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Bifunctional protein GlmU [Includes: UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase); Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157)]

 K0EKS3_ALTMB            Unreviewed;       452 AA.
K0EKS3;
28-NOV-2012, integrated into UniProtKB/TrEMBL.
28-NOV-2012, sequence version 1.
16-JAN-2019, entry version 44.
RecName: Full=Bifunctional protein GlmU {ECO:0000256|HAMAP-Rule:MF_01631};
Includes:
RecName: Full=Glucosamine-1-phosphate N-acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01631};
EC=2.3.1.157 {ECO:0000256|HAMAP-Rule:MF_01631};
Includes:
RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_01631};
EC=2.7.7.23 {ECO:0000256|HAMAP-Rule:MF_01631};
AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase {ECO:0000256|HAMAP-Rule:MF_01631};
Name=glmU {ECO:0000256|HAMAP-Rule:MF_01631};
OrderedLocusNames=AMBAS45_18790 {ECO:0000313|EMBL:AFT97213.1};
Alteromonas macleodii (strain Balearic Sea AD45).
Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
Alteromonadaceae; Alteromonas.
NCBI_TaxID=1004787 {ECO:0000313|EMBL:AFT97213.1, ECO:0000313|Proteomes:UP000006308};
[1] {ECO:0000313|Proteomes:UP000006308}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Balearic Sea AD45 {ECO:0000313|Proteomes:UP000006308};
PubMed=23019517; DOI=10.1038/srep00696;
Lopez-Perez M., Gonzaga A., Martin-Cuadrado A.B., Onyshchenko O.,
Ghavidel A., Ghai R., Rodriguez-Valera F.;
"Genomes of surface isolates of Alteromonas macleodii: the life of a
widespread marine opportunistic copiotroph.";
Sci. Rep. 2:696-696(2012).
-!- FUNCTION: 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. {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083685}.
-!- CATALYTIC ACTIVITY:
Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP =
diphosphate + UDP-N-acetyl-alpha-D-glucosamine;
Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776;
EC=2.7.7.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS01124206};
-!- CATALYTIC ACTIVITY:
Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+)
+ N-acetyl-alpha-D-glucosamine 1-phosphate;
Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516;
EC=2.3.1.157; Evidence={ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS01124218};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_01631};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_01631};
-!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A
biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083707}.
-!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate
from alpha-D-glucosamine 6-phosphate (route II): step 2/2.
{ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00381596}.
-!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-
acetyl-alpha-D-glucosamine 1-phosphate: step 1/1.
{ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00381463}.
-!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00569615}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00381517}.
-!- SIMILARITY: In the C-terminal section; belongs to the transferase
hexapeptide repeat family. {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00569628}.
-!- SIMILARITY: In the N-terminal section; belongs to the N-
acetylglucosamine-1-phosphate uridyltransferase family.
{ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00569629}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01631}.
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EMBL; CP003873; AFT97213.1; -; Genomic_DNA.
RefSeq; WP_014980644.1; NC_018679.1.
EnsemblBacteria; AFT97213; AFT97213; AMBAS45_18790.
KEGG; amb:AMBAS45_18790; -.
PATRIC; fig|1004787.3.peg.3921; -.
KO; K04042; -.
OMA; IEPQTHL; -.
BioCyc; AMAC1004787:G1HAX-3827-MONOMER; -.
UniPathway; UPA00113; UER00532.
UniPathway; UPA00113; UER00533.
UniPathway; UPA00973; -.
Proteomes; UP000006308; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-UniRule.
GO; GO:0000902; P:cell morphogenesis; IEA:UniProtKB-UniRule.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
CDD; cd03353; LbH_GlmU_C; 1.
Gene3D; 3.90.550.10; -; 1.
HAMAP; MF_01631; GlmU; 1.
InterPro; IPR005882; Bifunctional_GlmU.
InterPro; IPR038009; GlmU_C_LbH.
InterPro; IPR001451; Hexapep.
InterPro; IPR018357; Hexapep_transf_CS.
InterPro; IPR025877; MobA-like_NTP_Trfase.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
InterPro; IPR011004; Trimer_LpxA-like_sf.
Pfam; PF00132; Hexapep; 2.
Pfam; PF14602; Hexapep_2; 1.
Pfam; PF12804; NTP_transf_3; 1.
SUPFAM; SSF51161; SSF51161; 1.
SUPFAM; SSF53448; SSF53448; 1.
TIGRFAMs; TIGR01173; glmU; 1.
PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
3: Inferred from homology;
Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083661};
Cell shape {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083721};
Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083688}; Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000006308};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083649};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083580};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083557};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00458631};
Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083639};
Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083721};
Repeat {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083725};
Transferase {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083639, ECO:0000256|SAAS:SAAS00083661}.
DOMAIN 5 125 NTP_transf_3. {ECO:0000259|Pfam:PF12804}.
REGION 1 226 Pyrophosphorylase. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 8 11 UDP-GlcNAc binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 78 79 UDP-GlcNAc binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 227 247 Linker. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 248 452 N-acetyltransferase. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 383 384 Acetyl-CoA binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
COILED 227 247 {ECO:0000256|SAM:Coils}.
ACT_SITE 360 360 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01631}.
METAL 102 102 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01631}.
METAL 224 224 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 22 22 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 73 73 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 137 137 UDP-GlcNAc; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01631}.
BINDING 151 151 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 166 166 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 224 224 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 330 330 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 348 348 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 363 363 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 374 374 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 377 377 Acetyl-CoA; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01631}.
BINDING 402 402 Acetyl-CoA. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 420 420 Acetyl-CoA; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01631}.
BINDING 437 437 Acetyl-CoA. {ECO:0000256|HAMAP-
Rule:MF_01631}.
SEQUENCE 452 AA; 47923 MW; 29ECB59ECB4386A5 CRC64;
MAFSVVVLAA GKGTRMKSSL PKVLHKVGGV PMVQRIINTV KSLGADNIHL VYGHGGDQLK
ATVVEDNLNW CLQAEQLGTG HAVQQAAPHI KDNEDVLVLV GDAPLIREET LSALKAAKES
CDLALLTVNL DDPTGMGRII RENDNITAIV EHKDATDAQR EIKEINTGMM MMSGADLKRW
LGELSNDNAQ GEYYLTDVIA MAAAEGKRIQ SAQPQSAVEV EGVNNRLQLA NLERALQRRQ
AEELMANGVT LLDPARFDLR GQLETGNDVI IDVNVIVEGK VTLGSNVNIG ANCILRNCTI
ADNAVIEANS IVEEASVGEA CTVGPFARLR PGAVMQKNAK VGNFVEMKKA ILGEGAKANH
LTYLGDAEVG AKANIGAGTI TCNYDGVNKS KTVIGENAFI GSNSSLVAPV NIGKGATVGA
GSVITSTVDE DALAVARGKQ RNIPNWPRPT KK


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Pathways :
WP1493: Carbon assimilation C4 pathway
WP1657: Glycerolipid metabolism
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP1028: Pentose Phosphate Pathway
WP1147: Pentose Phosphate Pathway
WP122: Pentose Phosphate Pathway
WP1231: Pentose Phosphate Pathway
WP134: Pentose Phosphate Pathway
WP1658: Glycerophospholipid metabolism
WP1664: Inositol phosphate metabolism
WP1665: Limonene and pinene degradation
WP1684: Pentose phosphate pathway
WP1689: Porphyrin and chlorophyll metabolism
WP1690: Propanoate metabolism
WP1713: Two-component system
WP1714: Tyrosine metabolism
WP2185: Purine metabolism
WP220: Ribose and Deoxyribose Phosphate Metabolism
WP2212: Methylerythritol phosphate pathway
WP228: Deoxyribose phosphate metabolism
WP253: Glycolysis
WP260: Glucose-1-phosphate metabolism
WP282: Pentose Phosphate Pathway
WP312: Pentose Phosphate Pathway

Related Genes :

Bibliography :
[23485416] Crystal structures identify an atypical two-metal-ion mechanism for uridyltransfer in GlmU: its significance to sugar nucleotidyl transferases.
[23099094] Inhibitors of the acetyltransferase domain of N-acetylglucosamine-1-phosphate-uridylyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU). Part 2: Optimization of physical properties leading to antibacterial aryl sulfonamides.
[21594607] Kinetic properties of Mycobacterium tuberculosis bifunctional GlmU.
[21370307] Self-association studies of the bifunctional N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli.
[19804974] Systematic study on the broad nucleotide triphosphate specificity of the pyrophosphorylase domain of the N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli K12.
[18573680] Expression, essentiality, and a microtiter plate assay for mycobacterial GlmU, the bifunctional glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase.
[11329257] Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites.
[11173485] Purification, crystallization and preliminary X-ray data for Escherichia coli GlmU: a bifunctional acetyltransferase/uridyltransferase.
[11118459] Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture.
[11084021] Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into autonomously functional domains and evidence that trimerization is absolutely required for glucosamine-1-phosphate acetyltransferase activity and cell growth.