(data stored in SCRATCH zone)

SWISSPROT: C7QHI4_CATAD

ID   C7QHI4_CATAD            Unreviewed;       508 AA.
AC   C7QHI4;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 63.
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   OrderedLocusNames=Caci_0168 {ECO:0000313|EMBL:ACU69123.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69123.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69123.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
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:SAAS00650355}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + alpha-D-glucosamine 1-phosphate =
CC       CoA + N-acetyl-alpha-D-glucosamine 1-phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00650344}.
CC   -!- CATALYTIC ACTIVITY: UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
CC       = diphosphate + UDP-N-acetyl-alpha-D-glucosamine.
CC       {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00650293}.
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:SAAS00650347}.
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:SAAS00650354}.
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:SAAS00650342}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_01631,
CC       ECO:0000256|SAAS:SAAS00650301}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631,
CC       ECO:0000256|SAAS:SAAS00650327}.
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:SAAS00650305}.
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:SAAS00650312}.
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; CP001700; ACU69123.1; -; Genomic_DNA.
DR   RefSeq; WP_012784418.1; NC_013131.1.
DR   ProteinModelPortal; C7QHI4; -.
DR   STRING; 479433.Caci_0168; -.
DR   EnsemblBacteria; ACU69123; ACU69123; Caci_0168.
DR   KEGG; cai:Caci_0168; -.
DR   eggNOG; ENOG4105CAJ; Bacteria.
DR   eggNOG; COG1207; LUCA.
DR   HOGENOM; HOG000283476; -.
DR   KO; K04042; -.
DR   OMA; VNHLSYI; -.
DR   OrthoDB; POG091H02I2; -.
DR   UniPathway; UPA00113; UER00532.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000902; P:cell morphogenesis; IEA:UniProtKB-HAMAP.
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-HAMAP.
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   Gene3D; 3.90.550.10; -; 1.
DR   HAMAP; MF_01631; GlmU; 1.
DR   InterPro; IPR005882; Bifunctional_GlmU.
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.
DR   Pfam; PF00132; Hexapep; 2.
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; C7QHI4.
DR   SWISS-2DPAGE; C7QHI4.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00650319};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00650332};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00650295};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00650352};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00650323};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00650321};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00650297};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00650324};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00650358};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00650299};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00650328}.
FT   DOMAIN        9    142       NTP_transf_3. {ECO:0000259|Pfam:PF12804}.
FT   REGION        1    244       Pyrophosphorylase. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION       12     15       UDP-GlcNAc binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION       84     85       UDP-GlcNAc binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION      245    265       Linker. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   REGION      266    508       N-acetyltransferase. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION      400    401       Acetyl-CoA binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   ACT_SITE    377    377       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   METAL       113    113       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   METAL       242    242       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING      26     26       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING      79     79       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     150    150       UDP-GlcNAc; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01631}.
FT   BINDING     169    169       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     184    184       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     242    242       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     347    347       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     365    365       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     380    380       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     391    391       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     394    394       Acetyl-CoA; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01631}.
FT   BINDING     437    437       Acetyl-CoA; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01631}.
FT   BINDING     454    454       Acetyl-CoA. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
SQ   SEQUENCE   508 AA;  52153 MW;  30AEE63FE135761F CRC64;
     MTDQHAPTVI ILAAGEGKRM KSATPKVLHE LCGRTMLGHV VAAAQDLAPS RLAVVVGKGR
     DLVAPHVAAI APEARIVVQE PQNGTGQAAR LALEALVAEG GPAEGTVLVL LGDGAMVTGG
     TLRHLIAVHE SSGNAVTDLT AVVPDPRGLG RILREPDGTA EGRVLGIVEE KDCTPAQATI
     PEINSGIFAF DGKLLRDALS RLTTDNAQGE ELLTDVLAIA VGDGLPVGAV VAADYHEVLA
     ANDRAQLADL RRLMNQRITR QWMLEGVTIV DPATTWIDVH ATLEPDATIR PNTQLEGATR
     IAAGADVGPN CTLRDTVVGE RARVTNATTD GAEIGPEASV GPYTYLRPGT KLGRKSKAGG
     FVEMKKSTIG EGTKVPHLAY IGDATIGAGT NIGAGVITAN YDGYNKFPTR IGDHAFVGTN
     TTLIAPAEVA DGAYIAAGSA VNMPVGPGEL AVARGRQRNI AGYVARKRPD SVAAQAAARA
     AERAAAGGQP AVETNPTGGG PGAQADAV
//

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