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Database: UniProt
Entry: A0A0R2HM58_9FIRM
LinkDB: A0A0R2HM58_9FIRM
Original site: A0A0R2HM58_9FIRM 
ID   A0A0R2HM58_9FIRM        Unreviewed;       314 AA.
AC   A0A0R2HM58;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=GlmU protein {ECO:0000313|EMBL:KRN50516.1};
GN   ORFNames=IV49_GL002010 {ECO:0000313|EMBL:KRN50516.1};
OS   Kandleria vitulina DSM 20405.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Coprobacillaceae; Kandleria.
OX   NCBI_TaxID=1410657 {ECO:0000313|EMBL:KRN50516.1, ECO:0000313|Proteomes:UP000051841};
RN   [1] {ECO:0000313|EMBL:KRN50516.1, ECO:0000313|Proteomes:UP000051841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20405 {ECO:0000313|EMBL:KRN50516.1,
RC   ECO:0000313|Proteomes:UP000051841};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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   -!- 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:KRN50516.1}.
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DR   EMBL; JQBL01000008; KRN50516.1; -; Genomic_DNA.
DR   RefSeq; WP_031589003.1; NZ_JQBL01000008.1.
DR   AlphaFoldDB; A0A0R2HM58; -.
DR   PATRIC; fig|1410657.5.peg.2074; -.
DR   Proteomes; UP000051841; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd02540; GT2_GlmU_N_bac; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
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; 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:UP000051841};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          5..226
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   314 AA;  34535 MW;  79934C14D7C581D3 CRC64;
     MKVYAIVLAA GKGTRMKSDK PKVVHEVLYK PMINHVVDEL KKIGADETIV VVGHEAEQVK
     ALLDDSVTAV YQKEQLGTGH AVLMAKEALG DKEGMTLILC GDAPLIRAET LQGMIEAHEK
     NHNMGTVMTA DCDTSTHYGR IVKEDGQVTG IVEFKDLQPD QMDITEMNTG EYCFDNKALF
     EALEEVSNEN AQNEYYLTDV IGIMNNKGLK VDTYKIDDFN EVGGVNDRVA LEDATKMLQK
     RINHDWLVEG VSIIDASTTY IGRDVEIGAD AVIEPGCIIT GHSRIGSHAH IGAYSILHDV
     VVEDGEQIDA YTKR
//
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