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

 A0A1Q7D3R4_9ACTN        Unreviewed;       417 AA.
A0A1Q7D3R4;
12-APR-2017, integrated into UniProtKB/TrEMBL.
12-APR-2017, sequence version 1.
20-JUN-2018, entry version 12.
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=AUI15_17070 {ECO:0000313|EMBL:OLB94513.1};
Actinobacteria bacterium 13_2_20CM_2_66_6.
Bacteria; Actinobacteria.
NCBI_TaxID=1803492 {ECO:0000313|EMBL:OLB94513.1};
[1] {ECO:0000313|EMBL:OLB94513.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=27843720;
Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C.,
Singh A., Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G.,
Northen T., Pan C., Banfield J.F.;
"Proteogenomic analyses indicate bacterial methylotrophy and archaeal
heterotrophy are prevalent below the grass root zone.";
PeerJ 4:E2687-E2687(2016).
-!- 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:OLB94513.1}.
-----------------------------------------------------------------------
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EMBL; MNDY01000235; OLB94513.1; -; Genomic_DNA.
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-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: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};
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};
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 3 118 NTP_transf_3. {ECO:0000259|Pfam:PF12804}.
REGION 1 208 Pyrophosphorylase. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 62 63 UDP-GlcNAc binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 209 229 Linker. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 230 417 N-acetyltransferase. {ECO:0000256|HAMAP-
Rule:MF_01631}.
ACT_SITE 325 325 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01631}.
METAL 86 86 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01631}.
METAL 206 206 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 7 7 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 57 57 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 122 122 UDP-GlcNAc; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01631}.
BINDING 137 137 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 152 152 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 206 206 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 295 295 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 328 328 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 339 339 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 342 342 Acetyl-CoA; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01631}.
BINDING 385 385 Acetyl-CoA; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01631}.
SEQUENCE 417 AA; 44501 MW; 84E201C8C775BFD1 CRC64;
MRSRTPKVLH PICGRPMVDW VVDAVAGAGA TAIKAVVSSH HAEVAAHLDS RAQVIYQREP
LGTGDAVKQV PAEQFQQGDV LVVNGDSPLL TADSIRAVVE EHRRTGAQAT IATVDDPRRD
DGRVIRNPDG TFRQIVERND VTEEQRASHE FNVGVYCFQG TPLADALGKL TNENRSGEFY
LPDVLSNLKP ITIVKIADPD EALGINDRAT LAIAVAAMRE RILRRHMLAG VTITDPASTF
IDATVQIGED TVIEPFTFIK GQSVIGEGCR IGPHAHIEDA RVGDRSDCGP FVKIRAGTDV
AEDVHIGSFA ELVRTRVGRG SKVPHMSYLG DTAIGEDANV GAGTITANFN GEVKNRTQIG
DRAFVGVDTM LVAPVKLGKG SRTGAGSVVT KDVPDGATAV GVPARVLRKK AVNSDHK


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