ID   A0A7W8NT27_9BURK        Unreviewed;       452 AA.
AC   A0A7W8NT27;
DT   02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 1.
DT   19-JAN-2022, entry version 3.
DE   RecName: Full=Bifunctional protein GlmU {ECO:0000256|HAMAP-Rule:MF_01631};
DE   Includes:
DE     RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_01631};
DE              EC=2.7.7.23 {ECO:0000256|HAMAP-Rule:MF_01631};
DE     AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase {ECO:0000256|HAMAP-Rule:MF_01631};
DE   Includes:
DE     RecName: Full=Glucosamine-1-phosphate N-acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01631};
DE              EC=2.3.1.157 {ECO:0000256|HAMAP-Rule:MF_01631};
GN   Name=glmU {ECO:0000256|HAMAP-Rule:MF_01631};
GN   ORFNames=HDC89_000236 {ECO:0000313|EMBL:MBB5390090.1};
OS   Herbaspirillum sp. SJZ102.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herbaspirillum; unclassified Herbaspirillum.
OX   NCBI_TaxID=2723070 {ECO:0000313|EMBL:MBB5390090.1, ECO:0000313|Proteomes:UP000533379};
RN   [1] {ECO:0000313|EMBL:MBB5390090.1, ECO:0000313|Proteomes:UP000533379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJZ102 {ECO:0000313|EMBL:MBB5390090.1,
RC   ECO:0000313|Proteomes:UP000533379};
RA   Izquierdo J.A.;
RT   "Plant growth-promoting bacteria from the rhizosphere of the beachgrass
RT   Ammophila breviligulata.";
RL   Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MBB5390090.1, ECO:0000313|Proteomes:UP000533379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJZ102 {ECO:0000313|EMBL:MBB5390090.1,
RC   ECO:0000313|Proteomes:UP000533379};
RA   Izquierdo J., Huntemann M., Clum A., Wang J., Palaniappan K., Ritter S.,
RA   Chen I.-M., Stamatis D., Reddy T., O'Malley R., Daum C., Pennacchio C.,
RA   Ivanova N., Kyrpides N., Woyke T.;
RL   Submitted (AUG-2020) 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|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:0000256|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:0000256|HAMAP-Rule:MF_01631};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01631};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01631};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC       {ECO:0000256|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:0000256|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:0000256|HAMAP-
CC       Rule:MF_01631}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_01631}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_01631}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC       hexapeptide repeat family. {ECO:0000256|ARBA:ARBA00007707,
CC       ECO:0000256|HAMAP-Rule:MF_01631}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the N-
CC       acetylglucosamine-1-phosphate uridyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00007947, ECO:0000256|HAMAP-Rule:MF_01631}.
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:MBB5390090.1}.
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DR   EMBL; JACHCU010000001; MBB5390090.1; -; Genomic_DNA.
DR   UniPathway; UPA00113; UER00532.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000533379; Unassembled WGS sequence.
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; IPR025877; MobA-like_NTP_Trfase.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   Pfam; PF00132; Hexapep; 2.
DR   Pfam; PF14602; Hexapep_2; 1.
DR   Pfam; PF12804; NTP_transf_3; 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|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW   Rule:MF_01631};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_01631};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_01631};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01631};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01631};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01631};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW   Rule:MF_01631};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_01631};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_01631};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_01631};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01631}.
FT   DOMAIN          4..129
FT                   /note="NTP_transf_3"
FT                   /evidence="ECO:0000259|Pfam:PF12804"
FT   REGION          1..224
FT                   /note="Pyrophosphorylase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   REGION          6..9
FT                   /note="UDP-GlcNAc binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   REGION          76..77
FT                   /note="UDP-GlcNAc binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   REGION          98..100
FT                   /note="UDP-GlcNAc binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   REGION          225..245
FT                   /note="Linker"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   REGION          246..452
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   REGION          381..382
FT                   /note="Acetyl-CoA binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   ACT_SITE        358
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   METAL           100
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   METAL           222
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         20
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         71
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         135
FT                   /note="UDP-GlcNAc; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         149
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         164
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         222
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         328
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         346
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         361
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         372
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         375
FT                   /note="Acetyl-CoA; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         400
FT                   /note="Acetyl-CoA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         418
FT                   /note="Acetyl-CoA; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         435
FT                   /note="Acetyl-CoA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
SQ   SEQUENCE   452 AA;  47290 MW;  7C9C40E708BA71B7 CRC64;
     MNIVILAAGM GKRMQSALPK VLHPLAGKPL LGHVIDTARS LSPRQLCVVY GHGGDAVPKA
     FADAGLSFAK QEPQLGTGHA VMQALPHIED DAPTLVLYGD VPLTTSASLQ RLLDAAGNDK
     LGVLTITLDD PTGYGRIVRE NGRITSIVEQ KDASQAQRAI REINTGIIAA PTARLRKWLA
     ALSNQNAQGE YYLTDIIALA VADGVEVVSA QPDDVAETLG VNSKAQLAEL ERVHQRNIAN
     RLLEQGVTLA DPARIDVRGE LTCGRDVAID VNCVFEGRVS IAEGAAIGAN CVIKNASIGA
     CANIKPFTHI EGATVGAGAQ VGPYARLRPG TELEQDVHVG NFVEVKNSIV GIGSKANHLA
     YVGDADVGSG VNIGAGVITC NYDGANKFRT VIEDDAFIGS DSQLVAPVRV GKGATLGAGT
     TLTKDAPAGQ LTLSRAKQLS LPGWQRPVKI KK
//