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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)]

 H0BJ79_9ACTN            Unreviewed;       481 AA.
H0BJ79;
22-FEB-2012, integrated into UniProtKB/TrEMBL.
22-FEB-2012, sequence version 1.
16-JAN-2019, entry version 48.
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};
ORFNames=SPW_5338 {ECO:0000313|EMBL:EHM26305.1};
Streptomyces sp. W007.
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces.
NCBI_TaxID=1055352 {ECO:0000313|EMBL:EHM26305.1, ECO:0000313|Proteomes:UP000004626};
[1] {ECO:0000313|EMBL:EHM26305.1, ECO:0000313|Proteomes:UP000004626}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=W007 {ECO:0000313|EMBL:EHM26305.1,
ECO:0000313|Proteomes:UP000004626};
PubMed=22374958; DOI=10.1128/JB.06701-11;
Qin S., Zhang H., Li F., Zhu B., Zheng H.;
"Draft Genome Sequence of Marine Streptomyces sp. Strain W007, Which
Produces Angucyclinone Antibiotics with a Benz[a]anthracene
Skeleton.";
J. Bacteriol. 194:1628-1629(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}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:EHM26305.1}.
-----------------------------------------------------------------------
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EMBL; AGSW01000188; EHM26305.1; -; Genomic_DNA.
RefSeq; WP_007455205.1; NZ_AGSW01000188.1.
EnsemblBacteria; EHM26305; EHM26305; SPW_5338.
PATRIC; fig|1055352.3.peg.5470; -.
UniPathway; UPA00113; UER00532.
UniPathway; UPA00113; UER00533.
UniPathway; UPA00973; -.
Proteomes; UP000004626; Unassembled WGS sequence.
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; IPR025877; MobA-like_NTP_Trfase.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
InterPro; IPR011004; Trimer_LpxA-like_sf.
Pfam; PF00132; Hexapep; 2.
Pfam; PF12804; NTP_transf_3; 1.
SUPFAM; SSF51161; SSF51161; 1.
SUPFAM; SSF53448; SSF53448; 1.
TIGRFAMs; TIGR01173; glmU; 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};
Complete proteome {ECO:0000313|Proteomes:UP000004626};
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 9 138 NTP_transf_3. {ECO:0000259|Pfam:PF12804}.
REGION 1 237 Pyrophosphorylase. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 12 15 UDP-GlcNAc binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 83 84 UDP-GlcNAc binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 238 258 Linker. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 259 481 N-acetyltransferase. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 393 394 Acetyl-CoA binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
ACT_SITE 370 370 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01631}.
METAL 109 109 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01631}.
METAL 235 235 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 26 26 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 78 78 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 146 146 UDP-GlcNAc; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01631}.
BINDING 162 162 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 177 177 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 235 235 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 340 340 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 358 358 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 373 373 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 384 384 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 387 387 Acetyl-CoA; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01631}.
BINDING 412 412 Acetyl-CoA. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 430 430 Acetyl-CoA; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01631}.
BINDING 447 447 Acetyl-CoA. {ECO:0000256|HAMAP-
Rule:MF_01631}.
SEQUENCE 481 AA; 49627 MW; F6B58F5E8CA07904 CRC64;
MSATSPAAVV VLAAGEGTRM KSKTPKVLHE ISGRSLVGHV VAAARELDPQ HLVVVVGHAS
EQVTAHLNAG DAVRTAFQAE QNGTGHAVRM GLEELGGNVE GTVIVVCGDT PLLSGGTLGA
LAATHAADAN AVTVLSAEVP DSTGYGRIVR DPATGAVTEI VEHKDATDEQ RAIREINSGV
FAFDGRLLGD ALGKVRTDNS QGEEYLTDVL SILREAGHRV GASVAGDHRE ILGINNRLQL
AEARRLLNER LLERAMLAGV TVVDPASTLI DATVTYERDA VVHPGTQLLG ATHLAEDSEV
GPNSRIENTV VGAGARVDNS VTLSAEIGAG ALVGPYAYLR PGTRLGTKAK AGTYVEMKNA
TIGEGTKVPH LSYVGDATIG DHTNIGAASV FVNYDGVAKH HTTIGSHCRT GSDNMFVAPV
TVGDGVYTAA GSVITKDVPA GSLAVARGQQ RNIEGWVARK RPGSAAAQAA QASSQETDGQ
S


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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.