ACL_RS05125

Uniprot: A9NH16
Description: bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase
EC number: 2.7.7.23; 2.3.1.157
Annotation score: 4 out of 5
Miscellaneous [CC]:
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01631}.; CATALYTIC ACTIVITY: UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine. {ECO:0000255|HAMAP-Rule:MF_01631}.
Cofactor: COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01631}; ; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01631}
Enzyme regulation:
Function [CC]: 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:0000255|HAMAP-Rule:MF_01631}.
Pathway: 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:0000255|HAMAP-Rule:MF_01631}.; 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:0000255|HAMAP-Rule:MF_01631}.; PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01631}.
Active site: ACT_SITE 361 361 Proton acceptor. {ECO:0000255|HAMAP-Rule:MF_01631}.
Binding site: BINDING 22 22 UDP-GlcNAc. {ECO:0000255|HAMAP-Rule:MF_01631}.; BINDING 72 72 UDP-GlcNAc. {ECO:0000255|HAMAP-Rule:MF_01631}.; BINDING 139 139 UDP-GlcNAc; via amide nitrogen. {ECO:0000255|HAMAP-Rule:MF_01631}.; BINDING 154 154 UDP-GlcNAc. {ECO:0000255|HAMAP-Rule:MF_01631}.; BINDING 169 169 UDP-GlcNAc. {ECO:0000255|HAMAP-Rule:MF_01631}.; BINDING 226 226 UDP-GlcNAc. {ECO:0000255|HAMAP-Rule:MF_01631}.; BINDING 331 331 UDP-GlcNAc. {ECO:0000255|HAMAP-Rule:MF_01631}.; BINDING 349 349 UDP-GlcNAc. {ECO:0000255|HAMAP-Rule:MF_01631}.; BINDING 364 364 UDP-GlcNAc. {ECO:0000255|HAMAP-Rule:MF_01631}.; BINDING 375 375 UDP-GlcNAc. {ECO:0000255|HAMAP-Rule:MF_01631}.; BINDING 421 421 Acetyl-CoA; via amide nitrogen. {ECO:0000255|HAMAP-Rule:MF_01631}.; BINDING 438 438 Acetyl-CoA. {ECO:0000255|HAMAP-Rule:MF_01631}.
Calcium binding:
DNA binding:
Metal binding: METAL 102 102 Magnesium. {ECO:0000255|HAMAP-Rule:MF_01631}.; METAL 226 226 Magnesium. {ECO:0000255|HAMAP-Rule:MF_01631}.
Nucleotide binding:
Site:
Gene names (primary): glmU
Gene names (synonym):
Mass: 51,183
Subunit structure [CC]: SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01631}.
Gene ontology (GO): cytoplasm [GO:0005737]; glucosamine-1-phosphate N-acetyltransferase activity [GO:0019134]; magnesium ion binding [GO:0000287]; UDP-N-acetylglucosamine diphosphorylase activity [GO:0003977]; cell morphogenesis [GO:0000902]; cell wall organization [GO:0071555]; lipid A biosynthetic process [GO:0009245]; lipopolysaccharide biosynthetic process [GO:0009103]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360]; UDP-N-acetylglucosamine biosynthetic process [GO:0006048]
Gene ontology IDs: GO:0000287; GO:0000902; GO:0003977; GO:0005737; GO:0006048; GO:0008360; GO:0009103; GO:0009245; GO:0009252; GO:0019134; GO:0071555
Chain: CHAIN 1 460 Bifunctional protein GlmU. /FTId=PRO_1000088122.
Signal peptide:
Domain [CC]:
Sequence similarities: SIMILARITY: In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01631}.; SIMILARITY: In the C-terminal section; belongs to the transferase hexapeptide repeat family. {ECO:0000255|HAMAP-Rule:MF_01631}.
Protein families: N-acetylglucosamine-1-phosphate uridyltransferase family; Transferase hexapeptide repeat family
Coiled coil:
Domain [FT]:
Motif:
Region: REGION 1 228 Pyrophosphorylase. {ECO:0000255|HAMAP-Rule:MF_01631}.; REGION 8 11 UDP-GlcNAc binding. {ECO:0000255|HAMAP-Rule:MF_01631}.; REGION 77 78 UDP-GlcNAc binding. {ECO:0000255|HAMAP-Rule:MF_01631}.; REGION 229 249 Linker. {ECO:0000255|HAMAP-Rule:MF_01631}.; REGION 250 460 N-acetyltransferase. {ECO:0000255|HAMAP-Rule:MF_01631}.; REGION 384 385 Acetyl-CoA binding. {ECO:0000255|HAMAP-Rule:MF_01631}.
EMBL: CP000896
ProteinModelPortal: A9NH16
MEROPS:
EnsemblBacteria KO: ABX81646
UniPathway: K04042
CDD:
Gene3D:
HAMAP: 3.90.550.10
InterPro: MF_01631
PANTHER: IPR005882;IPR001451;IPR018357;IPR005835;IPR029044;IPR011004
PIRSF:
PRINTS:
PROSITE:
Pfam: PS00101
ProDom: PF00132;PF00483
SMART:
SUPFAM:
TIGRFAMs: SSF51161;SSF53448

1063764-1065147(-)

>nucleotide sequence
CTATTCTTCTTTTTTAGGTTTTGGACTAATCAAGTATTTTGAGTAGTCTTCTTTAGTCAC
TTGACGGCTTCTTGCAATAGCAAACCCGTTATCAGGAATGTCCTTAGTCACTGTTGAACC
TGCTGCAATAAAGACATTGTCTCCAATTTTTATTGGTGCAATAAGGTTTGTATTGCATCC
AATAAAGACATTGTCTCCTATTTCAGTTTTATGTTTTAACTTTCCGTCGTAGTTCACTGT
AACAGAACCACAACCAAAGTTAACAGATTCACCAACAACTGAATCACCAATGTAAGCTAG
GTGGCTTGCTTTTGTGTTGTGTCCTGTACTAGATTTTTTAACCTCTACGAAGTTACCAAT
TCTATTATGTGTACCAATATCAGCATGATCTCTTAAATGAGCAAATGGACCAACTGTTGT
TCCTTCTCTAACGATACTATCATAAACAAGACTGTGTCTGACTACTACATGACTATCAAT
TCGTGAGTTATGTATTTCTGTATTAGGTCCTACAATTGCCCCTGCTTTAATTACTGTGTC
CCCAGTAATTGTAGTATTGGGGTTAATTGTAACACCTGGTTCAATTATGACGTTATGTCC
AATTGTAATGGTTTCTGGGTTAATCATTGATACCCCATTTAGCATATGATCTTTATTAAT
ATATTCTCTTAAATACTTCTCAGCTTTGCTGATTGCATATAAGTCATTTACACCCATAGC
TAAAGAGTTATTTTTGATCATATATGAACCTATCTTATAATCTTTTTTCATTAACTCTAC
CATATCTGTGATATAGTACTCACCTTTAGCGTTGTTGTTATTCAAGTTTTTTAATAAAGA
AAAGAACTTTTTATTATTAACAATGTATATACCAGTATTGACTTCTTTAATTTCTTTTTC
AAAGTCGTTAGCATCTTTTTCTTCAACAATACGTTGAATGACACCTTGTTCATTACGTAC
AATACGTCCATAACCTTCTGGATCTTCATAATGAGCTGTAACGATTGTAAAATCATTACC
ATTGTCTTCATGAACAGCAAACATTCTATCAATAGATTTATACCAGATGAGTGGCACATC
ACCAGGCATAATAAACGTATTACCATCTAGTTTAGATAATACTGGTGCAGCCATCATGGC
TGCATGACCAGTACCTAGTTGTTCTTCTTGATAGACATACTTAGCACGGTCTTTAACAAT
ACCTTCTACAACTTCTCTTTTATATCCTAATACAAGGTAGATTTCTTCTACACTTGATTT
TTCAATATTTTCTACAATATACTCAATCATTGGTTTTCTTAGTATTGGAAAAGCAACTTT
AGGTATATCTGATTTCATACGAGTGCCTTTACCAGCTGCAAGTACTAATGCATAATTTTT
CAT

>protein sequence
MKNYALVLAAGKGTRMKSDIPKVAFPILRKPMIEYIVENIEKSSVEEIYLVLGYKREVVE
GIVKDRAKYVYQEEQLGTGHAAMMAAPVLSKLDGNTFIMPGDVPLIWYKSIDRMFAVHED
NGNDFTIVTAHYEDPEGYGRIVRNEQGVIQRIVEEKDANDFEKEIKEVNTGIYIVNNKKF
FSLLKNLNNNNAKGEYYITDMVELMKKDYKIGSYMIKNNSLAMGVNDLYAISKAEKYLRE
YINKDHMLNGVSMINPETITIGHNVIIEPGVTINPNTTITGDTVIKAGAIVGPNTEIHNS
RIDSHVVVRHSLVYDSIVREGTTVGPFAHLRDHADIGTHNRIGNFVEVKKSSTGHNTKAS
HLAYIGDSVVGESVNFGCGSVTVNYDGKLKHKTEIGDNVFIGCNTNLIAPIKIGDNVFIA
AGSTVTKDIPDNGFAIARSRQVTKEDYSKYLISPKPKKEE