SUSB_BACTN
ID SUSB_BACTN Reviewed; 738 AA.
AC G8JZS4; P71094; Q7C3Z2;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Glucan 1,4-alpha-glucosidase SusB;
DE EC=3.2.1.3;
DE AltName: Full=Alpha-glucosidase SusB;
DE AltName: Full=Glucoamylase SusB;
DE AltName: Full=Starch-utilization system protein B;
DE Flags: Precursor;
GN Name=susB; OrderedLocusNames=BT_3703;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=8955399; DOI=10.1128/jb.178.24.7173-7179.1996;
RA D'Elia J.N., Salyers A.A.;
RT "Contribution of a neopullulanase, a pullulanase, and an alpha-glucosidase
RT to growth of Bacteroides thetaiotaomicron on starch.";
RL J. Bacteriol. 178:7173-7179(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 22-738 IN COMPLEX WITH CALCIUM
RP AND ACARBOSE, FUNCTION, ACTIVE SITE, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF GLU-439;
RP GLU-508 AND GLU-532.
RX PubMed=18981178; DOI=10.1074/jbc.m806115200;
RA Kitamura M., Okuyama M., Tanzawa F., Mori H., Kitago Y., Watanabe N.,
RA Kimura A., Tanaka I., Yao M.;
RT "Structural and functional analysis of a glycoside hydrolase family 97
RT enzyme from Bacteroides thetaiotaomicron.";
RL J. Biol. Chem. 283:36328-36337(2008).
CC -!- FUNCTION: Glucoamylase that hydrolyzes alpha-1,4-glucosidic linkages,
CC alpha-1,6-, alpha-1,3- and alpha-1,2-glucosidic linkages during starch
CC degradation. {ECO:0000269|PubMed:18981178, ECO:0000269|PubMed:8955399}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues
CC successively from non-reducing ends of the chains with release of
CC beta-D-glucose.; EC=3.2.1.3; Evidence={ECO:0000269|PubMed:18981178};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:18981178};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:18981178};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.05 mM for maltose {ECO:0000269|PubMed:18981178};
CC KM=0.29 mM for maltotriose {ECO:0000269|PubMed:18981178};
CC KM=0.64 mM for maltotetraose {ECO:0000269|PubMed:18981178};
CC KM=1.29 mM for maltopentaose {ECO:0000269|PubMed:18981178};
CC KM=2.71 mM for maltohexaose {ECO:0000269|PubMed:18981178};
CC KM=4.58 mM for maltoheptaose {ECO:0000269|PubMed:18981178};
CC KM=6.89 mM for amylose DP17 {ECO:0000269|PubMed:18981178};
CC KM=0.67 mM for soluble starch {ECO:0000269|PubMed:18981178};
CC KM=2.39 mM for kojibiose {ECO:0000269|PubMed:18981178};
CC KM=3.14 mM for nigerose {ECO:0000269|PubMed:18981178};
CC KM=6.34 mM for isomaltose {ECO:0000269|PubMed:18981178};
CC KM=0.31 mM for panose {ECO:0000269|PubMed:18981178};
CC KM=0.16 mM for p-nitrophenyl alpha-glucoside
CC {ECO:0000269|PubMed:18981178};
CC Note=kcat is 182 sec(-1) for maltose. kcat is 270 sec(-1) for
CC maltotriose. kcat is 321 sec(-1) for maltotetraose. kcat is 434 sec(-
CC 1) for maltopentaose. kcat is 346 sec(-1) for maltohexaose. kcat is
CC 381 sec(-1) for maltoheptaose. kcat is 321 sec(-1) for amylose DP17.
CC kcat is 115 sec(-1) for soluble starch. kcat is 141 sec(-1) for
CC kojibiose. kcat is 207 sec(-1) for nigerose. kcat is 105 sec(-1) for
CC isomaltose. kcat is 160 sec(-1) for panose. kcat is 161 sec(-1) for
CC p-nitrophenyl alpha-glucoside. {ECO:0000269|PubMed:18981178};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:18981178};
CC -!- PATHWAY: Glycan degradation; starch degradation.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18981178}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:8955399}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 97 family. {ECO:0000305}.
CC -!- CAUTION: Although initially defined as an alpha-glucosidase, it
CC produces beta-glucose by an inverting mechanism, suggesting it rather
CC acts as a glucan 1,4-alpha-glucosidase. {ECO:0000305|PubMed:18981178}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U66897; AAC44671.1; -; Genomic_DNA.
DR EMBL; AE015928; AAO78808.1; -; Genomic_DNA.
DR RefSeq; NP_812614.1; NC_004663.1.
DR RefSeq; WP_008767003.1; NC_004663.1.
DR PDB; 2D73; X-ray; 1.60 A; A/B=22-738.
DR PDB; 2JKA; X-ray; 1.90 A; A/B=22-738.
DR PDB; 2JKE; X-ray; 1.70 A; A/B=22-738.
DR PDB; 2JKP; X-ray; 1.99 A; A/B=22-738.
DR PDB; 2ZQ0; X-ray; 1.60 A; A/B=22-738.
DR PDB; 3WFA; X-ray; 2.00 A; A/B=22-738.
DR PDBsum; 2D73; -.
DR PDBsum; 2JKA; -.
DR PDBsum; 2JKE; -.
DR PDBsum; 2JKP; -.
DR PDBsum; 2ZQ0; -.
DR PDBsum; 3WFA; -.
DR AlphaFoldDB; G8JZS4; -.
DR SMR; G8JZS4; -.
DR STRING; 226186.BT_3703; -.
DR CAZy; GH97; Glycoside Hydrolase Family 97.
DR PaxDb; G8JZS4; -.
DR PRIDE; G8JZS4; -.
DR EnsemblBacteria; AAO78808; AAO78808; BT_3703.
DR GeneID; 60924872; -.
DR KEGG; bth:BT_3703; -.
DR PATRIC; fig|226186.12.peg.3763; -.
DR eggNOG; COG1082; Bacteria.
DR HOGENOM; CLU_011166_2_0_10; -.
DR OMA; MMKTDDG; -.
DR SABIO-RK; G8JZS4; -.
DR UniPathway; UPA00153; -.
DR PRO; PR:G8JZS4; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MENGO.
DR GO; GO:0004558; F:alpha-1,4-glucosidase activity; IMP:MENGO.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0005983; P:starch catabolic process; IDA:UniProtKB.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR029483; GH97_C.
DR InterPro; IPR019563; GH97_catalytic.
DR InterPro; IPR029486; GH97_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF14509; GH97_C; 1.
DR Pfam; PF14508; GH97_N; 1.
DR Pfam; PF10566; Glyco_hydro_97; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Metal-binding; Periplasm; Polysaccharide degradation; Reference proteome;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..738
FT /note="Glucan 1,4-alpha-glucosidase SusB"
FT /id="PRO_0000425886"
FT ACT_SITE 532
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:18981178"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:18981178"
FT BINDING 215..217
FT /ligand="substrate"
FT BINDING 437..439
FT /ligand="substrate"
FT BINDING 507..508
FT /ligand="substrate"
FT BINDING 508
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:18981178"
FT BINDING 526
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:18981178"
FT BINDING 532
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:18981178"
FT SITE 194
FT /note="Substrate"
FT SITE 331
FT /note="Substrate"
FT SITE 467
FT /note="Substrate"
FT MUTAGEN 439
FT /note="E->Q: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:18981178"
FT MUTAGEN 508
FT /note="E->Q: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:18981178"
FT MUTAGEN 532
FT /note="E->Q: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:18981178"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:2D73"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 97..110
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 120..133
FT /evidence="ECO:0007829|PDB:2D73"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 138..147
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 163..171
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:2D73"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:2D73"
FT HELIX 205..212
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 240..246
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:2D73"
FT TURN 260..263
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 288..296
FT /evidence="ECO:0007829|PDB:2D73"
FT HELIX 297..302
FT /evidence="ECO:0007829|PDB:2D73"
FT HELIX 305..308
FT /evidence="ECO:0007829|PDB:2D73"
FT HELIX 318..321
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 325..330
FT /evidence="ECO:0007829|PDB:2D73"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:2D73"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:2D73"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:2D73"
FT HELIX 370..382
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 386..390
FT /evidence="ECO:0007829|PDB:2D73"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:2D73"
FT HELIX 420..429
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 433..439
FT /evidence="ECO:0007829|PDB:2D73"
FT HELIX 444..460
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 465..469
FT /evidence="ECO:0007829|PDB:2D73"
FT HELIX 484..499
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 503..506
FT /evidence="ECO:0007829|PDB:2D73"
FT HELIX 515..517
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 522..525
FT /evidence="ECO:0007829|PDB:2D73"
FT HELIX 531..535
FT /evidence="ECO:0007829|PDB:2D73"
FT HELIX 543..545
FT /evidence="ECO:0007829|PDB:2D73"
FT HELIX 547..549
FT /evidence="ECO:0007829|PDB:2D73"
FT TURN 550..554
FT /evidence="ECO:0007829|PDB:2D73"
FT HELIX 568..570
FT /evidence="ECO:0007829|PDB:2D73"
FT HELIX 583..592
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 596..599
FT /evidence="ECO:0007829|PDB:2D73"
FT HELIX 604..607
FT /evidence="ECO:0007829|PDB:2D73"
FT HELIX 611..619
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 622..633
FT /evidence="ECO:0007829|PDB:2D73"
FT TURN 634..636
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 637..644
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 650..656
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 661..666
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 676..683
FT /evidence="ECO:0007829|PDB:2D73"
FT TURN 689..691
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 696..703
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 708..713
FT /evidence="ECO:0007829|PDB:2D73"
FT STRAND 718..725
FT /evidence="ECO:0007829|PDB:2D73"
FT HELIX 729..731
FT /evidence="ECO:0007829|PDB:2ZQ0"
SQ SEQUENCE 738 AA; 84378 MW; 2BFE87C3552C9A12 CRC64;
MKKRKILSLI AFLCISFIAN AQQKLTSPDN NLVMTFQVDS KGAPTYELTY KNKVVIKPST
LGLELKKEDN TRTDFDWVDR RDLTKLDSKT NLYDGFEVKD TQTATFDETW QPVWGEEKEI
RNHYNELAVT LYQPMNDRSI VIRFRLFNDG LGFRYEFPQQ KSLNYFVIKE EHSQFGMNGD
HIAFWIPGDY DTQEYDYTIS RLSEIRGLMK EAITPNSSQT PFSQTGVQTA LMMKTDDGLY
INLHEAALVD YSCMHLNLDD KNMVFESWLT PDAKGDKGYM QTPCNTPWRT IIVSDDARNI
LASRITLNLN EPCKIADAAS WVKPVKYIGV WWDMITGKGS WAYTDELTSV KLGETDYSKT
KPNGKHSANT ANVKRYIDFA AAHGFDAVLV EGWNEGWEDW FGNSKDYVFD FVTPYPDFDV
KEIHRYAARK GIKMMMHHET SASVRNYERH MDKAYQFMAD NGYNSVKSGY VGNIIPRGEH
HYGQWMNNHY LYAVKKAADY KIMVNAHEAT RPTGICRTYP NLIGNESARG TEYESFGGNK
VYHTTILPFT RLVGGPMDYT PGIFETHCNK MNPANNSQVR STIARQLALY VTMYSPLQMA
ADIPENYERF MDAFQFIKDV ALDWDETNYL EAEPGEYITI ARKAKDTDDW YVGCTAGENG
HTSKLVFDFL TPGKQYIATV YADAKDADWK ENPQAYTIKK GILTNKSKLN LHAANGGGYA
ISIKEVKDKS EAKGLKRL
