ID E4NWE1_HALBP Unreviewed; 390 AA.
AC E4NWE1;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Bifunctional protein GlmU {ECO:0000256|ARBA:ARBA00013414};
DE EC=2.3.1.157 {ECO:0000256|ARBA:ARBA00012225};
DE EC=2.7.7.23 {ECO:0000256|ARBA:ARBA00012457};
GN OrderedLocusNames=Hbor_36550 {ECO:0000313|EMBL:ADQ69361.1};
GN ORFNames=C499_12355 {ECO:0000313|EMBL:ELY26250.1};
OS Halogeometricum borinquense (strain ATCC 700274 / DSM 11551 / JCM 10706 /
OS KCTC 4070 / PR3).
OG Plasmid pHBOR04 {ECO:0000313|EMBL:ADQ69361.1,
OG ECO:0000313|Proteomes:UP000006663}.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halogeometricum.
OX NCBI_TaxID=469382 {ECO:0000313|EMBL:ADQ69361.1, ECO:0000313|Proteomes:UP000006663};
RN [1] {ECO:0000313|Proteomes:UP000006663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700274 / DSM 11551 / JCM 10706 / KCTC 4070 / PR3
RC {ECO:0000313|Proteomes:UP000006663};
RC PLASMID=pHBOR04 {ECO:0000313|Proteomes:UP000006663};
RX PubMed=21304651; DOI=10.4056/sigs.23264;
RA Malfatti S., Tindall B.J., Schneider S., Fahnrich R., Lapidus A.,
RA Labuttii K., Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Anderson I.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA D'haeseleer P., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Chain P.;
RT "Complete genome sequence of Halogeometricum borinquense type strain
RT (PR3).";
RL Stand. Genomic Sci. 1:150-159(2009).
RN [2] {ECO:0000313|EMBL:ADQ69361.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PR 3 {ECO:0000313|EMBL:ADQ69361.1};
RC PLASMID=pHBOR04 {ECO:0000313|EMBL:ADQ69361.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA Mikhailova N., Anderson I., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA Wu D., Tindal B., Klenk H.-P., Eisen J.A.;
RT "The complete plasmid4 of Halogeometricum borinquense DSM 11551.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ELY26250.1, ECO:0000313|Proteomes:UP000011585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11551 {ECO:0000313|EMBL:ELY26250.1,
RC ECO:0000313|Proteomes:UP000011585};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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. {ECO:0000256|ARBA:ARBA00024726}.
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:0000256|ARBA:ARBA00001851};
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:0000256|ARBA:ARBA00000731};
CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC hexapeptide repeat family. {ECO:0000256|ARBA:ARBA00007707}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the N-
CC acetylglucosamine-1-phosphate uridyltransferase family.
CC {ECO:0000256|ARBA:ARBA00007947}.
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DR EMBL; CP001694; ADQ69361.1; -; Genomic_DNA.
DR EMBL; AOHT01000040; ELY26250.1; -; Genomic_DNA.
DR RefSeq; WP_006055778.1; NZ_AOHT01000040.1.
DR AlphaFoldDB; E4NWE1; -.
DR GeneID; 9989287; -.
DR KEGG; hbo:Hbor_36550; -.
DR PATRIC; fig|469382.19.peg.2438; -.
DR HOGENOM; CLU_029499_0_1_2; -.
DR OrthoDB; 15372at2157; -.
DR Proteomes; UP000006663; Plasmid pHBOR04.
DR Proteomes; UP000011585; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd04181; NTP_transferase; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR43584:SF3; BIFUNCTIONAL PROTEIN GLMU; 1.
DR PANTHER; PTHR43584; NUCLEOTIDYL TRANSFERASE; 1.
DR Pfam; PF14602; Hexapep_2; 2.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Plasmid {ECO:0000313|EMBL:ADQ69361.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006663};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..230
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 390 AA; 40763 MW; 8853491C98D595DD CRC64;
MSAVSEAVVL AAGEGRRLRP LTKYLPKPML PVANRPVIDY VLDALVESGI ERVVVVVGYR
GDRIQTHLTA EYKGANIEFV QQPSRLGSGH ALLQATGMVN GEFLVVNGDS IINAAIVTST
LERYDSTDCA ATVAVAHSDT PEEYGVVITN RGLIADIDEH PVEREGYVVN AGVYVFDESV
FAALDRTEPW QGEIRLTDAI EHLDGPVTSI LVNGGWLDPS TPWQLLSVSE TLLGSRFGSD
VYVADSARVH ESAVVEGPVV IGKDCDVGPG AVIRPGTCLQ DNVHVGANAV VERSILSTDA
HVGAHTLLRD SVVGSGARIG DCVASPGGRA DVVVDGRLYT DRKIGSIVAD RATVGANATL
AAGSSVGAEA TVGAGVVVDG PVREKSEVAA
//
