GLMU_RHIWR
ID GLMU_RHIWR Reviewed; 452 AA.
AC A5VF26;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Bifunctional protein GlmU {ECO:0000255|HAMAP-Rule:MF_01631};
DE Includes:
DE RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01631};
DE EC=2.7.7.23 {ECO:0000255|HAMAP-Rule:MF_01631};
DE AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase {ECO:0000255|HAMAP-Rule:MF_01631};
DE Includes:
DE RecName: Full=Glucosamine-1-phosphate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01631};
DE EC=2.3.1.157 {ECO:0000255|HAMAP-Rule:MF_01631};
GN Name=glmU {ECO:0000255|HAMAP-Rule:MF_01631}; OrderedLocusNames=Swit_4554;
OS Rhizorhabdus wittichii (strain DSM 6014 / CCUG 31198 / JCM 15750 / NBRC
OS 105917 / EY 4224 / RW1) (Sphingomonas wittichii).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Rhizorhabdus.
OX NCBI_TaxID=392499;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6014 / CCUG 31198 / JCM 15750 / NBRC 105917 / EY 4224 / RW1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Halden R.U., Miller T.R., Salzberg S.L., Eisen J.A.,
RA Richardson P.;
RT "Complete sequence of chromosome of Sphingomonas wittichii RW1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the last two sequential reactions in the de novo
CC biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-
CC terminal domain catalyzes the transfer of acetyl group from acetyl
CC coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-
CC acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into
CC UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-
CC triphosphate), a reaction catalyzed by the N-terminal domain.
CC {ECO:0000255|HAMAP-Rule:MF_01631}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-
CC acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01631};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP =
CC diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01631};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01631};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01631};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from
CC alpha-D-glucosamine 6-phosphate (route II): step 2/2.
CC {ECO:0000255|HAMAP-Rule:MF_01631}.
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-
CC acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01631}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01631}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01631}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01631}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the N-
CC acetylglucosamine-1-phosphate uridyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_01631}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC hexapeptide repeat family. {ECO:0000255|HAMAP-Rule:MF_01631}.
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DR EMBL; CP000699; ABQ70892.1; -; Genomic_DNA.
DR RefSeq; WP_012050728.1; NC_009511.1.
DR AlphaFoldDB; A5VF26; -.
DR SMR; A5VF26; -.
DR STRING; 392499.Swit_4554; -.
DR EnsemblBacteria; ABQ70892; ABQ70892; Swit_4554.
DR KEGG; swi:Swit_4554; -.
DR eggNOG; COG1207; Bacteria.
DR HOGENOM; CLU_029499_15_2_5; -.
DR OMA; TAIVEHK; -.
DR OrthoDB; 1381953at2; -.
DR UniPathway; UPA00113; UER00532.
DR UniPathway; UPA00113; UER00533.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000001989; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000902; P:cell morphogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03353; LbH_GlmU_C; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR HAMAP; MF_01631; GlmU; 1.
DR InterPro; IPR005882; Bifunctional_GlmU.
DR InterPro; IPR038009; GlmU_C_LbH.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR025877; MobA-like_NTP_Trfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF00132; Hexapep; 3.
DR Pfam; PF12804; NTP_transf_3; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR01173; glmU; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cell shape; Cell wall biogenesis/degradation; Cytoplasm;
KW Magnesium; Metal-binding; Multifunctional enzyme; Nucleotidyltransferase;
KW Peptidoglycan synthesis; Reference proteome; Repeat; Transferase.
FT CHAIN 1..452
FT /note="Bifunctional protein GlmU"
FT /id="PRO_1000056203"
FT REGION 1..233
FT /note="Pyrophosphorylase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT REGION 234..254
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT REGION 255..452
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT ACT_SITE 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 11..14
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 25
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 76
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 81..82
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 104..106
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 106
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 144
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 159
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 174
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 231
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 320
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 338
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 353
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 364
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 367
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 373..374
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 392
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 410
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 427
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
SQ SEQUENCE 452 AA; 47727 MW; 1A2936175EBB836C CRC64;
MTDRPFAALI LAAGKGTRMK SDLHKVLHPI AGKPMLGHLI AAVDRLGAAR KLVVTGAGRE
QVEAFVAPLG VEVATQEPQL GTAHAVQQGE AALADFDGDV LILYGDVPLV PAETIRRMLD
RLQGEDAPVA VVLGFRPDDA LAYGRILARG DGAIDDMVEY KDATTEQRAI DLCNSGLMAV
RGRDLWRLLA QVGNDNAAGE YYLPDIVRIA RAEGGRSVVV EAEAWEVAGV NSRAELAAVE
AEWQRRRRLA AMADGATLIA PETVWFSHDT MVGRDVVIEP HVVFGPGVTI EDGVAIHGFS
HVEGATVRTG AEIGPYARLR PGADIGEGAK IGNFVEVKNG RFGKGAKANH LSYIGDADVG
AKANIGAGTI TCNYDGFLKY RTVIGEGAFI GSNSALVAPV TIGDGAIVGA GSTVTRDVEA
DALAVARGKQ ESRTGWAARF REAMKIKKAA RK
