ID A0A0A7I8K1_9BIFI Unreviewed; 1745 AA.
AC A0A0A7I8K1;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=1,4-alpha-D-glucan glucanohydrolase {ECO:0000256|ARBA:ARBA00030238};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.41 {ECO:0000256|ARBA:ARBA00024062};
DE AltName: Full=Alpha-dextrin endo-1,6-alpha-glucosidase {ECO:0000256|ARBA:ARBA00029618};
DE AltName: Full=Pullulan 6-glucanohydrolase {ECO:0000256|ARBA:ARBA00031076};
GN ORFNames=AH67_04975 {ECO:0000313|EMBL:AIZ16361.1};
OS Bifidobacterium pseudolongum PV8-2.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1447715 {ECO:0000313|EMBL:AIZ16361.1, ECO:0000313|Proteomes:UP000030636};
RN [1] {ECO:0000313|EMBL:AIZ16361.1, ECO:0000313|Proteomes:UP000030636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV8-2 {ECO:0000313|EMBL:AIZ16361.1,
RC ECO:0000313|Proteomes:UP000030636};
RX PubMed=25614573;
RA Vazquez-Gutierrez P., Lacroix C., Chassard C., Klumpp J., Stevens M.J.,
RA Jans C.;
RT "Bifidobacterium pseudolongum Strain PV8-2, Isolated from a Stool Sample of
RT an Anemic Kenyan Infant.";
RL Genome Announc. 3:0-0(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|ARBA:ARBA00000548};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan,
CC amylopectin and glycogen, and in the alpha- and beta-limit dextrins
CC of amylopectin and glycogen.; EC=3.2.1.41;
CC Evidence={ECO:0000256|ARBA:ARBA00023965};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR EMBL; CP007457; AIZ16361.1; -; Genomic_DNA.
DR STRING; 1447715.AH67_04975; -.
DR KEGG; bpsp:AH67_04975; -.
DR HOGENOM; CLU_001641_2_1_11; -.
DR OrthoDB; 9763188at2; -.
DR Proteomes; UP000030636; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051060; F:pullulanase activity; IEA:UniProtKB-EC.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR CDD; cd11341; AmyAc_Pullulanase_LD-like; 1.
DR CDD; cd10315; CBM41_pullulanase; 2.
DR CDD; cd02860; E_set_Pullulanase; 1.
DR Gene3D; 2.60.40.1110; -; 2.
DR Gene3D; 2.60.40.1220; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR005085; CBM25.
DR InterPro; IPR005323; CBM41_pullulanase.
DR InterPro; IPR014755; Cu-Rt/internalin_Ig-like.
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 InterPro; IPR011840; PulA_typeI.
DR NCBIfam; TIGR02104; pulA_typeI; 1.
DR PANTHER; PTHR43002; GLYCOGEN DEBRANCHING ENZYME; 1.
DR PANTHER; PTHR43002:SF11; PULLULANASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00128; Alpha-amylase; 2.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR Pfam; PF03423; CBM_25; 1.
DR Pfam; PF02922; CBM_48; 1.
DR Pfam; PF03714; PUD; 2.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SMART; SM01066; CBM_25; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 2.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030636};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 38..1745
FT /note="1,4-alpha-D-glucan glucanohydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002029495"
FT TRANSMEM 1720..1741
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 51..431
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 440..519
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
FT DOMAIN 548..626
FT /note="Carbohydrate binding module family 25"
FT /evidence="ECO:0000259|SMART:SM01066"
FT REGION 1650..1713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1659..1673
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1694..1713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1745 AA; 187442 MW; 51C9736C03094431 CRC64;
MVIQQVRDCM RRTTGIGVAI AMVGTGALLA VPMAANAAED TGQTTLPAKT DVQVIAFQQT
WNSIAKECTN TYGPQGVAYV EISPPQESIQ GTEWWTSYQP VSYKLDSKLG TEAEFKNMIT
TCDAAGVGII ADVVLNQTTG LDVAAGEQTG VAGTKYNGLT GDYPGFTGEN GQYPQGVTAA
DFHDYNNGAS VSDYKNQQEV QEGRLNSMWD FDTSSEKVQD IQSDYLAKLY KMGVKGFRMD
AVKHINNEDI KGIKDKMAQK VGKNANDIYW IQEVIGNASE APGIQPRNYL ETGTVTQFDY
KSDLNAKFKG KIAELKDLST RIGDLSANPN ALESANANVF VTNWDTARND GAITYKNDSM
YALANAFMLA YDYGTPRLLS DYKYDDNAAG APGATATAVP DVDFDQACST KDGDWNCQQR
WTTTRGMIAF HNYVDGTSVS DWQDDGANNI AFSRGDKGFV AINNSTEDKE AEYATSMPDG
EYCDVYAVQD CSKTVTVSGG KAKVTVPAMQ AVAIYGGATK ATHPASDVAV DPSTPDVVIP
DTTVKPDDQT TTVWYKPTNK WDKVFVHHGA GSDWTAVPGE EMEGPDAQGY YKKTIDTKGE
EHQICFNDGG SDWDSNNGSN YLIAKGITQV GVENGALSVG NPEAIGAQTR LVVHYKPAAD
EATANRGVYV WGKDIAGADM TAVNHPFTGE DCYGKVADLT FDGKFEDLGF IITTEDWNKF
GGDRNVTVSK TGTVEVWVDG AGDASETLTE APADYKCKAD KVDVTVHYMR NDGLYFNAAD
TETKVPQWDL WMWNSNSNGF ASKFTKHDDW GELATASFSN YTYQASNGES DFGLLRRYGA
DEWKKKDGSD GDIKMSADAL VFSNDGTAKA EVWLLQDDPT VYTARPALGA RISEAEIAQN
NAIDAKLTKP ADVKAEDVKV TDAKGNTVDI DAVKTDGAVV TVTLKDDLDL TAKYTVEIEG
FGSADAVAGS VVRTDAFDKE YAYDGDDLGA TWADDGTTFK LWAPTASKVE LVTFKDAKTA
DAEAADTIAM DRGEKGVWST TAKVADGTAY IYRVSFADGT VNDSADPYAR ASVVNGKRSV
VLSPAKTTVK DSGRMAPFSK NTDAVIAETH IRDLTKNENS GVDAAKRGKY LGMIQNGTKN
SAGKSTGVDY LKELGITHVQ IQPMFDYASV DETKPLDDSN YNWGYDPLNY NVPEGSYASD
PTDPANRVVE AKQMVNGLHA NGLRVIMDVV YNHVADAATN PFGLTVPGYY FRYQNGSLVN
NSGCGNDTAS ERAMMRKYIV DSVAYWAKEY NMDGFRFDLM GLHDVETMKQ VRSALDKIDP
SIIIVGEGWD MNTTMDKSAM SIQPNGYKLD TPNSTIAFFN DSIRDGLKGS VFSDEDNGFV
SGKQGMEPLI MNNMLGCRNL DGTAEGAFCT NGNANVKYAN AGQVVNYVEI HDNLTLNDKL
EKSLFVQGRN EGLDEAGQKA KVIETSKLAN SAVFMAFGIS EFQVGQEFLR TKGGDENSYK
SGDTVNAVDW DRMNDTDYGD HAQYVKDLIA IRKKTSALRV ESYEKISNST KELKAADNVV
AYEIARDNGT YVVALNAGDE AAAVPGVTAG DYGVLVSNGR TYLHPAQTVA LTDEADGVDA
SVAGAAIAVK DGQNVVVPAH SAVLLAPVAD LGQPDTPDQP DTPGQPTKPD TPVNPDEPGD
TDKPAAGEQP DGQTGGNAAG SQSSTGAEQQ VAGVASTGSA IALLVAVAVA FVAAGVGLLT
VRRRD
//
