ID K9RHX1_9CYAN Unreviewed; 648 AA.
AC K9RHX1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN ORFNames=Riv7116_4699 {ECO:0000313|EMBL:AFY57116.1};
OS Rivularia sp. PCC 7116.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Rivulariaceae;
OC Rivularia.
OX NCBI_TaxID=373994 {ECO:0000313|EMBL:AFY57116.1, ECO:0000313|Proteomes:UP000010380};
RN [1] {ECO:0000313|EMBL:AFY57116.1, ECO:0000313|Proteomes:UP000010380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7116 {ECO:0000313|EMBL:AFY57116.1,
RC ECO:0000313|Proteomes:UP000010380};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Rivularia sp. PCC 7116.";
RL Submitted (AUG-2012) 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|RuleBase:RU361134};
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; CP003549; AFY57116.1; -; Genomic_DNA.
DR RefSeq; WP_015120675.1; NC_019678.1.
DR AlphaFoldDB; K9RHX1; -.
DR STRING; 373994.Riv7116_4699; -.
DR KEGG; riv:Riv7116_4699; -.
DR PATRIC; fig|373994.3.peg.5016; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_006462_7_3_3; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000010380; Chromosome.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd05467; CBM20; 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; 1.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR013784; Carb-bd-like_fold.
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; PTHR10357:SF215; ALPHA-AMYLASE 1; 1.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF00686; CBM_20; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 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, ECO:0000313|EMBL:AFY57116.1};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000256|RuleBase:RU361134};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000010380};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 540..644
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
SQ SEQUENCE 648 AA; 75465 MW; 64F11EADFC58BFE9 CRC64;
MVNTPPSRAS DSQYNIENPQ AEVEVIVETP DSNADIDLEF LYTRDIEFRQ ETIYFIVVDR
FHDGNPRNNK GFNEELYDPD RKEWGKYWGG DLQGIIDKLD YLRNMGVTAI WLTPLFEQVE
ELFIESAAIH GYWTKDFKRL NPRYIAADDE PSLNKTQDTK NTDFDRLIEE LHNRNMKLIL
DIVCNHSSPD TGGSKGELYD DGVKIADFND DKDNWYHHYG EVSDWENEWQ VQNCELSGLA
TFNENNVQYR SYIKSAIKQW LDRGVDALRV DTVKHMPIWF WQEFNSEMYN HKPDVFIFGE
WIYSRPDDAL SVEFANNSGM TILDFGLCMA LRQALGTNDE AGFYLVNDIL KQDYRYNGSR
ELITFIDNHD MHRFLSLNPD IDNLRLAVDF LMTSRGIPCL FYGTEQYLHN DTNADDNIYG
NNDPYNRPMM ENWDTETDIY WHVRKLSGLR RLNPAVSMGS QWEKYITPDV FCYVRRYNGS
RCFVALNRGY ALTIKEVDTE LPDREHTCVL TGRKFEVKDG KIYNLELSPK EAIVISHVGE
RLKAQTLVRA QLNGVQTQPG ERLVVIGDCP ELGNWDIKKA YPLEYINSNT WFAEIPFNES
AGKLISYKYV ILREAISPLR ENLLARRWVI ASEGTVKWRD TWASGRES
//
