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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)]

 A0A1Q8KIP6_9PSEU        Unreviewed;       525 AA.
A0A1Q8KIP6;
12-APR-2017, integrated into UniProtKB/TrEMBL.
12-APR-2017, sequence version 1.
20-JUN-2018, entry version 11.
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=Ae707Ps1_0656c {ECO:0000313|EMBL:OLM16398.1};
Pseudonocardia sp. Ae707_Ps1.
Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
Pseudonocardia.
NCBI_TaxID=1885572 {ECO:0000313|EMBL:OLM16398.1, ECO:0000313|Proteomes:UP000186124};
[1] {ECO:0000313|EMBL:OLM16398.1, ECO:0000313|Proteomes:UP000186124}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ae707_Ps1 {ECO:0000313|EMBL:OLM16398.1,
ECO:0000313|Proteomes:UP000186124};
Holmes N.A., Innocent T.M., Heine D., Al Bassam M., Worsley S.F.,
Trottmann F., Patrick E.H., Yu D.W., Murrell J.C., Schioett M.,
Wilkinson B., Boomsma J., Hutchings M.I.;
"Genome Analysis of Two Pseudonocardia Phylotypes Associated with
Acromyrmex Leafcutter Ants Reveals Their Biosynthetic Potential.";
Front. Microbiol. 7:1-16(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:OLM16398.1}.
-----------------------------------------------------------------------
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EMBL; MCIR01000001; OLM16398.1; -; Genomic_DNA.
UniPathway; UPA00113; UER00532.
UniPathway; UPA00113; UER00533.
UniPathway; UPA00973; -.
Proteomes; UP000186124; 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, ECO:0000313|EMBL:OLM16398.1};
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:UP000186124};
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, ECO:0000313|EMBL:OLM16398.1};
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,
ECO:0000313|EMBL:OLM16398.1}.
DOMAIN 23 162 NTP_transf_3. {ECO:0000259|Pfam:PF12804}.
REGION 1 256 Pyrophosphorylase. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 26 29 UDP-GlcNAc binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 102 103 UDP-GlcNAc binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 126 128 UDP-GlcNAc binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 257 277 Linker. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 278 525 N-acetyltransferase. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 412 413 Acetyl-CoA binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
ACT_SITE 389 389 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01631}.
METAL 128 128 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01631}.
METAL 254 254 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 40 40 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 97 97 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 165 165 UDP-GlcNAc; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01631}.
BINDING 181 181 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 196 196 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 254 254 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 359 359 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 377 377 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 392 392 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 403 403 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 406 406 Acetyl-CoA; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01631}.
BINDING 431 431 Acetyl-CoA. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 449 449 Acetyl-CoA; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01631}.
SEQUENCE 525 AA; 53717 MW; 6BAE9295E411395E CRC64;
MPDPHQGDDG GPTDPARAAV AAGVVLAAGA GSRMRSATPK VLHPLGGRPM LGHALHAVAG
VRPEHLVVVV GHQRERVAGA VTGFSGELGR EVATAVQEQM LGTGDAVRCG LTALPADLTG
TVLVTYGDVP LLDSTTLSSL VTEHERHAAA VTLLTGEPAD PTGYGRIVRD GPAGAVTAIV
EHSDAGPEQR AIGEVNSGVY AFDAEFLRAG VTGLAAHNEQ QELYLTDLVE SAVAGGRTVH
AVRCDDEWLL RGVNDRVQLA ELRAELNRRV LRGWMLAGVT VVDPATTWVD VQVELGTDVV
LHPGTQLHGA CTVGEGAEIG PDTTLTACAV GAGATVVRTH GSDSEIGEGA SVGPFAYLRP
HARLGARGKI GTFVEVKNAD IGAGSKVPHL TYVGDASIGE MSNIGASSVF VNYDGVRKQR
TTIGSHVRTG SDTMFIAPVT VGDGAYTGAG TVLRSDVPPG ALAVSGGTQR TIEGWVNRKR
PGTPAAEAAE RAGSGPAGDG TSGGVDHDAG NNSDNRDLSR GGTAR


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