ID E8N2S8_ANATU Unreviewed; 1710 AA.
AC E8N2S8;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Putative amylopullulanase {ECO:0000313|EMBL:BAJ65078.1};
DE EC=3.2.1.1 {ECO:0000313|EMBL:BAJ65078.1};
DE EC=3.2.1.41 {ECO:0000313|EMBL:BAJ65078.1};
GN OrderedLocusNames=ANT_30520 {ECO:0000313|EMBL:BAJ65078.1};
OS Anaerolinea thermophila (strain DSM 14523 / JCM 11388 / NBRC 100420 /
OS UNI-1).
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Anaerolinea.
OX NCBI_TaxID=926569 {ECO:0000313|EMBL:BAJ65078.1, ECO:0000313|Proteomes:UP000008922};
RN [1] {ECO:0000313|EMBL:BAJ65078.1, ECO:0000313|Proteomes:UP000008922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14523 / JCM 11388 / NBRC 100420 / UNI-1
RC {ECO:0000313|Proteomes:UP000008922};
RA Narita-Yamada S., Kishi E., Watanabe Y., Takasaki K., Ankai A., Oguchi A.,
RA Fukui S., Takahashi M., Yashiro I., Hosoyama A., Sekiguchi Y., Hanada S.,
RA Fujita N.;
RT "Whole genome sequence of Anaerolinea thermophila UNI-1.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AP012029; BAJ65078.1; -; Genomic_DNA.
DR RefSeq; WP_013561419.1; NC_014960.1.
DR STRING; 926569.ANT_30520; -.
DR GeneID; 78351299; -.
DR KEGG; atm:ANT_30520; -.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG4733; Bacteria.
DR HOGENOM; CLU_002894_0_0_0; -.
DR InParanoid; E8N2S8; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000008922; Chromosome.
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; cd11338; AmyAc_CMD; 1.
DR CDD; cd02857; E_set_CDase_PDE_N; 1.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.1220; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 8.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR014755; Cu-Rt/internalin_Ig-like.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004185; Glyco_hydro_13_lg-like_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 InterPro; IPR032091; Malt_amylase_C.
DR InterPro; IPR032812; SbsA_Ig.
DR NCBIfam; NF041940; choice_anch_X; 2.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF234; INTRACELLULAR MALTOGENIC AMYLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02903; Alpha-amylase_N; 1.
DR Pfam; PF13205; Big_5; 1.
DR Pfam; PF16657; Malt_amylase_C; 1.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SMART; SM01065; CBM_2; 1.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 1.
DR PROSITE; PS50853; FN3; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000313|EMBL:BAJ65078.1};
KW Hydrolase {ECO:0000313|EMBL:BAJ65078.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008922};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1710
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003228627"
FT DOMAIN 1392..1487
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1483..1596
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
SQ SEQUENCE 1710 AA; 185623 MW; A395C34DF157D6EB CRC64;
MRNSVLRTVL SLFILLNLLL VPAGVQPVTA APAAAPAVSW CAAGTFNGWN NTGQPLYDDG
THGDLLAGDG VYSVALTPAA GDYFWKAVEC GNWDNSYPAG NDSWFTADGT SPVVLTFDTN
NHASDAGWAL TPARNIVNVL GGVLPASFTV VGHFQGWNNA NPDTVMTPLG RGLYRLAYTF
TESGTTEVKI TETGSWARQY TVNGRQTDGG TLVLNYTAGQ TYIFLLDTNT GRWGAFLNGS
STGDWCAAGD FNGWNNAGLP MVDDGTQGDL LGGDGIFSAE VTVATAGRYE WKAFHCGTWN
GVPNANSWFH TSSDGQKVIF TLDTNDHASD AGAKLLPAQN IVNVLGDTLP ASLNVVGSFQ
GWNPSDVNYT MQKVGNWAVL VKPLAKGTYE GKITSTGNWD AFGADGRNVN AANVAFQVFA
NNDPVTFLLD TVSGRMLIYA PVSAQAAHDN EIWGGDLYHD SRSTFYRTPG GPVPAGTAVT
LRFRAAKNDL TGVQVRVYND RTNTQTLLNM TRITEDDRYE YWEVTLPASS DPTVFWYRFI
AMDGTARAYY EDDPSRDGGV GQTFASSPDN SWQVSVYDPA FQTPDWAKHA IIYQIFPDRF
RDGNTANNKP AGTFFYNEPG GTVFRSLDPE GDWNTPVCDP RASGACQGTY SKNFYGGDLQ
GLIDQLDYLQ SLGITAIYLN PIFESPSNHG YDTTDYGKIN PFLGDLPTFQ TLVTEAHNRN
IRIILDGVFN HTSSDSIYFD RYGRYETVGA CESPSSPYRS WYFFTDVTPG TGVCAGSDGT
PNAATYRSWW GYDSLPILNS ANPQVRQFIW NALTTDPIAK YWMQWADGWR LDVAGDIDQG
TINSPENDYW EGFRQAVHAV KPDAYIIGEE WGNATSWILG GEWDAVMNYQ FSTAVLGFWR
DEPFVDNDHN SASSAGIIQP LTPSQLDARL KNLAERYPPE ALYAMMNLLG SHDTNRALFM
LDHNTDQNNP TLYQNPNYDW SDAITRLKGV ALLQMTLPGA PTIYYGDEIG LVGPVAYDGS
TWQDDPYNRQ PYPWLDETGT PFYAHLQSTT ARQDLFNYYA ALINARKSYD ALSIGDFRTL
LTDDANGVYA FGRKSAASAA VVVLNRSTSP RNVVLDLSGY LPAGKQFSEV LSGANYTVAA
NGTLTLSSVP ARGGMVLVAT LSETAPAAVS DLHVTAEGDG TVSLAWSAVS GAGRYDIYRS
LVSGGGYQKV GETASTTFTD TGLTNATRYY YVVVAVDTTT LLQSGYSNEA MGLPHLNIGW
ANLQWPPSII HTIGTTPTQY IYGQVWINGV TSQPGATPGL LAQVGYGPDG SDPSAGTGWI
WVNAEFNDDA GNNDEFRGQL LPEAVGTFDY AYRYSTDGGN TWLYADLDGT GNGYDPAQAG
ALTVNASSDT EAPTAPTLSI VHWTPTSIHL SWMASTDNAA VYAYDIYRSL TSGGAGEKIA
RVLAPATTYV DTSVVAGTTY YYTVKALDTS FNASPLSNEA GQKAEGRLVE VTFNVTVPSF
TTGTVYFTRA INSDGTVGDW NAAAVPLTQV DATHWRLVAN LLDGQTVEFK FTRGSWDTVI
KGANGNEELS NLSLTVTHDQ TTGKQTFDYT VQNWRDPLIT AFTPADASSH ASAPAITWTW
SQAINPADLK GTLERKVGTN WVPVAGTVTY DSGTLTCTFT PAQALPYNTQ YRVTVSGQVD
AGNDVQQVTY QWQFTIQPFV LYFPQVYRAP
//
