ID U5VVX2_9ACTN Unreviewed; 551 AA.
AC U5VVX2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN ORFNames=AFR_13355 {ECO:0000313|EMBL:AGZ40957.1};
OS Actinoplanes friuliensis DSM 7358.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ40957.1, ECO:0000313|Proteomes:UP000017746};
RN [1] {ECO:0000313|EMBL:AGZ40957.1, ECO:0000313|Proteomes:UP000017746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ40957.1,
RC ECO:0000313|Proteomes:UP000017746};
RX PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL J. Biotechnol. 178:41-42(2014).
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}.
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DR EMBL; CP006272; AGZ40957.1; -; Genomic_DNA.
DR AlphaFoldDB; U5VVX2; -.
DR STRING; 1246995.AFR_13355; -.
DR KEGG; afs:AFR_13355; -.
DR PATRIC; fig|1246995.3.peg.2712; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_006462_2_1_11; -.
DR Proteomes; UP000017746; Chromosome.
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; 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; IPR045857; O16G_dom_2.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF219; MALTOSE ALPHA-D-GLUCOSYLTRANSFERASE; 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:UP000017746}.
FT DOMAIN 18..421
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 551 AA; 63400 MW; 335BC3893F27BAC4 CRC64;
MTVAERWYRN GVIYNFDVRA FQDSNGDGVG DLRGLISRID YLGRLGVTTL WLSPVHPSPW
RDGGYDVTDH YNIDPALGSL GDFAELMNVA DERGLRIMLD LVLNHTSDEH PWFRSACSDP
RSQYRDWYVW SEQEPPDRSE GMVFPGVQKT TWTYSDRAGA WYHHRFYDFQ PDLNIANPDV
REELAKIVSF WERLGVSGFR IDAAPFVIER TEPGGDPENR DYSVLTELRE RMSWRRGDAV
FLAEANVPND DLIRFFGNAD GAANRLQMLF AFRLNEALML SLARQDSGAV AEALVKLPRL
PRHGQWATFL RNHDEVDLSQ LLECEREEVL TAFGPERRHQ LYGRGIRRRL ATMLGGSQRR
LRMANSLQFT MPGTPVLRYG DEIGMGEDLR LPERDAIRTP MQWSATTNAG FSTAAAHDLV
RPVISDGSFS YERINVTDQR RDPDSLLVWF ERMLHTRHEC GEIGIGDHQL IRVEPSHVFV
HRADAPRGSI VFLHNLGDRP ARINLPLQPD ETTEPVEVFS DREYPDLDLR DLELDGFGYR
WIRLRRSHLR H
//
