ID Q9L036_STRCO Unreviewed; 993 AA. AC Q9L036; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 02-SEP-2026, entry version 135. DE SubName: Full=Secreted alpha-amylase {ECO:0000313|EMBL:CAB88152.1}; GN Name=aml {ECO:0000313|EMBL:CAB88152.1}; GN OrderedLocusNames=SCO7019 {ECO:0000313|EMBL:CAB88152.1}; OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group. OX NCBI_TaxID=100226 {ECO:0000313|EMBL:CAB88152.1, ECO:0000313|Proteomes:UP000001973}; RN [1] {ECO:0000313|EMBL:CAB88152.1, ECO:0000313|Proteomes:UP000001973} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-471 / A3(2) / M145 RC {ECO:0000313|Proteomes:UP000001973}; RX PubMed=8843436; DOI=10.1046/j.1365-2958.1996.6191336.x; RA Redenbach M., Kieser H.M., Denapaite D., Eichner A., Cullum J., Kinashi H., RA Hopwood D.A.; RT "A set of ordered cosmids and a detailed genetic and physical map for the 8 RT Mb Streptomyces coelicolor A3(2) chromosome."; RL Mol. Microbiol. 21:77-96(1996). RN [2] {ECO:0000313|EMBL:CAB88152.1, ECO:0000313|Proteomes:UP000001973} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-471 / A3(2) / M145 RC {ECO:0000313|Proteomes:UP000001973}; RX PubMed=12000953; DOI=10.1038/417141a; RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L., RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.H., RA Kieser T., Larke L., Murphy L., Oliver K., O'Neil S., Rabbinowitsch E., RA Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D., RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., RA Woodward J., Barrell B.G., Parkhill J., Hopwood D.A.; RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor RT A3(2)."; RL Nature 417:141-147(2002). CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|ARBA:ARBA00001913}; 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; AL645882; CAB88152.1; -; Genomic_DNA. DR EMBL; AL939130; CAB88152.1; -; Genomic_DNA. DR RefSeq; WP_011031383.1; NC_003888.3. DR AlphaFoldDB; Q9L036; -. DR STRING; 100226.gene:17764679; -. DR CAZy; CBM25; Carbohydrate-Binding Module Family 25. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR PaxDb; 100226-gene:17764679; -. DR KEGG; sco:SCO7019; -. DR PATRIC; fig|100226.15.peg.7122; -. DR eggNOG; COG0366; Bacteria. DR HOGENOM; CLU_007947_0_0_11; -. DR InParanoid; Q9L036; -. DR OrthoDB; 9805159at2; -. DR PhylomeDB; Q9L036; -. DR Proteomes; UP000001973; Chromosome. DR AbasyAtlas; Q9L036; -. DR GO; GO:2001070; F:starch binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR CDD; cd11339; AmyAc_bac_CMD_like_2; 1. DR CDD; cd00063; FN3; 1. DR FunFam; 3.20.20.80:FF:000200; Alpha-amylase; 1. DR FunFam; 2.60.40.10:FF:001114; Chitinase A1; 1. DR FunFam; 2.60.40.10:FF:002433; Secreted alpha-amylase; 2. DR FunFam; 3.20.20.80:FF:000345; Secreted alpha-amylase; 1. DR Gene3D; 3.20.20.80; Glycosidases; 3. DR Gene3D; 2.60.40.10; Immunoglobulins; 3. DR InterPro; IPR005085; CBM25. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR006047; GH13_cat_dom. DR InterPro; IPR017853; GH_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; 2. DR Pfam; PF03423; CBM_25; 2. DR Pfam; PF00041; fn3; 1. DR SMART; SM00642; Aamy; 1. DR SMART; SM01066; CBM_25; 2. DR SMART; SM00060; FN3; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF49265; Fibronectin type III; 1. DR PROSITE; PS50853; FN3; 1. PE 4: Predicted; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326}; KW Reference proteome {ECO:0000313|Proteomes:UP000001973}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}. FT SIGNAL 1..26 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 27..993 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5038892395" FT DOMAIN 255..348 FT /note="Fibronectin type-III" FT /evidence="ECO:0000259|PROSITE:PS50853" FT REGION 377..397 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 993 AA; 106977 MW; 1006272E0AA67606 CRC64; MRWLGRPLTA AVAVTAVLSA VPAPPAASPA TDPAAAAAET GNTATVFYYT KTKNWDRYNL HYAPDGGSWT EVPGVAMEAA CTDWVKRTVP LGSAEGLRAT FNNGSGTWDN NGGENYALGT GALTVKDGVV AHSDPCAGGQ DPGPTPGGGN RATVYYSTRT LGWTTANIHY RPAGGSWTAV PGVGMRAACA GWWKKDVDLG AATSLTAAFN NGNGVWDNNK GADYTLPAGV TTVADNTVTA DADDPCAEEV PDTAAPTVPA GVSARADGVS VVLTWEPSTD DTGVAKYQVT RSGGTGGEVV SDVGSTVFSD TGLEERTTYT YTVRATDAAG NVSAASAAAI ATTGTRPPAP AAGRPLATDP RKDPIYFVLT ARFNDGDATN NRGGSQHEKS GNAANDDPMF RGDFKGLVNK LDYIKGLGFS AVWITPVVLN RSDYDYHGYH GYDFYKVDPR LESAGASYQD LIDAAHAKGM KIYQDVVYNH SSRWGAKGLF TPTVYGVRDS QWSWYYDEKQ PGFEYDGLTV EPKSGKSYYN GDLWSTAEPT GNTCVNWGRP TGAKSPEGYT LYDCQWPSPT SGMFPKALYH NCWIGNWEGE DSRSCWLHED LADFNTENPQ VQNYLIGAYD KYIDMGVDGF RVDTAVHIPR TTWNRRFLPA IQERVAQQHG AEAAKNFFVF GEVAAFVNDK WNRGSVNHSA QFYTWKERKE YSADDAKAAL EMYEYEQQQG TGNQPTSANA FLEGNSYHVP DHSRFSGMNV IDMRMHMNFG DASNAFHNGK DSDDSYNDAT YNVVYVDSHD YGPNKSSERF SGGTDAWAEN MSLMWTFRGI PTLYYGSEIE FQKGRKIDCG PTCPLATTGR AYYGDHLAGD VTASDFSRVD SATGAVATTL AQPLVKHVQR LNQIRRAVPA LQMGQYSTDG ITGDMAFKRR YTDGGTDSFA LVTVSGGAAY DGIPNGTYRD AVTGDTRTVT DGRLTVAAPG KGNLRVYVLN GPGKIGADGP YLK //