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Q7V8F2

- GLMU_PROMM

UniProt

Q7V8F2 - GLMU_PROMM

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Protein

Bifunctional protein GlmU

Gene

glmU

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.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.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei21 – 211UDP-GlcNAcUniRule annotation
Binding sitei73 – 731UDP-GlcNAcUniRule annotation
Metal bindingi103 – 1031MagnesiumUniRule annotation
Binding sitei140 – 1401UDP-GlcNAc; via amide nitrogenUniRule annotation
Binding sitei155 – 1551UDP-GlcNAcUniRule annotation
Binding sitei170 – 1701UDP-GlcNAcUniRule annotation
Metal bindingi224 – 2241MagnesiumUniRule annotation
Binding sitei224 – 2241UDP-GlcNAcUniRule annotation
Binding sitei329 – 3291Acetyl-CoA; amide nitrogenUniRule annotation
Binding sitei347 – 3471Acetyl-CoAUniRule annotation
Active sitei359 – 3591Proton acceptorUniRule annotation
Binding sitei362 – 3621Acetyl-CoAUniRule annotation
Binding sitei373 – 3731Acetyl-CoAUniRule annotation
Binding sitei419 – 4191Acetyl-CoA; via amide nitrogenUniRule annotation
Binding sitei436 – 4361Acetyl-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

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:PMT_0400
OrganismiProchlorococcus marinus (strain MIT 9313)
Taxonomic identifieri74547 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000001423: 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 – 446446Bifunctional protein GlmUPRO_0000233816Add
BLAST

Interactioni

Subunit structurei

Homotrimer.UniRule annotation

Protein-protein interaction databases

STRINGi74547.PMT0400.

Structurei

3D structure databases

ProteinModelPortaliQ7V8F2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 226226PyrophosphorylaseUniRule annotationAdd
BLAST
Regioni7 – 104UDP-GlcNAc bindingUniRule annotation
Regioni78 – 792UDP-GlcNAc bindingUniRule annotation
Regioni227 – 24721LinkerUniRule annotationAdd
BLAST
Regioni248 – 446199N-acetyltransferaseUniRule annotationAdd
BLAST
Regioni382 – 3832Acetyl-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.
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

« Hide

        10         20         30         40         50
MLAVAILAAG KGTRMKSCLP KVLQPLAGST LVERVLTSCS GLQPQRRLLI
60 70 80 90 100
VGHQAQEVQQ QLTDWQGLEF VVQQPQNGTG HAVQQVLPVL EGFDGELLVL
110 120 130 140 150
NGDVPLLRPS TIEHLVNEHR SSGADVTLLT ARLADPTGYG RVFSDQQGRV
160 170 180 190 200
SSIVEHRDCS DEQRHNNLTN AGIYCFNWKK LAAVLPQLCS DNDQGELYLT
210 220 230 240 250
DTVALLPIAM HVEVADPDEV NGINDRCQLA NCEALLQERL RNYWMKEGVT
260 270 280 290 300
FTDPASCTLS EDCQFGRDVV IEPQTHLRGC CNIGDGCQLG PGSLIENAEL
310 320 330 340 350
GHGVSVLHSV VCDAKVGNEV AIGPFSHLRP GAGIADQCRI GNFVEIKKSQ
360 370 380 390 400
IGEGSKVNHL SYIGDAQLGR HVNVGAGTIT ANYDGVRKHL TVVGDNSKTG
410 420 430 440
ANSVLVAPIV LGSDVTVGAG STLTKDVPNG ALALGRSKQL IKNGWQ
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: October 29, 2014
This is version 76 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, Reference proteome

Documents

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

External Data

Dasty 3