(data stored in SCRATCH zone)

SWISSPROT: D6XV45_BACIE

ID   D6XV45_BACIE            Unreviewed;       452 AA.
AC   D6XV45;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 69.
DE   RecName: Full=Bifunctional protein GlmU {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};
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};
GN   Name=glmU {ECO:0000256|HAMAP-Rule:MF_01631};
GN   OrderedLocusNames=Bsel_0052 {ECO:0000313|EMBL:ADH97603.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97603.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97603.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the last two sequential reactions in the de
CC       novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-
CC       GlcNAc). The C-terminal domain catalyzes the transfer of acetyl
CC       group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P)
CC       to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is
CC       converted into UDP-GlcNAc by the transfer of uridine 5-
CC       monophosphate (from uridine 5-triphosphate), a reaction catalyzed
CC       by the N-terminal domain. {ECO:0000256|HAMAP-Rule:MF_01631,
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;
CC         Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776;
CC         EC=2.7.7.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01631,
CC         ECO:0000256|SAAS:SAAS01124206};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+)
CC         + N-acetyl-alpha-D-glucosamine 1-phosphate;
CC         Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516;
CC         EC=2.3.1.157; Evidence={ECO:0000256|HAMAP-Rule:MF_01631,
CC         ECO:0000256|SAAS:SAAS01124218};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01631};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01631};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01631,
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
CC       from alpha-D-glucosamine 6-phosphate (route II): step 2/2.
CC       {ECO:0000256|HAMAP-Rule:MF_01631, 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|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00083673}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_01631,
CC       ECO:0000256|SAAS:SAAS00569615}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631,
CC       ECO:0000256|SAAS:SAAS00083712}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC       hexapeptide repeat family. {ECO:0000256|HAMAP-Rule:MF_01631,
CC       ECO:0000256|SAAS:SAAS00569628}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the N-
CC       acetylglucosamine-1-phosphate uridyltransferase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00569629}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01631}.
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DR   EMBL; CP001791; ADH97603.1; -; Genomic_DNA.
DR   RefSeq; WP_013171033.1; NC_014219.1.
DR   STRING; 439292.Bsel_0052; -.
DR   EnsemblBacteria; ADH97603; ADH97603; Bsel_0052.
DR   KEGG; bse:Bsel_0052; -.
DR   eggNOG; ENOG4105CAJ; Bacteria.
DR   eggNOG; COG1207; LUCA.
DR   HOGENOM; HOG000283476; -.
DR   KO; K04042; -.
DR   OMA; IEPQTHL; -.
DR   OrthoDB; 1381953at2; -.
DR   BioCyc; BSEL439292:G1GLR-59-MONOMER; -.
DR   UniPathway; UPA00113; UER00532.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000271; Chromosome.
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:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro.
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; 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   Pfam; PF00132; Hexapep; 3.
DR   Pfam; PF12804; NTP_transf_3; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR01173; glmU; 1.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6XV45.
DR   SWISS-2DPAGE; D6XV45.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00458646};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00083584};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00458644};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00458650};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00458735};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00458606};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00083642};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00458661};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00458685};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00458660};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00458747}.
FT   DOMAIN        6    144       NTP_transf_3. {ECO:0000259|Pfam:PF12804}.
FT   REGION        1    230       Pyrophosphorylase. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION        9     12       UDP-GlcNAc binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION       78     79       UDP-GlcNAc binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION      101    103       UDP-GlcNAc binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION      231    251       Linker. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   REGION      252    452       N-acetyltransferase. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION      386    387       Acetyl-CoA binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   ACT_SITE    363    363       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   METAL       103    103       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   METAL       228    228       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING      23     23       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING      73     73       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     140    140       UDP-GlcNAc; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01631}.
FT   BINDING     155    155       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     170    170       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     228    228       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     333    333       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     351    351       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     366    366       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     377    377       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     423    423       Acetyl-CoA; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01631}.
FT   BINDING     440    440       Acetyl-CoA. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
SQ   SEQUENCE   452 AA;  48359 MW;  4B545ABDDC509500 CRC64;
     MKNRYAVVLA AGKGTRMKSS LYKVLHPVCG KPMVQHIVDQ LTACEVDDIV TIVGHGADKV
     KDQLGERTSY ALQAEQLGTG HAVMQAESVL GGKDGTTLVV SGDTPLLTAE TLTELMKHHE
     ETGAKATILT AVAEDPTGYG RVLRNDGDQV ERIVEHKDAT YKERRVKEIN TGTYVFDNTA
     LFDALANVGN DNVQGEYYLP DVIEILQTRG ETVSAHIAPD FNETMGVNDR VALSEAEKWM
     KRRINRHWMT QGVSMTDPEQ TYISSDAVIG ADTVIEPGSM IKGNVTIGQG CVIGPHTVIE
     ESAVADNSVI RQSTVNRSRV GSGVAIGPFA HLRPETTLGN DVKVGNFVEL KKMSMGDGSK
     ASHLSYLGDA DIGSDVNMGC GSITVNYDGK NKFLTTIEDG AFVGCNANLI APVTVGKGAY
     VAAGSTITDD VPGESLAIAR ARQTNKEGYS KK
//

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