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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)]

 H8E7G7_9MICO            Unreviewed;       490 AA.
H8E7G7;
16-MAY-2012, integrated into UniProtKB/TrEMBL.
16-MAY-2012, sequence version 1.
28-MAR-2018, entry version 40.
RecName: Full=Bifunctional protein GlmU {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};
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};
Name=glmU {ECO:0000256|HAMAP-Rule:MF_01631};
ORFNames=OR221_2794 {ECO:0000313|EMBL:EIC07158.1};
Microbacterium laevaniformans OR221.
Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
Microbacterium.
NCBI_TaxID=1160710 {ECO:0000313|EMBL:EIC07158.1, ECO:0000313|Proteomes:UP000004547};
[1] {ECO:0000313|EMBL:EIC07158.1, ECO:0000313|Proteomes:UP000004547}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=OR221 {ECO:0000313|EMBL:EIC07158.1,
ECO:0000313|Proteomes:UP000004547};
PubMed=22628508; DOI=10.1128/JB.00474-12;
Brown S.D., Palumbo A.V., Panikov N., Ariyawansa T., Klingeman D.M.,
Johnson C.M., Land M.L., Utturkar S.M., Epstein S.S.;
"Draft Genome Sequence for Microbacterium laevaniformans Strain OR221,
a Bacterium Tolerant to Metals, Nitrate, and Low pH.";
J. Bacteriol. 194:3279-3280(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:SAAS00650355}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + alpha-D-glucosamine 1-phosphate =
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate.
{ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00650344}.
-!- CATALYTIC ACTIVITY: UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
= diphosphate + UDP-N-acetyl-alpha-D-glucosamine.
{ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00650293}.
-!- 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:SAAS00650347}.
-!- 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:SAAS00650354}.
-!- 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:SAAS00650342}.
-!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00650301}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00650327}.
-!- SIMILARITY: In the C-terminal section; belongs to the transferase
hexapeptide repeat family. {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00650305}.
-!- SIMILARITY: In the N-terminal section; belongs to the N-
acetylglucosamine-1-phosphate uridyltransferase family.
{ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00650312}.
-!- 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:EIC07158.1}.
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EMBL; AJGR01000257; EIC07158.1; -; Genomic_DNA.
RefSeq; WP_005052460.1; NZ_AJGR01000257.1.
EnsemblBacteria; EIC07158; EIC07158; OR221_2794.
PATRIC; fig|1160710.3.peg.2327; -.
OrthoDB; POG091H02I2; -.
UniPathway; UPA00113; UER00532.
UniPathway; UPA00113; UER00533.
UniPathway; UPA00973; -.
Proteomes; UP000004547; 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; 3.
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:SAAS00650319};
Cell shape {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00650358};
Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00650295};
Complete proteome {ECO:0000313|Proteomes:UP000004547};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00650352};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00650323};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00650321};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00650297};
Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00650324};
Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00650358};
Reference proteome {ECO:0000313|Proteomes:UP000004547};
Repeat {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00650299};
Transferase {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00650319, ECO:0000256|SAAS:SAAS00650324}.
DOMAIN 12 140 NTP_transf_3. {ECO:0000259|Pfam:PF12804}.
REGION 1 239 Pyrophosphorylase. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 15 18 UDP-GlcNAc binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 87 88 UDP-GlcNAc binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 110 112 UDP-GlcNAc binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 240 260 Linker. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 261 490 N-acetyltransferase. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 395 396 Acetyl-CoA binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
ACT_SITE 372 372 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01631}.
METAL 112 112 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01631}.
METAL 237 237 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 29 29 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 82 82 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 149 149 UDP-GlcNAc; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01631}.
BINDING 164 164 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 179 179 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 237 237 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 342 342 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 360 360 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 375 375 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 386 386 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 389 389 Acetyl-CoA; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01631}.
BINDING 414 414 Acetyl-CoA. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 432 432 Acetyl-CoA; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01631}.
SEQUENCE 490 AA; 50665 MW; 4317BF09B81F78FD CRC64;
MTENTLDASL AVVILAAGQG TRMRSSLPKV LHRIGGRPLV GHVLDTARDL SPAHVLVVVR
HERDLVADAV TGISPEVVVV DQDEIPGTGR AVEVALDAVP DFVGDVLVLS GDVPLLDADT
LSTLIRDHRS SRAAITLLSA VLDDATGYGR VVRATNGGVE RIVEQKDATA AEAAISEINA
GVYVFRAELL RAQLARVGTE NAQGEKYLTD VVGLARAAGH VVTASVVSDV SLTLGVNDRA
QLAEAGRLLN ARTVRRWQLA GVTIQDPATT WIDVTATLAP DVTVLPNTHI LRASAVAAGA
TIGPDTTLED CEVGENAVVR RADATLAVIG AGASVGPFAY LRPGTVLADG GKIGTFVETK
NSTIGEGSKV PHLSYIGDTT IGRGVNLGAG AITANYDDIA KHRTEIGDEV HSGSHNVFVA
PVRIGDGAKT GAGAVIRKDV PPGALALSVA PQRNVEGWVE NHRPGTGAAE AAARSRTAQE
ADHGAQEAHG


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