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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)]

 GLMU_MYCSS              Reviewed;         497 AA.
Q1B431;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
11-JUL-2006, sequence version 1.
22-NOV-2017, entry version 82.
RecName: Full=Bifunctional protein GlmU {ECO:0000255|HAMAP-Rule:MF_01631};
Includes:
RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01631};
EC=2.7.7.23 {ECO:0000255|HAMAP-Rule:MF_01631};
AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase {ECO:0000255|HAMAP-Rule:MF_01631};
Includes:
RecName: Full=Glucosamine-1-phosphate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01631};
EC=2.3.1.157 {ECO:0000255|HAMAP-Rule:MF_01631};
Name=glmU {ECO:0000255|HAMAP-Rule:MF_01631};
OrderedLocusNames=Mmcs_4248;
Mycobacterium sp. (strain MCS).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium.
NCBI_TaxID=164756;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MCS;
US DOE Joint Genome Institute;
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Hauser L.,
Kyrpides N., Kim E., Miller C.D., Hughes J.E., Anderson A.J.,
Sims R.C., Richardson P.;
"Complete sequence of chromosome of Mycobacterium sp. MCS.";
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
-!- 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:0000255|HAMAP-Rule:MF_01631}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + alpha-D-glucosamine 1-phosphate =
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate.
{ECO:0000255|HAMAP-Rule:MF_01631}.
-!- CATALYTIC ACTIVITY: UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
= diphosphate + UDP-N-acetyl-alpha-D-glucosamine.
{ECO:0000255|HAMAP-Rule:MF_01631}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_01631};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
Rule:MF_01631};
-!- 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:0000255|HAMAP-Rule:MF_01631}.
-!- 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:0000255|HAMAP-Rule:MF_01631}.
-!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A
biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01631}.
-!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01631}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01631}.
-!- SIMILARITY: In the N-terminal section; belongs to the N-
acetylglucosamine-1-phosphate uridyltransferase family.
{ECO:0000255|HAMAP-Rule:MF_01631}.
-!- SIMILARITY: In the C-terminal section; belongs to the transferase
hexapeptide repeat family. {ECO:0000255|HAMAP-Rule:MF_01631}.
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EMBL; CP000384; ABG10353.1; -; Genomic_DNA.
RefSeq; WP_011561626.1; NC_008146.1.
ProteinModelPortal; Q1B431; -.
SMR; Q1B431; -.
EnsemblBacteria; ABG10353; ABG10353; Mmcs_4248.
GeneID; 32418986; -.
KEGG; mmc:Mmcs_4248; -.
HOGENOM; HOG000283476; -.
KO; K04042; -.
OMA; VNHLSYI; -.
UniPathway; UPA00113; UER00532.
UniPathway; UPA00113; UER00533.
UniPathway; UPA00973; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-EC.
GO; GO:0000902; P:cell morphogenesis; IEA:InterPro.
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-KW.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.90.550.10; -; 1.
HAMAP; MF_01631; GlmU; 1.
InterPro; IPR005882; Bifunctional_GlmU.
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; Cell shape; Cell wall biogenesis/degradation;
Cytoplasm; Magnesium; Metal-binding; Multifunctional enzyme;
Nucleotidyltransferase; Peptidoglycan synthesis; Repeat; Transferase.
CHAIN 1 497 Bifunctional protein GlmU.
/FTId=PRO_0000263142.
REGION 1 243 Pyrophosphorylase. {ECO:0000255|HAMAP-
Rule:MF_01631}.
REGION 16 19 UDP-GlcNAc binding. {ECO:0000255|HAMAP-
Rule:MF_01631}.
REGION 92 93 UDP-GlcNAc binding. {ECO:0000255|HAMAP-
Rule:MF_01631}.
REGION 244 264 Linker. {ECO:0000255|HAMAP-
Rule:MF_01631}.
REGION 265 497 N-acetyltransferase. {ECO:0000255|HAMAP-
Rule:MF_01631}.
REGION 399 400 Acetyl-CoA binding. {ECO:0000255|HAMAP-
Rule:MF_01631}.
ACT_SITE 376 376 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_01631}.
METAL 118 118 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_01631}.
METAL 241 241 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_01631}.
BINDING 30 30 UDP-GlcNAc. {ECO:0000255|HAMAP-
Rule:MF_01631}.
BINDING 87 87 UDP-GlcNAc. {ECO:0000255|HAMAP-
Rule:MF_01631}.
BINDING 153 153 UDP-GlcNAc; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_01631}.
BINDING 168 168 UDP-GlcNAc. {ECO:0000255|HAMAP-
Rule:MF_01631}.
BINDING 183 183 UDP-GlcNAc. {ECO:0000255|HAMAP-
Rule:MF_01631}.
BINDING 241 241 UDP-GlcNAc. {ECO:0000255|HAMAP-
Rule:MF_01631}.
BINDING 346 346 UDP-GlcNAc. {ECO:0000255|HAMAP-
Rule:MF_01631}.
BINDING 364 364 UDP-GlcNAc. {ECO:0000255|HAMAP-
Rule:MF_01631}.
BINDING 379 379 UDP-GlcNAc. {ECO:0000255|HAMAP-
Rule:MF_01631}.
BINDING 390 390 UDP-GlcNAc. {ECO:0000255|HAMAP-
Rule:MF_01631}.
BINDING 393 393 Acetyl-CoA; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_01631}.
BINDING 418 418 Acetyl-CoA. {ECO:0000255|HAMAP-
Rule:MF_01631}.
BINDING 436 436 Acetyl-CoA; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_01631}.
SEQUENCE 497 AA; 51455 MW; A0C22BEC4EDD38A8 CRC64;
MTSSTTSSTD TAVLVLAAGA GTRMRSDIPK VLHTLGGRSM LAHALHTVAK VAPQHLVVVL
GHDRERIAPA VEALATDLGR PIDVAIQDQQ LGTGHAAECG LAALPEDFTG VVVVTAGDVP
LLDADTMADL LATHGSAAAT VLTTTVDDPT GYGRILRTQD NEVTSIVEQA DASPSQRAIR
EVNAGVYAFD ITALRSALRR LRSDNAQHEL YLTDVIAIFR QDGLSVRARH VDDSALVAGV
NDRVQLAALG AELNRRIVTA HQRAGVTVID PGSTWIDVDV TIGRDTVIRP GTQLLGRTRV
GGRCDVGPDT TLSDVTVGDG ASVVRTHGSE SLIGAGATVG PFTYLRPGTA LGAEGKLGAF
VETKNATIGA GTKVPHLTYV GDADIGEHSN IGASSVFVNY DGETKNRTTI GSHVRTGSDT
MFVAPVTVGD GAYTGAGTVI RRNVPPGALA VSAGSQRNIE GWVVRKRPGS AAARAAERAS
GEAAEQALGH HDDSQGS


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