ID K6YT49_9ALTE Unreviewed; 664 AA.
AC K6YT49;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00017303, ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN ORFNames=C427_1571 {ECO:0000313|EMBL:AGH43680.1};
OS Paraglaciecola psychrophila 170.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1129794 {ECO:0000313|EMBL:AGH43680.1, ECO:0000313|Proteomes:UP000011864};
RN [1] {ECO:0000313|EMBL:AGH43680.1, ECO:0000313|Proteomes:UP000011864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:AGH43680.1,
RC ECO:0000313|Proteomes:UP000011864};
RX PubMed=23640379;
RA Yin J., Chen J., Liu G., Yu Y., Song L., Wang X., Qu X.;
RT "Complete Genome Sequence of Glaciecola psychrophila Strain 170T.";
RL Genome Announc. 1:E00199-13(2013).
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 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; CP003837; AGH43680.1; -; Genomic_DNA.
DR AlphaFoldDB; K6YT49; -.
DR SMR; K6YT49; -.
DR STRING; 1129794.C427_1571; -.
DR KEGG; gps:C427_1571; -.
DR PATRIC; fig|1129794.4.peg.1557; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_013336_3_0_6; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000011864; Chromosome.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
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 PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 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|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000011864};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..664
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003900341"
FT DOMAIN 28..371
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 381..468
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
SQ SEQUENCE 664 AA; 72880 MW; 64F4C336FC0DFD63 CRC64;
MMKINKTLLA AVLGSTLLGQ PIVQAEPTTF VHLFEWSWLD VATECETFLG PKGFAAVQVS
PPNEHITTSQ WWARYQPVSY MLESRGGSRA EFIDMVQRCD AVGVDIYVDA IINHMAAGSG
TGTAGNSFGN KSYSIYSPQD FHTSCSIDNY SNRYQVQNCE LVGLADLDTD ATYVQDTIAA
FLSDLTNIGV KGFRLDASKH MPTEDISTIL SKVSGAPLIF QEVIDQGGEA ISAAEYASNG
LVTEFKYSVE IGNTFSNGNL AWLSNFGEGW GFMPSYQAVV FVDNHDNQRG HGGGGNVITY
EDGRLYDLAN VFMLAYPYGY PKLMSSYDYK GDTDVGGPSV PVHNNGTLEC FADKWKCEHR
YSYMSGGVDF RNNTTNHFAI SDWWDNGANQ IAFGRGSQGF VAINKETFGL NSNVATSMAQ
GQYCNVLKGE LSSDKLSCSG GVITVQPDGS INLDVPAFDA VAIHHNAKIQ GTSTPDDIQR
TVLFIQAQTQ GGQNMFVRGG IDHNYAASNL GLNCTSNNYV CAMPISHNNL NNTTTSSWKM
NDNFLDWYGI EAGQSTEAEG TALDWTTDIW PAAYGPLKTV ENDGYGQEPL NIWGPHHWML
DVEMDCSKTV NGWFELKAYI KNGQGWEGDI QQSNTPYSSN NHFAQCGKIN KFDFNNSNVE
IKDF
//
