BE_MYCTU
ID BE_MYCTU Reviewed; 526 AA.
AC P9WQ27; L0TE45; O53278; Q7D694;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Probable 1,4-alpha-glucan branching enzyme Rv3031;
DE EC=2.4.1.18;
DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase;
DE AltName: Full=Alpha-(1->4)-glucan branching enzyme;
DE AltName: Full=Branching enzyme;
DE Short=BE;
GN OrderedLocusNames=Rv3031;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP PROBABLE FUNCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17640872; DOI=10.1074/jbc.m702676200;
RA Stadthagen G., Sambou T., Guerin M., Barilone N., Boudou F.,
RA Kordulakova J., Charles P., Alzari P.M., Lemassu A., Daffe M., Puzo G.,
RA Gicquel B., Riviere M., Jackson M.;
RT "Genetic basis for the biosynthesis of methylglucose lipopolysaccharides in
RT Mycobacterium tuberculosis.";
RL J. Biol. Chem. 282:27270-27276(2007).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Catalyzes the formation of branch points in alpha-glucans by
CC cleavage of an alpha-1,4 glycosidic bond and subsequent transfer of the
CC cleaved-off oligosaccharide to a new alpha-1,6 position (Probable). Is
CC probably involved in the biosynthesis of 6-O-methylglucosyl
CC lipopolysaccharides (MGLP). {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Transfers a segment of a (1->4)-alpha-D-glucan chain to a
CC primary hydroxy group in a similar glucan chain.; EC=2.4.1.18;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 57 family. {ECO:0000305}.
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DR EMBL; AL123456; CCP45839.1; -; Genomic_DNA.
DR PIR; B70859; B70859.
DR RefSeq; NP_217547.1; NC_000962.3.
DR RefSeq; WP_003899891.1; NZ_NVQJ01000011.1.
DR AlphaFoldDB; P9WQ27; -.
DR SMR; P9WQ27; -.
DR STRING; 83332.Rv3031; -.
DR PaxDb; P9WQ27; -.
DR DNASU; 888543; -.
DR GeneID; 888543; -.
DR KEGG; mtu:Rv3031; -.
DR TubercuList; Rv3031; -.
DR eggNOG; COG1543; Bacteria.
DR OMA; CAYYEGL; -.
DR PhylomeDB; P9WQ27; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:UniProtKB-EC.
DR GO; GO:0102752; F:1,4-alpha-glucan branching enzyme activity (using a glucosylated glycogenin as primer for glycogen synthesis); IEA:UniProtKB-EC.
DR GO; GO:0030979; P:alpha-glucan biosynthetic process; IEA:InterPro.
DR Gene3D; 1.20.1430.10; -; 1.
DR Gene3D; 3.20.110.10; -; 1.
DR InterPro; IPR037090; 57_glycoside_trans_central.
DR InterPro; IPR015293; BE_C.
DR InterPro; IPR040042; Branching_enz_MT3115-like.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR InterPro; IPR004300; Glyco_hydro_57_N.
DR PANTHER; PTHR41695; PTHR41695; 1.
DR Pfam; PF09210; DUF1957; 1.
DR Pfam; PF03065; Glyco_hydro_57; 1.
DR SUPFAM; SSF88688; SSF88688; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycosyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..526
FT /note="Probable 1,4-alpha-glucan branching enzyme Rv3031"
FT /id="PRO_0000413972"
FT ACT_SITE 205
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 344
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 462
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 526 AA; 57815 MW; 6095D375968E9589 CRC64;
MNTSASPVPG LFTLVLHTHL PWLAHHGRWP VGEEWLYQSW AAAYLPLLQV LAALADENRH
RLITLGMTPV VNAQLDDPYC LNGVHHWLAN WQLRAEEAAS VRYARQSKSA DYPSCTPEAL
RAFGIRECAD AARALDNFAT RWRHGGSPLL RGLIDAGTVE LLGGPLAHPF QPLLAPRLRE
FALREGLADA QLRLAHRPKG IWAPECAYAP GMEVDYATAG VSHFMVDGPS LHGDTALGRP
VGKTDVVAFG RDLQVSYRVW SPKSGYPGHA AYRDFHTYDH LTGLKPARVT GRNVPSEQKA
PYDPERADRA VDVHVADFVD VVRNRLLSES ERIGRPAHVI AAFDTELFGH WWYEGPTWLQ
RVLRALPAAG VRVGTLSDAI ADGFVGDPVE LPPSSWGSGK DWQVWSGAKV ADLVQLNSEV
VDTALTTIDK ALAQTASLDG PLPRDHVADQ ILRETLLTVS SDWPFMVSKD SAADYARYRA
HLHAHATREI AGALAAGRRD TARRLAEGWN RADGLFGALD ARRLPK
