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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)]
A0A1S6RPY5_STRHY Unreviewed; 466 AA.
A0A1S6RPY5;
10-MAY-2017, integrated into UniProtKB/TrEMBL.
10-MAY-2017, sequence version 1.
16-JAN-2019, entry version 14.
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=SHXM_06412 {ECO:0000313|EMBL:AQW52949.1};
Streptomyces hygroscopicus.
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces.
NCBI_TaxID=1912 {ECO:0000313|EMBL:AQW52949.1, ECO:0000313|Proteomes:UP000191078};
[1] {ECO:0000313|EMBL:AQW52949.1, ECO:0000313|Proteomes:UP000191078}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=XM201 {ECO:0000313|EMBL:AQW52949.1,
ECO:0000313|Proteomes:UP000191078};
Wang X., Bai L.;
"PKS gene overexpression with strong endogenous promoters resulted in
improved geldanamycin production.";
Submitted (DEC-2016) 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:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083685}.
-!- CATALYTIC ACTIVITY:
Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP =
diphosphate + UDP-N-acetyl-alpha-D-glucosamine;
Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776;
EC=2.7.7.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS01124206};
-!- CATALYTIC ACTIVITY:
Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+)
+ N-acetyl-alpha-D-glucosamine 1-phosphate;
Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516;
EC=2.3.1.157; Evidence={ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS01124218};
-!- 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:SAAS00083707}.
-!- 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:SAAS00381596}.
-!- 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:SAAS00381463}.
-!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00569615}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00381517}.
-!- SIMILARITY: In the C-terminal section; belongs to the transferase
hexapeptide repeat family. {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00569628}.
-!- SIMILARITY: In the N-terminal section; belongs to the N-
acetylglucosamine-1-phosphate uridyltransferase family.
{ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00569629}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01631}.
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EMBL; CP018627; AQW52949.1; -; Genomic_DNA.
UniPathway; UPA00113; UER00532.
UniPathway; UPA00113; UER00533.
UniPathway; UPA00973; -.
Proteomes; UP000191078; Chromosome.
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; IPR005835; NTP_transferase_dom.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
InterPro; IPR011004; Trimer_LpxA-like_sf.
Pfam; PF00132; Hexapep; 1.
Pfam; PF00483; NTP_transferase; 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:SAAS00083661};
Cell shape {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083721};
Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083688};
Complete proteome {ECO:0000313|Proteomes:UP000191078};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083649};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083580};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083557};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00458631};
Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083639};
Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083721};
Repeat {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083725};
Transferase {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083639, ECO:0000256|SAAS:SAAS00083661}.
DOMAIN 5 256 NTP_transferase.
{ECO:0000259|Pfam:PF00483}.
REGION 1 222 Pyrophosphorylase. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 65 66 UDP-GlcNAc binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 223 243 Linker. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 244 466 N-acetyltransferase. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 378 379 Acetyl-CoA binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
ACT_SITE 355 355 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01631}.
METAL 94 94 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01631}.
METAL 220 220 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 7 7 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 60 60 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 131 131 UDP-GlcNAc; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01631}.
BINDING 147 147 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 162 162 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 220 220 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 325 325 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 343 343 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 358 358 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 369 369 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 372 372 Acetyl-CoA; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01631}.
BINDING 415 415 Acetyl-CoA; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01631}.
BINDING 432 432 Acetyl-CoA. {ECO:0000256|HAMAP-
Rule:MF_01631}.
SEQUENCE 466 AA; 48262 MW; 2D0BC322871E934C CRC64;
MKSATPKVLH ALCGRSLVGH VVAASRELSP EHLVVVVGHA REQVSAHLAE IDAEARTAVQ
HEQNGTGHAV RMGLEELSDS GVALDGTVIV VCGDTPLLTG GTLQRLAAAH SGDGNAVTVL
TAEVPDATGY GRIVRDDASG AVTAIVEHKD ATDTQRAIRE INSGVFAFDA QLLTDALGKV
RTDNSQGEEY LTDVLGILRE AGHRVGACVA ADHREIVGIN NRVQLAEARR LLNDRLLERA
MLSGVTVVDP ATTWIDVMAT FEPDALVHPG TQLLGATHLA ANAEVGPNSR LTDTTVGAGA
VVAFTVADGA VVGAGASVGP YAYLRPGTRL GARAKAGTYV EMKNATIGEG TKVPHLSYVG
DATIGEQTNI GAASVFVNYD GVNKHHTTIG SHCRTGADNM LVAPVTIGDG AYTAAGSVIT
KDVPPGSLAV ARGQQRNIEG WVARKRPGSA AARAAEAARQ EDEGQQ
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