ID A0A1G7E7V5_9ACTO Unreviewed; 1719 AA.
AC A0A1G7E7V5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=SAMN05421878_11541 {ECO:0000313|EMBL:SDE59709.1};
OS Actinobaculum suis.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinobaculum.
OX NCBI_TaxID=1657 {ECO:0000313|EMBL:SDE59709.1, ECO:0000313|Proteomes:UP000182744};
RN [1] {ECO:0000313|Proteomes:UP000182744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20639 {ECO:0000313|Proteomes:UP000182744};
RA Varghese N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FNAU01000015; SDE59709.1; -; Genomic_DNA.
DR Proteomes; UP000182744; Unassembled WGS sequence.
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; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
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; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000182744}.
FT DOMAIN 127..483
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 492..571
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
FT DOMAIN 603..680
FT /note="Carbohydrate binding module family 25"
FT /evidence="ECO:0000259|SMART:SM01066"
FT REGION 65..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1676..1704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1719 AA; 182115 MW; 0F768C9A2EDD6FCF CRC64;
MARNLKDESV DGKNMGLQNL RLHIRRAVAW LGALILALSG LGIAAFAGPL AQAAPETPAD
IASETPAVTA SETPADTTAD TTVDTPAGAL PEKPAETPPG IPADTTAEMP SGTAPAAAGE
APVGRSGVVV TLFQHPWNSV AKECTQTLGP AGVAYVQVSP PQETIKGSAW WTSYQPVSYQ
LESKLGTAAE FQQMINTCRA AGVGVIVDAV INHTTGVDRE AGTGIAGSSF DAAGNYPQAG
YGPEDFHKCT ENISDYRNAE NVWNCRLSGL QDLDTGSEKV RDRLGQYFAD LLGMGVAGFR
VDAVKHMSPE DVAAIKEKAA EKVEVPASRI WWMQEVIGNP GEAPQIQPSK YTGSGEVTEF
SFAYQLRQRF KGSLQGGERK LSDIASGLVP SQQATVFVDN WDTERGEATL SYKDGRMYQL
ANAFLLGYGY GTPNVYSGYQ FTDADAGAPG ASETAVPETS CGPGSGWNCT QRWTAIRGMI
AFHNATAGEP VQNWQDDGDN NIAFERGQQG FLALNNTAQP AAVSYHTSLP NGTYCNVYAA
GDCSQTVAVK DGKIATEIQP RSAVALIAGV QPGSDHPAAR GAASDPADPQ LPPESNTPAG
PADPETTIFY KPESTWTAPY LHYGRGDAWT QVPGQPMQKV GDGWYSLRIN TAQATEFVFN
NGAGVWDNPA GGGNYRVEPG TTYAAVADKQ LSFTNPVPPQ YEPKTRVIVH YAPAAGDTAG
AQRGVYLWGN DKEGNTLAGK HYQFTGEDSF GKVFETEIPG AYEPGKLGFI VTTPAWDKDG
GDRMLDASSG TAEVWITGGS DTTATQAPAQ YQKRPAVLDV KVHYLRPAGD YQDWDLWTWA
EGLNGSSRPF NSHDDWGKLA TFRLESGSGI ASPSFIVREG ADAWKSKDPG EGDRVIPQSA
ITITDPGGNG TNSKGEAEIW LVSGDWTVYT NPSVINTKRG LVKAEISGLS QITARLAGPV
DPAALTPQTV QVAGAQVANV ELAADKSAVV ITTAQPLDVA AAYQVSAPEY GEVTASAGAV
VRTPEFDAAY AYSGALGAQY EKTGTTFALW APTAAQVHVR LYKTTDREAP LATEHALTRG
EKGVWQVRLP GDLDGTAYDF RVTFANGTEN LSPDPYAHAA VENGMRSVVL SPESASRGAQ
GERMPAFGPA TNASIAEMNI RDFSIQPDSG ISAAKRGKYL GVVEGGTQAK TGNPSGLDYL
KQLGVTHVQI MPFYDFGSVD ESGDLGYAAA QHGQQNWGYD PENYNVPEGS YASDPADPKA
RLAEAKQMVA GLHKAGLRVI MDVVYNHVYN PEKHAFNLTV PGYYFRYDAA GKLVNNSGVG
NDTASERAMM RKYIVDSVVY WATEYGVDGF RFDLMGLHDV ETMREVRAAL NQIDPSIIVL
GEGWDMNRTL PKDAMAIQPN AGKLAPGAVG ADDNGVAFFN DSIRDGLKGS VFEASDTGFV
SGKSGQETLI ANNVLGCQKP EGLSPCTNGN ANTGYAAPGQ IVNYVEIHDN LTLFDKLLAS
RPDDSEQTRA ARAKLANSTV YLAQGIPAAQ LGQEFLRTKG GDENSYNSGD GPNAIDWSRA
HEQADSVAYT RGLLALRQSA PAFRYPTFEQ VNANSKLLRA ADGVVAWTVR DTEHSYVVVL
NSTDAAVPVD IPAGTYDLLV ANGKVELSAP QTVTIGETPY AAGALSATVL RLHTDNAGEP
GAEDADQTGA EDAGQAGAED AGQTGAEGTG IALVLLTLD
//
