ID   A0A1V6LQ05_9FLAO        Unreviewed;       761 AA.
AC   A0A1V6LQ05;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=BUL40_10920 {ECO:0000313|EMBL:OQD42275.1};
OS   Croceivirga radicis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Croceivirga.
OX   NCBI_TaxID=1929488 {ECO:0000313|EMBL:OQD42275.1, ECO:0000313|Proteomes:UP000191680};
RN   [1] {ECO:0000313|EMBL:OQD42275.1, ECO:0000313|Proteomes:UP000191680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HSG9 {ECO:0000313|EMBL:OQD42275.1,
RC   ECO:0000313|Proteomes:UP000191680};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU361134};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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:OQD42275.1}.
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DR   EMBL; MTBC01000007; OQD42275.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6LQ05; -.
DR   OrthoDB; 9806009at2; -.
DR   Proteomes; UP000191680; Unassembled WGS sequence.
DR   GO; GO:0019867; C:outer membrane; IEA:InterPro.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
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:UniProtKB-KW.
DR   CDD; cd11314; AmyAc_arch_bac_plant_AmyA; 1.
DR   CDD; cd12956; CBM_SusE-F_like; 2.
DR   CDD; cd12967; CBM_SusE-F_like_u1; 1.
DR   Gene3D; 2.60.40.3620; -; 3.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR015237; Alpha-amylase_C_pro.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR032187; SusF/SusE.
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; PF16411; SusF_SusE; 2.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191680};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..761
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013388530"
FT   DOMAIN          57..386
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   761 AA;  83232 MW;  BCB18E080DD9B665 CRC64;
     MKIKKYINLS LAALTFVFAA CTNDDFSPLK VKEANDAEDL PSGSAAGRTD ALVPGNGVMM
     QAFYWDVTEG GIWWNNVESK LDSWAANGID AIWIPPISKG QSGGFSMGYD PADYFDFGDF
     QQHGTVETRF GNRAELENMI GTAHENNIAV IADIVLNHNS GGQLEYNEFR QIETYTLFEP
     ASGLFNRTWL NYLPNAENLK DEGRFGGFPD LDLKNDYVRD WLWQSEESVA NYYMNTLKID
     GWRFDFVKGF SPDVVKDWIA TVGGYSVGEN FDGNVEGVVG PWVEASGANA FDFPNFFNMR
     NAFLNGNLNE LVKPSLLSTM PEKAVTFVGN HDTEARDGSN EFPDAFETHA YAYIMSAPGY
     PCVFYSHYED SGEEQKAKIN QLIQIRSELA AGDWTVNHVS NQEFVATRGG DAEKPGLVLY
     INLSGEEVSR EVQTHWASAN IKDYTEEYLI FEQSDASGLV TLKAPANGFA IWAATEDEQL
     AFPEVLYVPG GYQGWDPSSA PALNAVELPN LAGTFSGHVR FTEASNEFKF TDAPNWDNGI
     YADAGDGTTG VLASPGNNIV LAGPQDYEIN VDLANNTWSA NTWAIIGSAT PNGWDDPDTD
     MSYDFDRNVW TVSTTLADGE LKFRANNGWD VNLGDTGADG VLDNGGDNIA VTAGSYQIDL
     DVANNSFTLG NWGVIGSATP SGWDADTNMM YDTVNQVWTI TLDLVAGEMK FRFNDDWAVN
     LGDNNGDGSV EQDGANIAVA AAGNYTITLD LFTNTFTITG N
//