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Database: UniProt
Entry: A0A099KBI7_9GAMM
LinkDB: A0A099KBI7_9GAMM
Original site: A0A099KBI7_9GAMM 
ID   A0A099KBI7_9GAMM        Unreviewed;       914 AA.
AC   A0A099KBI7;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Glucan 1,4-alpha-maltohexaosidase {ECO:0000313|EMBL:KGJ88079.1};
DE            EC=3.2.1.98 {ECO:0000313|EMBL:KGJ88079.1};
GN   ORFNames=ND16A_2632 {ECO:0000313|EMBL:KGJ88079.1};
OS   Thalassotalea sp. ND16A.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Thalassotalea.
OX   NCBI_TaxID=1535422 {ECO:0000313|EMBL:KGJ88079.1, ECO:0000313|Proteomes:UP000029848};
RN   [1] {ECO:0000313|EMBL:KGJ88079.1, ECO:0000313|Proteomes:UP000029848}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND16A {ECO:0000313|EMBL:KGJ88079.1,
RC   ECO:0000313|Proteomes:UP000029848};
RA   Stelling S.C., Techtmann S.M., Utturkar S.M., Alshibli N., Brown S.D.,
RA   Hazen T.C.;
RT   "Draft Genome Sequence of Thalassotalea sp. strain ND16A Isolated from
RT   Eastern Mediterranean Deep Water.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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:KGJ88079.1}.
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DR   EMBL; JQDZ01000123; KGJ88079.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A099KBI7; -.
DR   STRING; 1535422.ND16A_2632; -.
DR   PATRIC; fig|1535422.3.peg.3759; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG2374; Bacteria.
DR   eggNOG; COG3291; Bacteria.
DR   Proteomes; UP000029848; Unassembled WGS sequence.
DR   GO; GO:0033927; F:glucan 1,4-alpha-maltohexaosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11318; AmyAc_bac_fung_AmyA; 1.
DR   Gene3D; 2.40.30.140; -; 1.
DR   Gene3D; 2.60.120.380; -; 2.
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; IPR015237; Alpha-amylase_C_pro.
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   InterPro; IPR007280; Peptidase_C_arc/bac.
DR   PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR   PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR   Pfam; PF09154; Alpha-amy_C_pro; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF00686; CBM_20; 1.
DR   Pfam; PF04151; PPC; 2.
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   4: Predicted;
KW   Glycosidase {ECO:0000313|EMBL:KGJ88079.1};
KW   Hydrolase {ECO:0000313|EMBL:KGJ88079.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029848}.
FT   DOMAIN          813..914
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
FT   REGION          260..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          891..914
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..309
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   914 AA;  101754 MW;  00A74CA1C4A0349A CRC64;
     MTNAFHGVKQ KIQNSLPMIQ KILSISAIIT GLLTTSSVVA LTDDDTTNLL TNNKSINKLF
     AQKDEILLYR FDVPQGTKEV VFQSRHGKGN ADLYVKLASK PSLADYDFSS IGKMNKEKIV
     IKDPQHGLYY IGVNATESFN KLQLIAKVKH PDYFVLLNKI VKPELRKGTG KDLRFRFDVP
     DNATELTFSS GGGTGNADLY VKHGTWATTT DFDYVGNNET NDETLTIANS NVLAGTYYVT
     VHAEHSYKNL NFTASYALDE AEPTEPTEPT EPTEPTEPTE PTEPTEPTEP TEPTEPTEPT
     EPTEPTEPPE LTDPVIAQAN GVMMQYFNWY TPNDGSLWTE VAQQAQNLAD AGITALWLPP
     AYKGSAGGAD VGYGVYDMYD LGEFDQKGSV RTKYGSKDEY LTAINEAHSH GIQIYGDVVF
     NHRGGADATE SVTAVRVDWN DRNQELGADV QIDAWTEFNF PGRGNTYSDF KWRWYHFDGV
     DWAANLNESS IFKFRGIGKA WDWEVATENG NYDYLMFADL DMDHPEVVQE LKDWGEWYVD
     FANVDGFRLD AVKHVKFAFF NEWLDHIRTA TQKELFTVGE FWSYNKEQLH HFIAQTGGRM
     SLFDAPLHMN FHIASASGGG YDMRSIMDNT LMKEQPGLAV TLVDNHDTQP CQALESAVQD
     WFKPLAYAFI LLREQGYPNI FHADYYGANY TTSDNGCDNT QITITSQKEN IDELLAARKE
     YAYGAQIDYL DHQDIIGWTR LGDAEHVTAM AVIMTDGPGG VKWMDVARVN TQFIDVTGNR
     SEVITTNNDG WGEFPVNGGS YAVWVEQTAD DTPPEPPVTE VQVTLNCANG NTYLGQNVYA
     VGNIDALGNW DVNNALLLNA DNYPTWSAQV TLAPVTAVEW KCVKVDGSNT EWQSGNNNSF
     TSPETGTADS NGGF
//
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