GLGB_MYCTU
ID GLGB_MYCTU Reviewed; 731 AA.
AC P9WN45; L0T925; Q10625;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB;
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=Glycogen-branching enzyme;
DE Short=BE;
GN Name=glgB; OrderedLocusNames=Rv1326c; ORFNames=MTCY130.11c;
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 FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, AND DISULFIDE BONDS.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17005418; DOI=10.1016/j.pep.2006.08.005;
RA Garg S.K., Alam M.S., Kishan K.V., Agrawal P.;
RT "Expression and characterization of alpha-(1,4)-glucan branching enzyme
RT Rv1326c of Mycobacterium tuberculosis H37Rv.";
RL Protein Expr. Purif. 51:198-208(2007).
RN [3]
RP FUNCTION IN CAPSULAR GLUCAN AND GLYCOGEN BIOSYNTHESIS, DISRUPTION
RP PHENOTYPE, ESSENTIALITY, AND PATHWAY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18808383; DOI=10.1111/j.1365-2958.2008.06445.x;
RA Sambou T., Dinadayala P., Stadthagen G., Barilone N., Bordat Y.,
RA Constant P., Levillain F., Neyrolles O., Gicquel B., Lemassu A., Daffe M.,
RA Jackson M.;
RT "Capsular glucan and intracellular glycogen of Mycobacterium tuberculosis:
RT biosynthesis and impact on the persistence in mice.";
RL Mol. Microbiol. 70:762-774(2008).
RN [4]
RP INTERACTION WITH WHIB1, AND DISULFIDE BOND.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19121228; DOI=10.1186/1471-2091-10-1;
RA Garg S., Alam M.S., Bajpai R., Kishan K.R., Agrawal P.;
RT "Redox biology of Mycobacterium tuberculosis H37Rv: protein-protein
RT interaction between GlgB and WhiB1 involves exchange of thiol-disulfide.";
RL BMC Biochem. 10:1-1(2009).
RN [5]
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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) OF 10-371, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, AND CATALYTIC MECHANISM.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20444687; DOI=10.1074/jbc.m110.121707;
RA Pal K., Kumar S., Sharma S., Garg S.K., Alam M.S., Xu H.E., Agrawal P.,
RA Swaminathan K.;
RT "Crystal structure of full-length Mycobacterium tuberculosis H37Rv glycogen
RT branching enzyme: insights of N-terminal beta-sandwich in substrate
RT specificity and enzymatic activity.";
RL J. Biol. Chem. 285:20897-20903(2010).
CC -!- FUNCTION: Essential enzyme that catalyzes the formation of the alpha-
CC 1,6-glucosidic linkages in glucan chains by scission of a 1,4-alpha-
CC linked oligosaccharide from growing alpha-1,4-glucan chains and the
CC subsequent attachment of the oligosaccharide to the alpha-1,6 position.
CC Is involved in the biosynthesis of both glycogen and capsular alpha-D-
CC glucan. {ECO:0000269|PubMed:17005418, ECO:0000269|PubMed:18808383}.
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 Evidence={ECO:0000269|PubMed:17005418, ECO:0000269|PubMed:20444687};
CC -!- ACTIVITY REGULATION: Is inhibited by divalent cations such as Zn(2+)
CC and Cu(2+), but not by Mg(2+), Mn(2+) and Ca(2+). Is not inhibited by
CC several known inhibitors of the GH13 family such as ADP, ADP glucose,
CC tunicamycin, castenospermine, nojirimycin, or acarbose.
CC {ECO:0000269|PubMed:17005418, ECO:0000269|PubMed:20444687}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:17005418};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius. Loses 20% of its maximum
CC activity at 37 degrees Celsius and is nearly inactive above 55
CC degrees Celsius. {ECO:0000269|PubMed:17005418};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000269|PubMed:18808383}.
CC -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC {ECO:0000269|PubMed:18808383}.
CC -!- SUBUNIT: Monomer. Interacts with WhiB1 via an intermolecular disulfide
CC bond. {ECO:0000269|PubMed:17005418, ECO:0000269|PubMed:19121228}.
CC -!- DISRUPTION PHENOTYPE: Disruption of glgB is lethal for the bacteria in
CC vitro. Affects the production of both extracellular alpha-D-glucan and
CC intracellular glycogen. {ECO:0000269|PubMed:18808383}.
CC -!- MISCELLANEOUS: Cysteine residues of GlgB form structural disulfide
CC bond(s), which allow the protein to exist in two different redox-
CC dependent conformational states. Although the conformational change do
CC not affect the branching enzyme activity, the change in surface
CC hydrophobicity could influence the interaction or dissociation of
CC different cellular proteins with GlgB in response to different
CC physiological states.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000305}.
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DR EMBL; AL123456; CCP44084.1; -; Genomic_DNA.
DR PIR; B70770; B70770.
DR RefSeq; NP_215842.1; NC_000962.3.
DR RefSeq; WP_003900318.1; NZ_NVQJ01000031.1.
DR PDB; 3K1D; X-ray; 2.33 A; A=10-731.
DR PDBsum; 3K1D; -.
DR AlphaFoldDB; P9WN45; -.
DR SMR; P9WN45; -.
DR STRING; 83332.Rv1326c; -.
DR PaxDb; P9WN45; -.
DR DNASU; 886893; -.
DR GeneID; 886893; -.
DR KEGG; mtu:Rv1326c; -.
DR TubercuList; Rv1326c; -.
DR eggNOG; COG0296; Bacteria.
DR OMA; FGMKWMM; -.
DR PhylomeDB; P9WN45; -.
DR BioCyc; MetaCyc:G185E-5505-MON; -.
DR BRENDA; 2.4.1.18; 3445.
DR UniPathway; UPA00164; -.
DR UniPathway; UPA00934; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IDA:MTBBASE.
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:0043169; F:cation binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0009250; P:glucan biosynthetic process; IMP:MTBBASE.
DR GO; GO:0005978; P:glycogen biosynthetic process; IMP:MTBBASE.
DR CDD; cd02855; E_set_GBE_prok_N; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.60.40.1180; -; 1.
DR HAMAP; MF_00685; GlgB; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR037439; Branching_enzy.
DR InterPro; IPR006407; GlgB.
DR InterPro; IPR044143; GlgB_N_E_set_prok.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004193; Glyco_hydro_13_N.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR43651; PTHR43651; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR Pfam; PF02922; CBM_48; 1.
DR PIRSF; PIRSF000463; GlgB; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 2.
DR TIGRFAMs; TIGR01515; branching_enzym; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsule biogenesis/degradation; Carbohydrate metabolism;
KW Disulfide bond; Glycogen biosynthesis; Glycogen metabolism;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..731
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000188718"
FT ACT_SITE 411
FT /note="Nucleophile"
FT ACT_SITE 464
FT /note="Proton donor"
FT DISULFID 193..617
FT /evidence="ECO:0000305|PubMed:17005418,
FT ECO:0000305|PubMed:19121228"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 34..48
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 140..152
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 239..245
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:3K1D"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 271..285
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 321..333
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:3K1D"
FT TURN 351..358
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 386..402
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 407..410
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 414..417
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 439..455
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 460..463
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 484..487
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 489..500
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 503..509
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 510..514
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 515..518
FT /evidence="ECO:0007829|PDB:3K1D"
FT TURN 519..521
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 525..529
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 531..533
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 541..544
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 549..565
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 566..573
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 576..578
FT /evidence="ECO:0007829|PDB:3K1D"
FT TURN 586..588
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 592..596
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 597..600
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 601..617
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 619..621
FT /evidence="ECO:0007829|PDB:3K1D"
FT TURN 622..626
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 628..630
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 631..638
FT /evidence="ECO:0007829|PDB:3K1D"
FT TURN 639..642
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 643..649
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 655..661
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 663..665
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 667..676
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 678..685
FT /evidence="ECO:0007829|PDB:3K1D"
FT HELIX 689..691
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 701..706
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 712..720
FT /evidence="ECO:0007829|PDB:3K1D"
FT STRAND 724..730
FT /evidence="ECO:0007829|PDB:3K1D"
SQ SEQUENCE 731 AA; 81729 MW; EE2BFEF765352617 CRC64;
MSRSEKLTGE HLAPEPAEMA RLVAGTHHNP HGILGAHEYD DHTVIRAFRP HAVEVVALVG
KDRFSLQHLD SGLFAVALPF VDLIDYRLQV TYEGCEPHTV ADAYRFLPTL GEVDLHLFAE
GRHERLWEVL GAHPRSFTTA DGVVSGVSFA VWAPNAKGVS LIGEFNGWNG HEAPMRVLGP
SGVWELFWPD FPCDGLYKFR VHGADGVVTD RADPFAFGTE VPPQTASRVT SSDYTWGDDD
WMAGRALRNP VNEAMSTYEV HLGSWRPGLS YRQLARELTD YIVDQGFTHV ELLPVAEHPF
AGSWGYQVTS YYAPTSRFGT PDDFRALVDA LHQAGIGVIV DWVPAHFPKD AWALGRFDGT
PLYEHSDPKR GEQLDWGTYV FDFGRPEVRN FLVANALYWL QEFHIDGLRV DAVASMLYLD
YSRPEGGWTP NVHGGRENLE AVQFLQEMNA TAHKVAPGIV TIAEESTPWS GVTRPTNIGG
LGFSMKWNMG WMHDTLDYVS RDPVYRSYHH HEMTFSMLYA FSENYVLPLS HDEVVHGKGT
LWGRMPGNNH VKAAGLRSLL AYQWAHPGKQ LLFMGQEFGQ RAEWSEQRGL DWFQLDENGF
SNGIQRLVRD INDIYRCHPA LWSLDTTPEG YSWIDANDSA NNVLSFMRYG SDGSVLACVF
NFAGAEHRDY RLGLPRAGRW REVLNTDATI YHGSGIGNLG GVDATDDPWH GRPASAVLVL
PPTSALWLTP A
