ID B9AGC9_METSM Unreviewed; 428 AA.
AC B9AGC9;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 43.
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 ORFNames=METSMIALI_01432 {ECO:0000313|EMBL:EEE42519.1};
OS Methanobrevibacter smithii DSM 2375.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=483214 {ECO:0000313|EMBL:EEE42519.1, ECO:0000313|Proteomes:UP000003489};
RN [1] {ECO:0000313|EMBL:EEE42519.1, ECO:0000313|Proteomes:UP000003489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2375 {ECO:0000313|EMBL:EEE42519.1,
RC ECO:0000313|Proteomes:UP000003489};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEE42519.1, ECO:0000313|Proteomes:UP000003489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2375 {ECO:0000313|EMBL:EEE42519.1,
RC ECO:0000313|Proteomes:UP000003489};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Methanobrevibacter smithii (DSM 2375).";
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:0000256|ARBA:ARBA00005166}.
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 {ECO:0000256|ARBA:ARBA00005208}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEE42519.1}.
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DR EMBL; ABYW01000012; EEE42519.1; -; Genomic_DNA.
DR RefSeq; WP_004032414.1; NZ_DS996911.1.
DR AlphaFoldDB; B9AGC9; -.
DR GeneID; 71696323; -.
DR PATRIC; fig|483214.13.peg.1377; -.
DR HOGENOM; CLU_029499_0_1_2; -.
DR OrthoDB; 15372at2157; -.
DR UniPathway; UPA00113; UER00532.
DR Proteomes; UP000003489; Unassembled WGS sequence.
DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05636; LbH_G1P_TT_C_like; 1.
DR CDD; cd04181; NTP_transferase; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 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 NCBIfam; TIGR03992; Arch_glmU; 1.
DR PANTHER; PTHR43584:SF3; BIFUNCTIONAL PROTEIN GLMU; 1.
DR PANTHER; PTHR43584; NUCLEOTIDYL TRANSFERASE; 1.
DR Pfam; PF00132; Hexapep; 2.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEE42519.1}.
FT DOMAIN 4..237
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 428 AA; 47254 MW; CD20A07AD49DD9EC CRC64;
MKLKAIILSA GEGSRMRPLT LTKPKTMLPV AGKPIIQYNI ESLRDNGITD ILLIVRYKEE
IVRNYFGDGS DFGVNISYKT QKDFLGTANA ISYGEDFIDD SIIVLNGDII LDDEIIHEII
KKYNYLSPDT LMLLTEVEDP SAFGVVEIEN GNIKNIVEKP KREEAPSNLV NAGIYIFNKD
IFDKIRETEI SERGEYEITD SVSLQIEDNK TVIGHKTSKD WIDVGRPWEL IEVNEELIGK
LKTEIKGTVE AGAVIHGEVF LDEGSVIKAG VYIEGNVYIG KNCDIGPNSY IRGNTYFGDN
VHVGNAVEIK NSIIMENTNV SHLSYVGDSV IGSNCNIAAG TNIANLRFDN ATIKTKIKNQ
KIDSGRRKLG AIIGDSVKTG INSSFSPGVK VGHNSTIGSG VLLYEDLPSD TRVLEKQTHI
IQKKKKKN
//
