ID   I4CPL8_STUST            Unreviewed;       551 AA.
AC   I4CPL8;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Glucan 1,4-alpha-maltohexaosidase {ECO:0000313|EMBL:AFM32025.1};
GN   ORFNames=A458_03865 {ECO:0000313|EMBL:AFM32025.1};
OS   Stutzerimonas stutzeri CCUG 29243.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Stutzerimonas.
OX   NCBI_TaxID=1196835 {ECO:0000313|EMBL:AFM32025.1, ECO:0000313|Proteomes:UP000006063};
RN   [1] {ECO:0000313|EMBL:AFM32025.1, ECO:0000313|Proteomes:UP000006063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 29243 {ECO:0000313|EMBL:AFM32025.1,
RC   ECO:0000313|Proteomes:UP000006063};
RX   PubMed=23144395; DOI=10.1128/JB.01753-12;
RA   Brunet-Galmes I., Busquets A., Pena A., Gomila M., Nogales B.,
RA   Garcia-Valdes E., Lalucat J., Bennasar A., Bosch R.;
RT   "Complete Genome Sequence of the Naphthalene-Degrading Bacterium
RT   Pseudomonas stutzeri AN10 (CCUG 29243).";
RL   J. Bacteriol. 194:6642-6643(2012).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR   EMBL; CP003677; AFM32025.1; -; Genomic_DNA.
DR   RefSeq; WP_014819186.1; NC_018028.1.
DR   AlphaFoldDB; I4CPL8; -.
DR   KEGG; psc:A458_03865; -.
DR   PATRIC; fig|1196835.3.peg.787; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_038814_0_0_6; -.
DR   Proteomes; UP000006063; Chromosome.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11314; AmyAc_arch_bac_plant_AmyA; 1.
DR   CDD; cd05810; CBM20_alpha_MTH; 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; IPR015165; AMT4_domain_C.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR002044; CBM_fam20.
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; PTHR43447; ALPHA-AMYLASE; 1.
DR   PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF09081; AMT4_dom_C; 1.
DR   Pfam; PF00686; CBM_20; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM01065; CBM_2; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR   PROSITE; PS51166; CBM20; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..551
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003687371"
FT   DOMAIN          449..551
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
SQ   SEQUENCE   551 AA;  59945 MW;  E0704961C22455F8 CRC64;
     MSQTLRAAVL AAILLPFPAL ADQAGKSPAG VRYHGGDEII LQGFHWNVVR EAPNDWYDIL
     RQQASTIAAD GFSAIWMPVP WRDFSSWSDG SKSGGGEGYF WHDFNKNGRY GSDAQLRQAA
     GALGGAGVKV LYDVVPNHMN RGYPDKEINL PAGQGFWRND CADPGNYPND CDDGDRFIGG
     ESDLNTGHPQ IYGMFRDELA NLRSGYGAGG FRFDFVRGYA PERVDSWMTD SADNSFCVGE
     LWKGPTEYPS WDWRNTASWQ QIIKDWSDRA KCPVFDFALK ERMQNGSIAD WKNGLNGNPD
     PRWREVAVTF VDNHDTGYSP GQNGGQHHWA LQDGLIRQAY AYILTSPGTP VVYWSHMYDW
     GYGDFIRQLI QVRRTAGVRA DSAISFHSGY SGLVATVSGS QQTLVVALNS DLASPGQVAS
     GSFSEAVNAS NGQVRVWRSG TGDGGGDDGS EGGLVSVNFR CDNGVTQMGD SVYAVGNVSQ
     LGNWSPASAV RLTDTSSYPT WKGSIALPDG QNVEWKCLIR NEADATLVRQ WQSGGNNQVQ
     AAAGASTSGS F
//