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Database: UniProt
Entry: A0A0P6XEH4_9SPHN
LinkDB: A0A0P6XEH4_9SPHN
Original site: A0A0P6XEH4_9SPHN 
ID   A0A0P6XEH4_9SPHN        Unreviewed;       454 AA.
AC   A0A0P6XEH4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 39.
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   ECO:0000313|EMBL:KPL66983.1};
GN   ORFNames=SZ64_02065 {ECO:0000313|EMBL:KPL66983.1};
OS   Erythrobacter sp. SG61-1L.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=1603897 {ECO:0000313|EMBL:KPL66983.1, ECO:0000313|Proteomes:UP000049978};
RN   [1] {ECO:0000313|EMBL:KPL66983.1, ECO:0000313|Proteomes:UP000049978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG61-1L {ECO:0000313|EMBL:KPL66983.1,
RC   ECO:0000313|Proteomes:UP000049978};
RA   Palumuru S., Dellas N., Pearce S.L., Warden A.C., Oakeshott J.G.,
RA   Pandey G.;
RT   "Phylogenetic and kinetic characterization of a suite of dehydrogenases
RT   from a newly isolated bacterium, strain SG51-1L, that catalyze the turnover
RT   of guaiacylglycerol-beta-guaiacyl ether stereoisomers.";
RL   Appl. Environ. Microbiol. 0:0-0(2015).
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|ARBA:ARBA00001851, ECO:0000256|HAMAP-
CC         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|ARBA:ARBA00000731, ECO:0000256|HAMAP-
CC         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:KPL66983.1}.
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DR   EMBL; JXQC01000003; KPL66983.1; -; Genomic_DNA.
DR   RefSeq; WP_054532048.1; NZ_JXQC01000003.1.
DR   AlphaFoldDB; A0A0P6XEH4; -.
DR   STRING; 1603897.SZ64_02065; -.
DR   PATRIC; fig|1603897.4.peg.299; -.
DR   OrthoDB; 9775031at2; -.
DR   UniPathway; UPA00113; UER00532.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000049978; 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; cd02540; GT2_GlmU_N_bac; 1.
DR   CDD; cd03353; LbH_GlmU_C; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   HAMAP; MF_01631; GlmU; 1.
DR   InterPro; IPR005882; Bifunctional_GlmU.
DR   InterPro; IPR038009; GlmU_C_LbH.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR018357; Hexapep_transf_CS.
DR   InterPro; IPR025877; MobA-like_NTP_Trfase.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   NCBIfam; TIGR01173; glmU; 1.
DR   PANTHER; PTHR43584:SF3; BIFUNCTIONAL PROTEIN GLMU; 1.
DR   PANTHER; PTHR43584; NUCLEOTIDYL TRANSFERASE; 1.
DR   Pfam; PF00132; Hexapep; 1.
DR   Pfam; PF12804; NTP_transf_3; 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, 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}; Reference proteome {ECO:0000313|Proteomes:UP000049978};
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          10..145
FT                   /note="MobA-like NTP transferase"
FT                   /evidence="ECO:0000259|Pfam:PF12804"
FT   REGION          1..234
FT                   /note="Pyrophosphorylase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   REGION          235..255
FT                   /note="Linker"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   REGION          256..454
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   ACT_SITE        351
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         13..16
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         27
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         77
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         82..83
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         105..107
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         107
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         145
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         159
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         174
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         232
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         232
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         321
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         339
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         354
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         365
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         368
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         374..375
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         393
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         411
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         428
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
SQ   SEQUENCE   454 AA;  48054 MW;  944B1C9C9DD2AFEC CRC64;
     MSDAKRPIAA IVLAAGKGTR MKSDIHKVLH PVAGRPMIEH LLASLAELAP ERTVVIVGDL
     RDQLKDALGG RVEMAVQDPQ LGTGHAVQQA EGALGGFAGD VLILYGDVPF VRPETMCAMA
     ERLNEGDAPA VVVLGFEPAD PLQYGRVIAE GGSISKMVEF KDASEAERAV RLCNSGLMAV
     RGEELFGLLH RVKNDNAQRE YYLPDIVNLA LADGRPCAVV VAEDADEVAG INSRAELAEA
     EARWQKRRRA QAMADGATLT APDTVFFSWD TQLGRDVLVG PNVIFGPGVS VADKARIRAF
     SHLEGATLAS GTEVGPYARL RPGAKVEEGA KVGNFVEMKN AVLGPGAKAN HLTYLGDAEV
     GAGANIGAGT ITCNYDGYFK YKTVIGPRAF IGSNSALIAP VKIGADAIVA AGSAVTRDVA
     EGELRMVRAE QLVKPGWADQ FHDAMKKKKA EKAK
//
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