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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)]

 U4KKG8_ACHPJ            Unreviewed;       459 AA.
U4KKG8;
11-DEC-2013, integrated into UniProtKB/TrEMBL.
11-DEC-2013, sequence version 1.
22-NOV-2017, entry version 30.
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,
ECO:0000313|EMBL:CCV64102.1};
ORFNames=BN85405250 {ECO:0000313|EMBL:CCV64102.1};
Acholeplasma palmae (strain ATCC 49389 / J233).
Bacteria; Tenericutes; Mollicutes; Acholeplasmatales;
Acholeplasmataceae; Acholeplasma.
NCBI_TaxID=1318466 {ECO:0000313|EMBL:CCV64102.1, ECO:0000313|Proteomes:UP000032740};
[1] {ECO:0000313|EMBL:CCV64102.1, ECO:0000313|Proteomes:UP000032740}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=J233 {ECO:0000313|EMBL:CCV64102.1,
ECO:0000313|Proteomes:UP000032740};
PubMed=24158107; DOI=10.1159/000354322;
Kube M., Siewert C., Migdoll A.M., Duduk B., Holz S., Rabus R.,
Seemuller E., Mitrovic J., Muller I., Buttner C., Reinhardt R.;
"Analysis of the Complete Genomes of Acholeplasma brassicae , A.
palmae and A. laidlawii and Their Comparison to the Obligate Parasites
from ' Candidatus Phytoplasma'.";
J. Mol. Microbiol. Biotechnol. 24:19-36(2013).
-!- 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}.
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EMBL; FO681347; CCV64102.1; -; Genomic_DNA.
RefSeq; WP_026657514.1; NC_022538.1.
EnsemblBacteria; CCV64102; CCV64102; BN85405250.
KEGG; apal:BN85405250; -.
KO; K04042; -.
UniPathway; UPA00113; UER00532.
UniPathway; UPA00113; UER00533.
UniPathway; UPA00973; -.
Proteomes; UP000032740; Chromosome Acholeplasma palmae.
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.
Gene3D; 3.90.550.10; -; 1.
HAMAP; MF_01631; GlmU; 1.
InterPro; IPR005882; Bifunctional_GlmU.
InterPro; IPR001451; Hexapep.
InterPro; IPR018357; Hexapep_transf_CS.
InterPro; IPR005835; NTP_transferase_dom.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
InterPro; IPR011004; Trimer_LpxA-like_sf.
Pfam; PF00132; Hexapep; 3.
Pfam; PF00483; NTP_transferase; 1.
SUPFAM; SSF51161; SSF51161; 1.
SUPFAM; SSF53448; SSF53448; 1.
TIGRFAMs; TIGR01173; glmU; 1.
PROSITE; PS00101; HEXAPEP_TRANSFERASES; 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:UP000032740};
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:CCV64102.1};
Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00650358};
Reference proteome {ECO:0000313|Proteomes:UP000032740};
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:CCV64102.1}.
DOMAIN 5 216 NTP_transferase.
{ECO:0000259|Pfam:PF00483}.
REGION 1 228 Pyrophosphorylase. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 8 11 UDP-GlcNAc binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 77 78 UDP-GlcNAc binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 229 249 Linker. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 250 459 N-acetyltransferase. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 384 385 Acetyl-CoA binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
ACT_SITE 361 361 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01631}.
METAL 102 102 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01631}.
METAL 226 226 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 22 22 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 72 72 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 139 139 UDP-GlcNAc; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01631}.
BINDING 154 154 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 169 169 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 226 226 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 331 331 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 349 349 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 364 364 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 375 375 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 421 421 Acetyl-CoA; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01631}.
BINDING 438 438 Acetyl-CoA. {ECO:0000256|HAMAP-
Rule:MF_01631}.
SEQUENCE 459 AA; 51066 MW; EE0669BF3341C9BF CRC64;
MKNYALVLAA GKGTRMKTDI PKVAFPILKK PMIEYIVENI EKSVVDETVL VLGYKREYIE
EILGNRSSYV YQEEQLGTGH AAMQATNYFK DKKGNTFIMP GDVPLIWYKD INKMFLAHEE
NGNDLTVVTA IYDNPKSYGR IVRNAQGAIQ AIVEENDCNE YQKTIKEINT GIYIVNNEKF
FPLLEKLEKN PKKGEYYITD MIALMKKDYK VGTYTVKNNS LVMGVNDLYS VSIAEKYLRE
YINKSHMLNG VSIINPETVT IGHNVVIESG VIINPNTTIT GNTVIKTGAT IGPNSELHNA
LVDENAVVRH SLVYDSHIGE GTTVGPYAHL RDHADIGTFN RVGNFVEVKN TKTGHKTKMS
HLAYVGDAEV GDRVNFGCGS VTVNYDGVNK HKTIIGSDVF IGCNVNLVAP IKVEDNVFIA
AGSTVTKDIP KGALSIARNQ QINKEDYFKN LIKPKPEKE


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