ID   A0A5P5ZH93_9LACO        Unreviewed;       461 AA.
AC   A0A5P5ZH93;
DT   22-APR-2020, integrated into UniProtKB/TrEMBL.
DT   22-APR-2020, sequence version 1.
DT   17-JUN-2020, entry version 2.
DE   RecName: Full=Bifunctional protein GlmU {ECO:0000256|SAAS:SAAS00083647};
GN   Name=glmU {ECO:0000313|EMBL:QFG50779.1};
GN   ORFNames=LA749_01510 {ECO:0000313|EMBL:QFG50779.1};
OS   Lactobacillus acetotolerans.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1600 {ECO:0000313|EMBL:QFG50779.1, ECO:0000313|Proteomes:UP000325393};
RN   [1] {ECO:0000313|EMBL:QFG50779.1, ECO:0000313|Proteomes:UP000325393}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LA749 {ECO:0000313|EMBL:QFG50779.1,
RC   ECO:0000313|Proteomes:UP000325393};
RA   Kim K.;
RT   "Genome sequencing of Lactobacillus acetotolerans.";
RL   Submitted (SEP-2019) 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:0000256|SAAS:SAAS00381483}.
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|SAAS:SAAS01124206};
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|SAAS:SAAS01124218};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00611499};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC       {ECO:0000256|SAAS:SAAS00083707}.
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|SAAS:SAAS00083565}.
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|SAAS:SAAS00083673}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|SAAS:SAAS00569615}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00083712}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC       hexapeptide repeat family. {ECO:0000256|SAAS:SAAS00569628}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the N-
CC       acetylglucosamine-1-phosphate uridyltransferase family.
CC       {ECO:0000256|SAAS:SAAS00569629}.
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DR   EMBL; CP044496; QFG50779.1; -; Genomic_DNA.
DR   RefSeq; WP_056970803.1; NZ_CP044496.1.
DR   UniPathway; UPA00113; UER00532.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000325393; Chromosome.
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   CDD; cd03353; LbH_GlmU_C; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR005882; Bifunctional_GlmU.
DR   InterPro; IPR038009; GlmU_C_LbH.
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; 3.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR01173; glmU; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|SAAS:SAAS00458646,
KW   ECO:0000313|EMBL:QFG50779.1}; Cell shape {ECO:0000256|SAAS:SAAS00083584};
KW   Cell wall biogenesis/degradation {ECO:0000256|SAAS:SAAS00458644};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00458650};
KW   Magnesium {ECO:0000256|SAAS:SAAS00458735};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00458606};
KW   Multifunctional enzyme {ECO:0000256|SAAS:SAAS00083642};
KW   Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00458661,
KW   ECO:0000313|EMBL:QFG50779.1};
KW   Peptidoglycan synthesis {ECO:0000256|SAAS:SAAS00458685};
KW   Repeat {ECO:0000256|SAAS:SAAS00458660};
KW   Transferase {ECO:0000256|SAAS:SAAS00458747, ECO:0000313|EMBL:QFG50779.1}.
FT   DOMAIN          6..219
FT                   /note="NTP_transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   461 AA;  50176 MW;  B726C0D440FA255C CRC64;
     MKKFVVILAA GKGTRMKSKL YKVLHKVCGK TMVEHVVDAA QGVKPDKIIT VVGSGAGKVE
     KVLSGKSEFA FQEKQLGTGD AVLTTKDILG DKDGATLVIT GDTPLFTTET FQNLFAYHAK
     KGNAATVLTA EAPDPYGYGR IIRDEQGNVL RIVEQKDGKP EELEIKEINT GVFCFDNKKL
     FEALKHVDND NAQGEYYLTD VLEILRNKGE RVGAYKMPDF SESLGVNDRI ALAQATKIMQ
     KRINRNHMCD GVSFVDPTTA YIDSDVKIGN DTVIEGNVVI EGNTEIGSDC HITSGSRIVD
     SKIGNNVTIT SSTLQEAEMD DDTDIGPNSH LRPNAVIRKG AHVGNFVEIK NSEIGENTKV
     GHLTYVGDAT LGKDINVGCG TIFSNYDGVK KFHTNVGDHS FVGAGVTLIA PINVADHSFI
     AADSTITKNV GKYDMAIARG RQTNKPDYWH KLPLSHDKDW Q
//