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   27-MAR-2024, entry version 64.
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; Bacteroidota; 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
CC         sec(-1) for maltopentaose. kcat is 346 sec(-1) for maltohexaose. kcat
CC         is 381 sec(-1) for maltoheptaose. kcat is 321 sec(-1) for amylose
CC         DP17. 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}.
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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; 226186-BT_3703; -.
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   InParanoid; G8JZS4; -.
DR   OrthoDB; 1109141at2; -.
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; Aldolase class I; 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   PANTHER; PTHR35803:SF1; GLUCAN 1,4-ALPHA-GLUCOSIDASE SUSB; 1.
DR   PANTHER; PTHR35803; GLUCAN 1,4-ALPHA-GLUCOSIDASE SUSB-RELATED; 1.
DR   Pfam; PF14509; GH97_C; 1.
DR   Pfam; PF14508; GH97_N; 1.
DR   Pfam; PF10566; Glyco_hydro_97; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 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
//