MPUS_MICLC
ID MPUS_MICLC Reviewed; 243 AA.
AC C5CBV8;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Undecaprenyl-phosphate mannosyltransferase;
DE EC=2.4.1.54 {ECO:0000269|PubMed:17072001, ECO:0000269|PubMed:5350943};
DE AltName: Full=Mannosylphosphorylundecaprenol synthase;
DE Short=MPUS;
GN OrderedLocusNames=Mlut_12000;
OS Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 /
OS NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Micrococcus.
OX NCBI_TaxID=465515;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC
RC 2665 / VKM Ac-2230;
RX PubMed=19948807; DOI=10.1128/jb.01254-09;
RA Young M., Artsatbanov V., Beller H.R., Chandra G., Chater K.F., Dover L.G.,
RA Goh E.B., Kahan T., Kaprelyants A.S., Kyrpides N., Lapidus A., Lowry S.R.,
RA Lykidis A., Mahillon J., Markowitz V., Mavromatis K., Mukamolova G.V.,
RA Oren A., Rokem J.S., Smith M.C., Young D.I., Greenblatt C.L.;
RT "Genome sequence of the Fleming strain of Micrococcus luteus, a simple
RT free-living actinobacterium.";
RL J. Bacteriol. 192:841-860(2010).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=5350943; DOI=10.1016/s0021-9258(18)63557-4;
RA Lahav M., Chiu T.H., Lennarz W.J.;
RT "Studies on the biosynthesis of mannan in Micrococcus lysodeikticus. II.
RT The enzymatic synthesis of mannosyl-l-phosphoryl-undecaprenol.";
RL J. Biol. Chem. 244:5890-5898(1969).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17072001; DOI=10.1385/1-59745-167-3:13;
RA Rush J.S., Waechter C.J.;
RT "Partial purification of mannosylphosphorylundecaprenol synthase from
RT Micrococcus luteus: a useful enzyme for the biosynthesis of a variety of
RT mannosylphosphorylpolyisoprenol products.";
RL Methods Mol. Biol. 347:13-30(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
RX PubMed=24386392; DOI=10.1371/journal.pone.0084508;
RA Ramkissoon K.R., Miller J.K., Ojha S., Watson D.S., Bomar M.G.,
RA Galande A.K., Shearer A.G.;
RT "Rapid identification of sequences for orphan enzymes to power accurate
RT protein annotation.";
RL PLoS ONE 8:E84508-E84508(2013).
CC -!- FUNCTION: Catalyzes the transfer of mannose from GDP-mannose to D-
CC mannosyl-1-phosphoundecaprenol. {ECO:0000269|PubMed:17072001,
CC ECO:0000269|PubMed:5350943, ECO:0000305|PubMed:24386392}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-trans,octa-cis-undecaprenyl phosphate + GDP-alpha-D-mannose
CC = D-mannosyl di-trans,octa-cis-undecaprenyl phosphate + GDP;
CC Xref=Rhea:RHEA:28118, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:60392, ChEBI:CHEBI:61761; EC=2.4.1.54;
CC Evidence={ECO:0000269|PubMed:17072001, ECO:0000269|PubMed:5350943};
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; CP001628; ACS30705.1; -; Genomic_DNA.
DR RefSeq; WP_010078652.1; NZ_WBMF01000034.1.
DR AlphaFoldDB; C5CBV8; -.
DR SMR; C5CBV8; -.
DR STRING; 465515.Mlut_12000; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PRIDE; C5CBV8; -.
DR EnsemblBacteria; ACS30705; ACS30705; Mlut_12000.
DR KEGG; mlu:Mlut_12000; -.
DR PATRIC; fig|465515.4.peg.1141; -.
DR eggNOG; COG1216; Bacteria.
DR HOGENOM; CLU_033536_13_0_11; -.
DR OMA; TAYIHGF; -.
DR OrthoDB; 1064289at2; -.
DR Proteomes; UP000000738; Chromosome.
DR GO; GO:0036427; F:all-trans-undecaprenyl-phosphate mannosyltransferase activity; IEA:RHEA.
DR GO; GO:0004582; F:dolichyl-phosphate beta-D-mannosyltransferase activity; IEA:InterPro.
DR CDD; cd06442; DPM1_like; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR039528; DPM1-like.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43398; PTHR43398; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..243
FT /note="Undecaprenyl-phosphate mannosyltransferase"
FT /id="PRO_0000425562"
SQ SEQUENCE 243 AA; 26765 MW; 6632072BAA7BDAFE CRC64;
MRVLTIIPTY NEIESLPLTL GRLRDAVPES DVLVVDDASP DGTGDWADTR AAEDPSVHVL
HRTTKDGLGG AYIAGFRWGL ERGYDVLVEM DADGSHQPEQ LPRLLEAVRT ADLVIGSRRV
PGGKMVNWPT SRKMISWAGS LYPRIMLGLN LTDITAGYRA YRADTLRAID LDAIESKGYG
FQVDMTFRTA RLGKRIVEVP ITFVERELGE SKMSGGIVGE AVVNVTRWGL AARWEGLRAR
LGL