ID   A4CNH0_ROBBH            Unreviewed;       561 AA.
AC   A4CNH0;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   OrderedLocusNames=RB2501_00136 {ECO:0000313|EMBL:EAR14437.1};
OS   Robiginitalea biformata (strain ATCC BAA-864 / HTCC2501 / KCTC 12146).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Robiginitalea.
OX   NCBI_TaxID=313596 {ECO:0000313|EMBL:EAR14437.1, ECO:0000313|Proteomes:UP000009049};
RN   [1] {ECO:0000313|EMBL:EAR14437.1, ECO:0000313|Proteomes:UP000009049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-864 / HTCC2501 / KCTC 12146
RC   {ECO:0000313|Proteomes:UP000009049};
RX   PubMed=19767438; DOI=10.1128/JB.01191-09;
RA   Oh H.M., Giovannoni S.J., Lee K., Ferriera S., Johnson J., Cho J.C.;
RT   "Complete genome sequence of Robiginitalea biformata HTCC2501.";
RL   J. Bacteriol. 191:7144-7145(2009).
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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR   EMBL; CP001712; EAR14437.1; -; Genomic_DNA.
DR   RefSeq; WP_015755225.1; NC_013222.1.
DR   AlphaFoldDB; A4CNH0; -.
DR   STRING; 313596.RB2501_00136; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; rbi:RB2501_00136; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_022115_0_1_10; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000009049; Chromosome.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10357:SF215; ALPHA-AMYLASE 1; 1.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   Pfam; PF00128; Alpha-amylase; 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|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009049}.
FT   DOMAIN          51..471
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   561 AA;  62894 MW;  C02AE128B94CBC05 CRC64;
     MHRLLLILAL SVSIYSCKPE PKTAQLPATE QVADQGRDSV PFLWEAANIY FLLTDRFRNG
     NPENDLNFDR VNPTGPLRGF MGGDLAGITE KIKDGYFTDL GINAIWFTPV VEQVHGDTDE
     GTGNTYAYHG YWAKDWTALD PNFGTRDELA ELVAAAHAKG IRILMDVVLN HTGPVTGEDP
     AWPESWVRLD PTCNFEDYQG TTACTLVENL PDIRTESSEA VVLPDALLAK WKAEGRLSEE
     LDELQVFFDR TGYPRAPRYY IIKWLTDYVN DLGIDGFRVD TAKHVNEDAW SELYREAAYA
     FQSWKRKHPG KVLDDTPFYM VGEVYGYGAS SGRDYDFGDR TVDYFDHGFK SLINFELKSD
     AGQSYDRIFE KYSTLLHDDL NGLGIVNYLS SHDDGSPFDP DRSKPFRSAN ILLLTPGASQ
     VYYGDESARG LVVEGTVGDA TLRSFMNWEE LDSLPEKQEI LAHWQKLGQF RNHHPAIGAG
     RHKRLASQPY VFSRTYTDGD YRDKVAVGLD LPEGPKSLYV RGFFGDGTVL RDAYSGSEAT
     VSGGRVELDT PYPIALLELA D
//