ID Q1IXJ3_DEIGD Unreviewed; 1021 AA.
AC Q1IXJ3;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Alpha amylase, catalytic region {ECO:0000313|EMBL:ABF46041.1};
GN OrderedLocusNames=Dgeo_1746 {ECO:0000313|EMBL:ABF46041.1};
OS Deinococcus geothermalis (strain DSM 11300 / AG-3a).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=319795 {ECO:0000313|EMBL:ABF46041.1, ECO:0000313|Proteomes:UP000002431};
RN [1] {ECO:0000313|Proteomes:UP000002431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11300 / AG-3a {ECO:0000313|Proteomes:UP000002431};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J.,
RA Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.;
RT "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000359; ABF46041.1; -; Genomic_DNA.
DR RefSeq; WP_011530872.1; NC_008025.1.
DR AlphaFoldDB; Q1IXJ3; -.
DR STRING; 319795.Dgeo_1746; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; dge:Dgeo_1746; -.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG3391; Bacteria.
DR HOGENOM; CLU_293507_0_0_0; -.
DR Proteomes; UP000002431; Chromosome.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro.
DR GO; GO:0043169; F:cation binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.1190; -; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 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; IPR006046; Alpha_amylase.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
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; PF13620; CarboxypepD_reg; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR SUPFAM; SSF49344; CBD9-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002431};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1021
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004191907"
FT DOMAIN 540..635
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 54..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1021 AA; 109266 MW; AD075EECB9953773 CRC64;
MKRFQKVGRS GALAVLTLAL SACGVLKAPE TGGNTRAWQD EVIYFAMTDR FANGNPANDN
GPNRNEGDRA DRTNPLGWHG GDFAGLKAKI EEGYFKRMGF TALWISPVVL QVPAIEGPKT
GPNAGKLFAG YHGYWAEDFF KVDPHFGTLD EYKSLIQTAH RNGIKVIQDI VVNHAGYGAT
LTKTNPDWFH TQAECDASTN KRVDCPLAGL PDFKQERPEV TTYLNDFVNS WRKETGIDGL
RIDTMQHVPD SYWQQFFAAG GPGDPSKIWS VGEVFNGDPA FLAHYMDDLG SPSVFDFALY
FAIKDGLSSA RGDLGRLADV FARDGAYRDP TRLTTFVDNH DVPRFVSEVQ ERGGTAAQAN
ERLDLALSLI YTSRGTPSVY QGTEIAQPGL GDPYNYATGQ GNREDMNFGA LSQSSIDERL
AALAAARAKY RALTHGVQQE LWRPNGGAPI FAYRRIVTDG QGGQPVVVVI NNGDTPVDLS
TLSGGGIPLL GTFSGTALTE ITGRTSDLSV SGGQLVGTVP ARSALAVTAP AGSGSTGTVN
PRLPEVTDLS AKAGDSAVQL TWTASTDLNV TGCRVYARTG SGQERLLNFA PLPKDQTTYL
AAGIPNDQET TFRVVTVDAQ GAESRGVSVK ATLSSKNTVR VTFTVDARSQ GNGPIELRRF
DTGSQLEYPM TQVSRGIWKT AIDLPLFREI KFKFGNDGPA AKNSGYEAPG QPDRSYVVGT
NPNVYTGTYD FITQPVPQTT IEGQVRGAGN PLANALVEAV TANPDLHYAM TFPDGTYTLF
VPAGTHTLQA KAGGYVAASR QAISPGTGAD FNLAQDLSTK YTIDGNLADW TAPKVTLQSP
TEGGFGPDNN WLTLQADSDD HYLYLAYTYR VKGNSAILYL DTKMGGAAQA DNFEAWKRAA
TFSGSMGGAD AFVARYENQM AQLRLVQSDT ATPEVNTGDY KFAASGTLPE QTVELAIPWT
ALGLSEKPAN GVNVVGGIFG GDGYGAGDIV PNTTSTPPGA NTIGTDAEQR RATFTQPLNV
R
//
