ID C0BRQ7_9BIFI Unreviewed; 1010 AA.
AC C0BRQ7;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN ORFNames=BIFPSEUDO_03321 {ECO:0000313|EMBL:EEG71351.1};
OS Bifidobacterium pseudocatenulatum DSM 20438 = JCM 1200 = LMG 10505.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=547043 {ECO:0000313|EMBL:EEG71351.1, ECO:0000313|Proteomes:UP000003875};
RN [1] {ECO:0000313|EMBL:EEG71351.1, ECO:0000313|Proteomes:UP000003875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20438 {ECO:0000313|EMBL:EEG71351.1,
RC ECO:0000313|Proteomes:UP000003875};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bifidobacterium pseudocatenulatum (DSM 20438).";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEG71351.1, ECO:0000313|Proteomes:UP000003875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20438 {ECO:0000313|EMBL:EEG71351.1,
RC ECO:0000313|Proteomes:UP000003875};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2009) 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEG71351.1}.
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DR EMBL; ABXX02000002; EEG71351.1; -; Genomic_DNA.
DR RefSeq; WP_004221262.1; NZ_JGZF01000003.1.
DR AlphaFoldDB; C0BRQ7; -.
DR KEGG; bpsc:BBPC_1479; -.
DR PATRIC; fig|547043.19.peg.1539; -.
DR eggNOG; COG0366; Bacteria.
DR Proteomes; UP000003875; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0043169; F:cation binding; IEA:InterPro.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11315; AmyAc_bac1_AmyA; 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; 3.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR031965; CBM26.
DR InterPro; IPR002044; CBM_fam20.
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 PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF16738; CBM26; 1.
DR Pfam; PF00686; CBM_20; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..44
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 45..1010
FT /note="alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009949465"
FT DOMAIN 76..426
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1010 AA; 107353 MW; 809AABE4A67F126C CRC64;
MKHRKPTPAW QKLGLRVSKK LAVGATALAT VFGGLAVASV SAQASTDRNS YADTVGNPTF
EAARKKYGLT KEMKNGAILH AWMWSFNTIT EHMDEIAEAG YTSIQTEPMS KIKVNDANGK
KFTENWYYVY QPTNTSIGNF VVGSEDDLKA MTVAAHAHGI RIIVDVVANH FTADWNAIDS
DWQKSEYFHA RNSCSGSGGD NIDYSNRWQV THCHLLGLWD LNTANPEVAN RMHDFLKTAV
NDGVDGFRFD AGKHVELPNE FDGSQYWTTI LQNGSQYQYG EVLQGDSGLD YKAYANLYAK
YGEGGGGATA SDYGKTIRSA LWSKNLNAGN LMSLRNGGVN DDQLVTWVES HDNYANSDKE
STYLTNDQIR FGWAVVGARA GGAPLFFNRP KASGGNQPQF AEASQLGDAG DDMWKDTAVA
AVNHFRNAMD GEAEYLRNCG SEQNNNSCLM VERYKTDNNA GNDGVSIANM GGDQNLAGTP
TKLDDGTYTD QVNGGTITVS NGKITSGTAK GDAVSVYFNT SVKESVSATV SKKFSSNTIK
VTLNASNATN LTYSLSNGKN GSFVDGDSLT IGGDMEIGDS VTLTVKGTGA ESGEALEFTA
TYTKVEVQAN TIYATKPSGW SKMYAYVYTG DGATAKNNAA WPGVEMTAMA AADSCAKAGT
YKYEVPDLGE GTYRVIFSNG NGSQMPGASQ PGFEFSGKVS WDGSSASLTA ITCTATPPVI
KTADITFSAT ADLKTGETLY AVGDWGQGKG KTWTRAGGVK LAKNGNAYTG TTTMTKGQAI
TARLIKVDAN GKTTWDEIGD VKATADKTKT VDLKWTNAVE NTVDITINAA ADLKTGETLY
AVGDWGQGKG KTWTRAGGVK LARYGNAYTG TTKVGKGNAI TFRLIKVDAN GKTTWDSAKD
RKSKADKTKA LGVSWTSGKV NEDGTIPDDS AISISGKGVA DGKLSIQKGN LAELYVIGTQ
DATPSDAVWW SDGAAVAVSG TGTVYGVQTG TAKVNVKVGN QTATITITIK
//
