ID E3D7L7_GARV3 Unreviewed; 2014 AA.
AC E3D7L7;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 83.
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 Name=pulA {ECO:0000313|EMBL:ADP39309.1};
GN OrderedLocusNames=HMPREF0421_21227 {ECO:0000313|EMBL:ADP39309.1};
OS Gardnerella vaginalis (strain ATCC 14019 / 317).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Gardnerella.
OX NCBI_TaxID=525284 {ECO:0000313|EMBL:ADP39309.1, ECO:0000313|Proteomes:UP000001453};
RN [1] {ECO:0000313|EMBL:ADP39309.1, ECO:0000313|Proteomes:UP000001453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14019 / 317 {ECO:0000313|Proteomes:UP000001453};
RX PubMed=20865041; DOI=10.1371/journal.pone.0012411;
RA Yeoman C.J., Yildirim S., Thomas S.M., Durkin A.S., Torralba M., Sutton G.,
RA Buhay C.J., Ding Y., Dugan-Rocha S.P., Muzny D.M., Qin X., Gibbs R.A.,
RA Leigh S.R., Stumpf R., White B.A., Highlander S.K., Nelson K.E.,
RA Wilson B.A.;
RT "Comparative genomics of Gardnerella vaginalis strains reveals substantial
RT differences in metabolic and virulence potential.";
RL PLoS ONE 5:E12411-E12411(2010).
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; CP002104; ADP39309.1; -; Genomic_DNA.
DR RefSeq; YP_003986332.1; NC_014644.1.
DR CAZy; CBM25; Carbohydrate-Binding Module Family 25.
DR CAZy; CBM41; Carbohydrate-Binding Module Family 41.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; gvg:HMPREF0421_21227; -.
DR PATRIC; fig|525284.18.peg.1208; -.
DR HOGENOM; CLU_001641_0_0_11; -.
DR OrthoDB; 9763188at2; -.
DR Proteomes; UP000001453; 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; 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 Glycosidase {ECO:0000313|EMBL:ADP39309.1};
KW Hydrolase {ECO:0000313|EMBL:ADP39309.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..2014
FT /note="1,4-alpha-D-glucan glucanohydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003167487"
FT TRANSMEM 1990..2009
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 57..414
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 423..502
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
FT DOMAIN 527..611
FT /note="Carbohydrate binding module family 25"
FT /evidence="ECO:0000259|SMART:SM01066"
FT REGION 504..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1654..1861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1662..1681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1682..1730
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1731..1754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1766..1814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1815..1829
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1830..1861
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2014 AA; 220043 MW; BFD5C02D8FB57051 CRC64;
MQMVAHRHLA SKIVSMIAAS AMLITGFAVV GNASASSESS SESSNPQSSN LTLNRKGVIV
TAFQQNWKSI AQECKTTYGP EGVKYVQVSP PNEHVKGTQW WTSYQPVSYK LKSKLGTENE
FKSMIDTCKV AGVGIIADAV INHMTGAGDT HTEGVGGSQY SAAKEDFPDA GYKKDDFHQD
ARNIEHYNNA EEVWNRRLVG LLDLDTSKQH VRETLGKYFA NLLKLGVAGF RIDAVKHISP
TDMAAIKKAA ADAAHTTPDK IWWMQETIGD PSEAKEIQPD QHLKEGEVNE FQYSYRLKSN
FYGSISNLKN ITNGLVPSDK ASIFVTNWDT PRENYVRTLT YKDGPRYELA NAFMLGYPYG
NPNIYSGYRF DAKNKDDGAP GATETSVPNV DCSPTTGWQC TQRWTSIRGM VGFFNAVNGA
QVTNWQESDN NNIAFSRAGK GFLAINNTPN AKKVLYTTDL PNGEYCNVYA AGNCSKTVKV
TDGKVAATIA PYSAIALHVD SKADSASKAG PARDESDPKY NVDDAKDQST TVYFNAKNKA
GNPSSVNIHY QIGNGSWTAV PGRPMRKVCD GWFARTIPNN GKQITAVFND GGSNWYNKNN
QSGANFEIQA GSKTYVVDAD LKGSESASIP CKVEDTSSKP TELKTKIVIH YKQKYGDNRH
MGVYIWGLKN ADGQEIKGAW HEFNGQDAFG KTYAVEADGT YESGKVGFII TEKPVDGQDW
HKDGGDRNIW QIEDGVGEAW VYGGDSNTFA EPPSEVSNKL NSIKTLNVTV HYRRTNKDYA
GWNLWTWCGS EKGVKQDFTA HDDFGKIAEY TFHNDSGIKD SKFIVRYSMQ GNDWVSKDPG
EGDRPIPAKA ITLSEDGNTG NAEIWLMQGD SRVYLSPNVI NTKANAINAD ITSFKEFTVN
VSGDPSEVEK KNVTVTDVTD SKKNQHKTID ISQVAVVDNR IVITAKNELD LKKMYEINIK
GVGGMPKTVS ASTVKGSKIV RTDEFDQKYA YTGDDLGAVV KDGSTTFKLW APTAAKVELV
TYKSTDEKAQ EDKKQDMTLG TEDGKLGVWS ITTSYAKAGT AYTYKVYFAD GTVNNSPDPY
AKAAVRNGMR SVVFGGNMAT PVSRKASFGK RPTDATIAEM NIRDFSIHES SGVDVAKRGK
YLGVIQSGAK KDGKPTGFDY LKSLGITHVQ IMPMYDFGSV NEAGDLSYVD KNDKDNPHQN
WGYDPINYNV PEGSYASDSA NPATRITELK QMVEGLHKAG LRVIMDVVYN HVYNAEKNAF
GQTVPGYYFR YNDDGSLSNR SGCGNDTASE RKMMRKYIVD SVKYWAKEYG IDGFRFDLMG
LIDLETIKEV REAVHAIDPN SIILGEGWDM SQLPYGNRTI QPNAYKLAEN NGVAFFNDSF
RDAVKGQGDD DVAGFVSGNR GSDNLVMQNL YGCQPGNASC TGRRYANAGQ TVQYVEAHDN
LNLYDKLKKS LPNETEENLK KRVMLANSLV MFAHGMPFFE LGQEFLRSKN GNANSYNAGD
GDNSVKWDLV KTNEDAVEYF KALIKLRNEI PALRDSEYSD VNNNMHWIKS SDGINAFSVD
NNGKTYVFIF NANSGEFTVN IGKGKYRVRI ADGKANSNDE SVCPEASVDD NGNYKVSALS
TSVLVKDAEK KNDNPFANIN VDDVLKYKMN PLDINKLKDG SKPGTQKPNP STPGHEQTPG
TVTPSPQPPV PGPVVPNPAP APGPHPQPGS NPVNPAPQPA PVPTPTPGET HPGTHEPNSS
TPGREQTPGD SDTENHPAPH TLVPDVGTAP SNSESGSASQ QGSKSNTPAH EPNNSIESKP
NAESHSTSEY QTHSKPKQNV HENSDQSKPA KTKPESSSNS AVSAPAKPSS AAPTPTAPAT
VQQLKSELRG TLLVRDNNVA NAGIVNKVNI RIQNGEFIER LNREGIAYAY AYIYSSPRLL
KGSDGSKYVT VRMVNGVPQF DAIFPAGYSG KHTVLLVDES GKQIAWTEVT VVDNGVSKRG
GSMLQTGSNI VYTFALFIIL TFVAAIARYK VAFR
//
