ID V2ZJT3_9FIRM Unreviewed; 227 AA.
AC V2ZJT3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Bifunctional protein GlmU {ECO:0000313|EMBL:USF27315.1};
DE SubName: Full=UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase {ECO:0000313|EMBL:ESL14905.1};
GN Name=glmU_1 {ECO:0000313|EMBL:USF27315.1};
GN ORFNames=N510_002261 {ECO:0000313|EMBL:USF27315.1}, N510_00939
GN {ECO:0000313|EMBL:ESL14905.1};
OS Firmicutes bacterium ASF500.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1378168 {ECO:0000313|EMBL:ESL14905.1};
RN [1] {ECO:0000313|EMBL:ESL14905.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF500 {ECO:0000313|EMBL:ESL14905.1};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
RN [2] {ECO:0000313|EMBL:USF27315.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF500 {ECO:0000313|EMBL:USF27315.1};
RA Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT Model to Study Microbiome Function.";
RL Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC hexapeptide repeat family. {ECO:0000256|ARBA:ARBA00007707}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the N-
CC acetylglucosamine-1-phosphate uridyltransferase family.
CC {ECO:0000256|ARBA:ARBA00007947}.
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DR EMBL; AYJP01000005; ESL14905.1; -; Genomic_DNA.
DR EMBL; CP097573; USF27315.1; -; Genomic_DNA.
DR AlphaFoldDB; V2ZJT3; -.
DR STRING; 1378168.N510_00939; -.
DR PATRIC; fig|1378168.3.peg.978; -.
DR eggNOG; COG1207; Bacteria.
DR HOGENOM; CLU_029499_15_2_9; -.
DR Proteomes; UP000017395; Chromosome.
DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:InterPro.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:InterPro.
DR CDD; cd03353; LbH_GlmU_C; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR InterPro; IPR038009; GlmU_C_LbH.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR43584:SF3; BIFUNCTIONAL PROTEIN GLMU; 1.
DR PANTHER; PTHR43584; NUCLEOTIDYL TRANSFERASE; 1.
DR Pfam; PF00132; Hexapep; 3.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000017395};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ESL14905.1}.
SQ SEQUENCE 227 AA; 23997 MW; 1674CC78BC2E0047 CRC64;
MNDYSAPLQA KREQLLAQGV LMMDPAAVYV EDQVEVGAGT TLLPGTILRG RTVIGQNCCI
GPQVMLTACT VEDGCTINAS QCEESVIERD CQIGPYAHIR PHCVVGAGSS IGAFVQLKNC
NLGRGTKMAH LTYVGDSDVG DGCNFGCGTI TCNYDGFQKY RTTIGSGVFV GCNTNLVAPV
TVEDGAFIAA GTTVTQPVPE DAMAIGRARQ EVKEGWAAEN RKKKGNR
//
