GENTAUR Molecular Products.

 A0A1S6RPY5_STRHY        Unreviewed;       466 AA.
 A0A1S6RPY5;
 10-MAY-2017, integrated into UniProtKB/TrEMBL.
 10-MAY-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=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: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; 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: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:UP000191078};
 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        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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