ID A0A1M3EIG6_9CELL Unreviewed; 589 AA.
AC A0A1M3EIG6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN ORFNames=BGO38_05985 {ECO:0000313|EMBL:OJV58280.1};
OS Cellulomonas sp. 73-145.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1895739 {ECO:0000313|EMBL:OJV58280.1, ECO:0000313|Proteomes:UP000184491};
RN [1] {ECO:0000313|EMBL:OJV58280.1, ECO:0000313|Proteomes:UP000184491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=73-145 {ECO:0000313|EMBL:OJV58280.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-maltose = alpha,alpha-trehalose; Xref=Rhea:RHEA:15145,
CC ChEBI:CHEBI:16551, ChEBI:CHEBI:17306; EC=5.4.99.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001595};
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|RuleBase:RU361134};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. TreS
CC subfamily. {ECO:0000256|ARBA:ARBA00005496}.
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:OJV58280.1}.
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DR EMBL; MKTI01000009; OJV58280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3EIG6; -.
DR STRING; 1895739.BGO38_05985; -.
DR Proteomes; UP000184491; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0047471; F:maltose alpha-D-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11334; AmyAc_TreS; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR032091; Malt_amylase_C.
DR InterPro; IPR045857; O16G_dom_2.
DR InterPro; IPR012810; TreS/a-amylase_N.
DR NCBIfam; TIGR02456; treS_nterm; 1.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF219; MALTOSE ALPHA-D-GLUCOSYLTRANSFERASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF16657; Malt_amylase_C; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW Glycosidase {ECO:0000256|RuleBase:RU361134};
KW Hydrolase {ECO:0000256|RuleBase:RU361134};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transferase {ECO:0000313|EMBL:OJV58280.1}.
FT DOMAIN 57..457
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 589 AA; 66383 MW; 4F5C5B9B12F22924 CRC64;
MRPRGARGRA VTEPPPTTAA LALHGLPARR QPQVPAAELP GAPTPDSQWY RTAVFYEVML
RCFSDSRGEG SGDIQGLIQR LDYLQWLGID CLWLPPFYPS PLRDGGYDVA DYTAVAAQYG
SIADFTELVQ QTHARGMRIV VDLVMNHTSD QHPWFQASRA DPEGPYGDFY VWRDDNAGYP
DARIIFVDTE TSNWTFDPVR RQYFWHRFFS HQPDLNFENP RVAEAMLDVG RFWLNLGVDG
FRLDAVPYLF EAEGTNCENL PATHAFLRRV RRMLDEEFPG RIMLAEANQW PEDVVDYFGT
PEEPECHMCF HFPVMPRIFY ALRDQRATPI VDILADTPPI PAGGQWSTFL RNHDELTLEM
VSTEERASMY GWYAQDSRMR ANVGIRRRLA PLLDNSRKEI ELAHALLLSL PGSPCLYYGD
EIGMGDNIWL ADRDSVRTPM QWTPDRNAGF STVDPGKLYL PLVQSLVHHY AHVNVEAQLA
QPTSLLHWVK GMLAVRRRYP ALGMGEFTVV PCDNDSILAF LRRTPTQTVL VVANLASTAR
AARVTLPGAA GSALRDVFGG APFPAVGPDD ACTFTLGSRD FYWLEVVTP
//
