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Database: UniProt
Entry: A0A2V3JVD2_9EURY
LinkDB: A0A2V3JVD2_9EURY
Original site: A0A2V3JVD2_9EURY 
ID   A0A2V3JVD2_9EURY        Unreviewed;       395 AA.
AC   A0A2V3JVD2;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Bifunctional protein GlmU {ECO:0000256|ARBA:ARBA00013414};
DE            EC=2.3.1.157 {ECO:0000256|ARBA:ARBA00012225};
DE            EC=2.7.7.23 {ECO:0000256|ARBA:ARBA00012457};
GN   ORFNames=C4B59_04200 {ECO:0000313|EMBL:PXF61445.1};
OS   ANME-2 cluster archaeon.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinales incertae sedis; ANME-2 cluster.
OX   NCBI_TaxID=2056317 {ECO:0000313|EMBL:PXF61445.1, ECO:0000313|Proteomes:UP000248329};
RN   [1] {ECO:0000313|EMBL:PXF61445.1, ECO:0000313|Proteomes:UP000248329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E20ANME2 {ECO:0000313|EMBL:PXF61445.1};
RA   Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the last two sequential reactions in the de novo
CC       biosynthetic pathway for UDP-N-acetyl-glucosamine (UDP-GlcNAc).
CC       Responsible for the acetylation of GlcN-1-P to GlcNAc-1-P, and for the
CC       uridyl transfer from UTP to GlcNAc-1-P, to produce UDP-GlcNAc and
CC       pyrophosphate. {ECO:0000256|ARBA:ARBA00024726}.
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};
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};
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|ARBA:ARBA00005166}.
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|ARBA:ARBA00005208}.
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}.
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:PXF61445.1}.
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DR   EMBL; PQXF01000005; PXF61445.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V3JVD2; -.
DR   UniPathway; UPA00113; UER00532.
DR   Proteomes; UP000248329; Unassembled WGS sequence.
DR   GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05636; LbH_G1P_TT_C_like; 1.
DR   CDD; cd04181; NTP_transferase; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   InterPro; IPR023915; Bifunctiontional_GlmU_arc-type.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   NCBIfam; TIGR03992; Arch_glmU; 1.
DR   PANTHER; PTHR43584:SF3; BIFUNCTIONAL PROTEIN GLMU; 1.
DR   PANTHER; PTHR43584; NUCLEOTIDYL TRANSFERASE; 1.
DR   Pfam; PF00132; Hexapep; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248329};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PXF61445.1}.
FT   DOMAIN          2..227
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   395 AA;  42037 MW;  584C5C7FA2DC282A CRC64;
     MKAVILAAGE GTRMRPLTAS CPKVMLSVAN RPILGHIIVA ARDAGIDEFV CVIGYMGDVV
     RDYFGDGSRF GVRIDYVEQR EQLGTAHAIG TASQSVEGRF LVLNGDAIIT PPDLRTLIGR
     KEDIVLATKE LENPAGYGVL KADGGRVARL IEKPDHAAGN LVNAGIYLFP DTIFDAIRET
     GESVRGEYEI TDSINALASV LDIGYSMLDT WIDIGRPWNL LDANEYLLAD IDSEIAGVVE
     PYATLNGNIR VGKGSIIRNG SYITGPAIIG ENCDIGPNCF IRPGTAIGDN VRIGNAVEVK
     NSIVMDGTNI GHLSYVGDSV IGRGCNLGAG TKIANLRHDG RNISVVVKRE SVDTGRRKLG
     VVMGDGVHTG INTSINVGVM MGACMSTRPG EVVMR
//
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