ID V9H6V8_9CLOT Unreviewed; 560 AA.
AC V9H6V8;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN ORFNames=CSBG_00730 {ECO:0000313|EMBL:EEH97104.2};
OS Clostridium sp. 7_2_43FAA.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=457396 {ECO:0000313|EMBL:EEH97104.2, ECO:0000313|Proteomes:UP000017809};
RN [1] {ECO:0000313|EMBL:EEH97104.2, ECO:0000313|Proteomes:UP000017809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7_2_43FAA {ECO:0000313|EMBL:EEH97104.2,
RC ECO:0000313|Proteomes:UP000017809};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Allen-Vercoe E., Strauss J.,
RA Ambrose C., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Clostridium sp. 7_2_43FAA.";
RL Submitted (JAN-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 -!- 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:EEH97104.2}.
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DR EMBL; ACDK02000035; EEH97104.2; -; Genomic_DNA.
DR RefSeq; WP_008680090.1; NZ_JH815222.1.
DR AlphaFoldDB; V9H6V8; -.
DR STRING; 457396.CSBG_00730; -.
DR GeneID; 65399909; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_006462_2_3_9; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000017809; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043169; F:cation binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11333; AmyAc_SI_OligoGlu_DGase; 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; IPR045857; O16G_dom_2.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF179; NEUTRAL AND BASIC AMINO ACID TRANSPORT PROTEIN RBAT; 1.
DR Pfam; PF00128; Alpha-amylase; 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 Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW Glycosidase {ECO:0000256|RuleBase:RU361134};
KW Hydrolase {ECO:0000256|RuleBase:RU361134};
KW Reference proteome {ECO:0000313|Proteomes:UP000017809}.
FT DOMAIN 13..417
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 560 AA; 65226 MW; AC9F453E4D62B2D9 CRC64;
MKKQWWQKEV VYQIYPKSFN DSNNDGIGDI KGITEKLDYL SDLGVTMLWI CPIYKSPMDD
NGYDISDYFD LAPEFGTMED LDELIEKAKE KGIKIILDLV INHTSDEHEW FMEAIRNPES
KYHNYYIFKD GKEVPNNWRS VFGGSVWEKV EGRDEYYFHA FGKKQPDLNW ENKEVRETLY
NMVNHWLEKG IAGFRIDAIT FIKKDLTYKD LEADGVDGLV KCTKASRNQP GIEEFLHELK
RETFDKYNCV TVAEAPGVSY DELGDFIGEN GYFSMIFDFK YADLDVASGS EWFKRIPWTI
KELREKIMAS QMAVQKYGWA ANFIENHDQP RSTTKYLLNE ASNEDAIKMM GAMYFLLRGT
PFIYQGQELG MTNFERTSIE EFNDISSIDQ YHRSIEEGFS KEEALKIVNL RSRDNSRAPF
PWNSSEYGGF SSKKPWLGMI ENYKEINAEA QVGQKGSIYE FYKDIINFRQ NSVHSDCLIY
GDIAPIDTKN DDLIAYTRHN NNETIYCYFN FSKKGVFEPL DMKDKKVIFN NLKDYEINEE
GIVLKPHQAL LVTINNMGEV
//
