GLMU_METJA
ID GLMU_METJA Reviewed; 408 AA.
AC Q58501;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Bifunctional protein GlmU;
DE Includes:
DE RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase;
DE EC=2.7.7.23;
DE AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase;
DE Includes:
DE RecName: Full=Glucosamine-1-phosphate N-acetyltransferase;
DE EC=2.3.1.157;
GN Name=glmU; OrderedLocusNames=MJ1101;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION AS AN URIDYLYLTRANSFERASE.
RX PubMed=17014089; DOI=10.1021/bi061018a;
RA White R.H., Xu H.;
RT "Methylglyoxal is an intermediate in the biosynthesis of 6-deoxy-5-
RT ketofructose-1-phosphate: a precursor for aromatic amino acid biosynthesis
RT in Methanocaldococcus jannaschii.";
RL Biochemistry 45:12366-12379(2006).
RN [3]
RP FUNCTION AS A PYROPHOSPHORYLASE AND ACETYLTRANSFERASE, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=900;
RX PubMed=18263721; DOI=10.1128/jb.01970-07;
RA Namboori S.C., Graham D.E.;
RT "Acetamido sugar biosynthesis in the Euryarchaea.";
RL J. Bacteriol. 190:2987-2996(2008).
CC -!- FUNCTION: Catalyzes the last two sequential reactions in the de novo
CC biosynthetic pathway for UDP-N-acetyl-glucosamine (UDP-GlcNAc).
CC Responsible for the acetylation of GlcN-1-P to GlcNAc-1-P, and for the
CC uridyl transfer from UTP to GlcNAc-1-P, to produce UDP-GlcNAc and
CC pyrophosphate. Also catalyzes the reverse reaction, i.e. the cleavage
CC of UDP-GlcNAc with pyrophosphate to form UTP and GlcNAc-1-P. To a
CC lesser extent, is also able to use dUTP or dTTP as the nucleotide
CC substrate, but not CTP, ATP or GTP. {ECO:0000269|PubMed:17014089,
CC ECO:0000269|PubMed:18263721}.
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:0000269|PubMed:18263721};
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:0000269|PubMed:18263721};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:18263721};
CC Temperature dependence:
CC Optimum temperature is 50-60 degrees Celsius. Activity is 22% lower
CC at 60 degrees Celsius and 60% lower at 100 degrees. Thermostable.
CC {ECO:0000269|PubMed:18263721};
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 -!- 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.
CC -!- SIMILARITY: In the N-terminal section; belongs to the N-
CC acetylglucosamine-1-phosphate uridyltransferase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC hexapeptide repeat family. {ECO:0000305}.
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DR EMBL; L77117; AAB99104.1; -; Genomic_DNA.
DR PIR; D64437; D64437.
DR RefSeq; WP_010870613.1; NC_000909.1.
DR AlphaFoldDB; Q58501; -.
DR SMR; Q58501; -.
DR STRING; 243232.MJ_1101; -.
DR EnsemblBacteria; AAB99104; AAB99104; MJ_1101.
DR GeneID; 1451998; -.
DR KEGG; mja:MJ_1101; -.
DR eggNOG; arCOG00666; Archaea.
DR HOGENOM; CLU_029499_0_1_2; -.
DR InParanoid; Q58501; -.
DR OMA; TAIVEHK; -.
DR OrthoDB; 61185at2157; -.
DR PhylomeDB; Q58501; -.
DR UniPathway; UPA00113; UER00532.
DR UniPathway; UPA00113; UER00533.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IDA:UniProtKB.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR023915; Bifunctiontional_GlmU_arc-type.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF00132; Hexapep; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR03992; Arch_glmU; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Multifunctional enzyme; Nucleotidyltransferase;
KW Reference proteome; Repeat; Transferase.
FT CHAIN 1..408
FT /note="Bifunctional protein GlmU"
FT /id="PRO_0000068761"
FT REGION 1..202
FT /note="Pyrophosphorylase"
FT REGION 203..222
FT /note="Linker"
FT REGION 223..408
FT /note="N-acetyltransferase"
FT ACT_SITE 306
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 6..9
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="N-acetyl-alpha-D-glucosamine 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57776"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="N-acetyl-alpha-D-glucosamine 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57776"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="N-acetyl-alpha-D-glucosamine 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57776"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="N-acetyl-alpha-D-glucosamine 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57776"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 399
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
SQ SEQUENCE 408 AA; 46056 MW; 03280F372CCD299A CRC64;
MDAIILCAGK GERLRPLTEN RPKPMIPIAG KPILQHIIEK VEDLVDNIYL IVKYKKEKIV
DYFKNHPKIK FLEQGEIDGT GQAVLTAKDY VDDEFLVING DIIFEDDLEE FLKYKYAVAV
KEVKNPENFG VVVLDDENNI IELQEKPENP KSNLINAGIY KFDKKIFELI EKTKISERGE
RELTDAIKHL IKEEKVKGIK LNGYWNDVGR PWDILEANKY LLDKINTDIK GKIEENVVIK
GEVIIEEGAI VKANSVIEGP AIIKKGAVVG PLAYIRPYTV LMENTFVGNS SEVKASIIMK
NTKIPHLSYV GDSIIGENCN FGCNTITANL RFDDKPVKVN IKSKRVESVR KLGVIMGDNV
KTGIQVSFMP GVKVGSNCWI GASCLIDRDI ESNTFVYKRD ELIFRKLK
