPIAM HVEVADPDEV NGINDRCQLA NCEALLQERL RNYWMKEGVT 250
FTDPASCTLS EDCQFGRDVV IEPQTHLRGC CNIGDGCQLG PGSLIENAEL 300
GHGVSVLHSV VCDAKVGNEV AIGPFSHLRP GAGIADQCRI GNFVEIKKSQ 350
IGEGSKVNHL SYIGDAQLGR HVNVGAGTIT ANYDGVRKHL TVVGDNSKTG 400
ANSVLVAPIV LGSDVTVGAG STLTKDVPNG ALALGRSKQL IKNGWQ 446
Length:446
Mass (Da):47,744
Last modified:October 1, 2003 - v1
Checksum:iC53372DB8F81E797
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX548175 Genomic DNA. Translation: CAE20575.1.
RefSeqiNP_894233.1. NC_005071.1.
WP_011129779.1. NC_005071.1.

Genome annotation databases

EnsemblBacteriaiCAE20575; CAE20575; PMT_0400.
GeneIDi1729380.
KEGGipmt:PMT0400.
PATRICi23008645. VBIProMar135351_0480.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX548175 Genomic DNA. Translation: CAE20575.1 .
RefSeqi NP_894233.1. NC_005071.1.
WP_011129779.1. NC_005071.1.

3D structure databases

ProteinModelPortali Q7V8F2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 74547.PMT0400.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAE20575 ; CAE20575 ; PMT_0400 .
GeneIDi 1729380.
KEGGi pmt:PMT0400.
PATRICi 23008645. VBIProMar135351_0480.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00113 ; UER00532 .
UPA00113 ; UER00533 .
UPA00973 .

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. 4 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: MIT 9313.

Entry informationi

Entry nameiGLMU_PROMM
AccessioniPrimary (citable) accession number: Q7V8F2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: October 1, 2003
Last modified: September 3, 2014
This is version 74 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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