SUSA_BACTN
ID SUSA_BACTN Reviewed; 617 AA.
AC Q8A1G0; P71093;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Neopullulanase SusA;
DE EC=3.2.1.135;
DE AltName: Full=Starch-utilization system protein A;
DE Flags: Precursor;
GN Name=susA; OrderedLocusNames=BT_3704;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-567, FUNCTION, SUBCELLULAR LOCATION,
RP AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Neopullulanase that cleaves 1,4-alpha-glucosidic linkages in
CC starch to produce disaccharides or trisaccharides in starch
CC degradation. {ECO:0000269|PubMed:8955399}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of pullulan to panose (6-alpha-D-glucosylmaltose).;
CC EC=3.2.1.135;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 1 Ca(2+) ion per subunit.;
CC -!- PATHWAY: Glycan degradation; starch degradation.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:8955399}.
CC -!- DISRUPTION PHENOTYPE: Reduction by 30% of the rate of growth on starch.
CC {ECO:0000269|PubMed:8955399}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC44670.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE015928; AAO78809.1; -; Genomic_DNA.
DR EMBL; U66897; AAC44670.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; NP_812615.1; NC_004663.1.
DR RefSeq; WP_008767002.1; NC_004663.1.
DR AlphaFoldDB; Q8A1G0; -.
DR SMR; Q8A1G0; -.
DR STRING; 226186.BT_3704; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; Q8A1G0; -.
DR PRIDE; Q8A1G0; -.
DR EnsemblBacteria; AAO78809; AAO78809; BT_3704.
DR GeneID; 60924873; -.
DR KEGG; bth:BT_3704; -.
DR PATRIC; fig|226186.12.peg.3764; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_006462_7_3_10; -.
DR InParanoid; Q8A1G0; -.
DR OMA; TPDWVKH; -.
DR UniPathway; UPA00153; -.
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:0004556; F:alpha-amylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031216; F:neopullulanase activity; IMP:MENGO.
DR GO; GO:0009313; P:oligosaccharide catabolic process; IBA:GO_Central.
DR GO; GO:0005983; P:starch catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR015171; Cyc-maltodext_N.
DR InterPro; IPR019492; Cyclo-malto-dextrinase_C.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
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 Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF10438; Cyc-maltodext_C; 1.
DR Pfam; PF09087; Cyc-maltodext_N; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycosidase; Hydrolase; Metal-binding; Periplasm;
KW Polysaccharide degradation; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..617
FT /note="Neopullulanase SusA"
FT /id="PRO_0000425888"
FT ACT_SITE 331
FT /evidence="ECO:0000250"
FT ACT_SITE 360
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT SITE 440
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 103
FT /note="T -> I (in Ref. 2; AAC44670)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="C -> S (in Ref. 2; AAC44670)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="R -> P (in Ref. 2; AAC44670)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 617 AA; 71184 MW; 034B45BE3309D4EC CRC64;
MKRNLLFIIL LLLLPGLHQV FATSTIKKVA PTFWWAGMKN PELQILLYGD RISSADVSLS
ADNITLQEVV KQENPNYLVL YLDLSKAAPQ NFDIILKQGK KQTKIPYELK QRRPNASAVE
GFDSSDVLYL IMPDRFANGN PSNDIIPGML EGNVDRNEPF ARHGGDLKGI ENHLDYIADL
GVTSIWLNPI QENDMKEGSY HGYAITDYYQ VDRRFGSNEE FRKLTQEANA KGLKVVMDMI
FNHCGSDNYL FKDMPSKDWF NFEGNYVQTS FKTATQMDPY ASDYEKKIAI DGWFTLTMPD
FNQRNRHVAT YLIQSSIWWI EYAGINGIRQ DTHPYADFDM MARWCKAVNE EYPKFNIVGE
TWLGNNVLIS YWQKDSRLAY PKNSNLPTVM DFPLMEEMNK AFDEETTEWN GGLFRLYEYL
SQDIVYSHPM SLLTFLDNHD TSRFYRSEAD TKNLDRYKQA LTFLLTTRGI PQIYYGTEIL
MAADKANGDG LLRCDFPGGW PNDTKNCFDA ANRTPQQNEA FSFMQKLLQW RKGNEVIAKG
QLKHFAPNKG VYVYERKYGD KSVVVFLNGN DREQTIDLVP YQEILPASSA FDLLTEKKVE
LRNELTLPSR EIYLLSF
