ID A0A1Q5N0L4_9ACTN Unreviewed; 1192 AA.
AC A0A1Q5N0L4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN ORFNames=AMK09_15505 {ECO:0000313|EMBL:OKK20024.1};
OS Streptomyces sp. CB02488.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703920 {ECO:0000313|EMBL:OKK20024.1, ECO:0000313|Proteomes:UP000186200};
RN [1] {ECO:0000313|EMBL:OKK20024.1, ECO:0000313|Proteomes:UP000186200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02488 {ECO:0000313|EMBL:OKK20024.1,
RC ECO:0000313|Proteomes:UP000186200};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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 -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
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:OKK20024.1}.
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DR EMBL; LIVO01000005; OKK20024.1; -; Genomic_DNA.
DR RefSeq; WP_073735377.1; NZ_LIVO01000005.1.
DR AlphaFoldDB; A0A1Q5N0L4; -.
DR STRING; 1703920.AMK09_15505; -.
DR OrthoDB; 9813435at2; -.
DR Proteomes; UP000186200; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07481; Peptidases_S8_BacillopeptidaseF-like; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 3.
DR Gene3D; 2.60.120.430; Galactose-binding lectin; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR033857; Bacillopeptidase_F.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR021720; Malectin_dom.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF13620; CarboxypepD_reg; 2.
DR Pfam; PF11721; Malectin; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 2.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000186200};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1192
FT /note="alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013338827"
FT DOMAIN 187..471
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 1034..1183
FT /note="Malectin"
FT /evidence="ECO:0000259|Pfam:PF11721"
FT ACT_SITE 196
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 243
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 415
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1192 AA; 123225 MW; 14CF2BA0DBDF0085 CRC64;
MNRRRPRWQG LFAAALATAV GAPFLGALPA AAADPGPKPA ALLRKADGQV LKALGSKDRV
SFWVQLDSQA DTSAARKAKK KADKDRAVIE AKTAHADRSQ KALRALLKNA GAHYTPYWIS
NTIEVTGDKG LAEKIAARPE VASIRADEAV KLPVPLNATT EPKVNGVEWN IDRINAPKVW
DEFGVRGEGV VIGSIDTGVD YRHPALVASY RGLKADGSYD HSYNWFDAVG TCAGDAPCDD
YGHGTHTVGS MVGDDGNGNA IGVAPGASWI AAKGCGTESC PQSALLAAGQ WMLAPTDADG
ENPRPDLAPD VINNSWGADS LDTWYQAMVQ GWRDAGIFPA FSNGNSGPSC DTAGSPGAYN
NTYSSGALDS SDRIADFSAR GPGVDGRVKP DIAAPGVNIR SAAPGGGYVA KSGTSMASPH
TAATVALIWS AAPSLRGDVA ATEALLNDAA TDVDATSCGG TAEFNNIYGH GRLDAYAAVS
AAPRTNVGAL TGTVTADGEP AAEIQVDVDG PMHASVHTKT DGTYSLPRLV AGDYRVTVSK
FGYVTVTADV TVAEDATVTH DAALTTAPTG TVTGTVTSAS GPEADVTVKV QGTPVRVETG
ADGRYTLTVP VGSYQFGVTP LNHCAAAVGV AVAVAKGANS RNVALASRAD VFGTTCRQTT
EAYPAGDTRL TLNPPTGSYA PVTLPFPVAL YGHTYDKGWV TRDGQLVFGS LYMGDNGGLP
STSGANGALS PFWDQLATDA SSGVYTSVRG SAPHREYVVE WRDMLLARDP SQRIGFAATI
SEDGTYTFHY KDIGDGAFEH GGGATIGAEN HDGTDAFLYS LNERSLRDGT AIRFRPEGHA
VVSGTVTDAN DGKPVSGATV AVTRSGTAVD TVTTRADGSY LTQIPAATAV SHRISVTAPH
YMTGNSTFTL QSLSAVGTAT ALRTGAVSYE TDADQQLIMT AGERRTRTLT LTNSGAPAAY
TVAEKNGAAW LKVSSASGSL ATGAGKAVTL TFDTTAATPG TVLTGTLVIA SESGRAPSLS
LPLKVVVPAY RTGIDVGADT ASVDGAGDTW SPDLGYADGS YGYVGRATTP TYTRKDIAGA
AGSRQQQLLR SGRQGVTEYR FDAVPNGTYE VELGFAEPAA MKPGQRVFDV TAEGAEKVPD
IDVRLESGGV RTALAKTFTV KVTDGGLEVG LSAIRGDTLI NSIRVTQRPD LI
//
