ID   I0HKR7_RUBGI            Unreviewed;       562 AA.
AC   I0HKR7;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Alpha-amylase MalS {ECO:0000313|EMBL:BAL93604.1};
DE            EC=3.2.1.1 {ECO:0000313|EMBL:BAL93604.1};
GN   Name=malS {ECO:0000313|EMBL:BAL93604.1};
GN   OrderedLocusNames=RGE_02590 {ECO:0000313|EMBL:BAL93604.1};
OS   Rubrivivax gelatinosus (strain NBRC 100245 / IL144).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Rubrivivax.
OX   NCBI_TaxID=983917 {ECO:0000313|EMBL:BAL93604.1, ECO:0000313|Proteomes:UP000007883};
RN   [1] {ECO:0000313|EMBL:BAL93604.1, ECO:0000313|Proteomes:UP000007883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100245 / IL144 {ECO:0000313|Proteomes:UP000007883};
RX   PubMed=22689232; DOI=10.1128/JB.00511-12;
RA   Nagashima S., Kamimura A., Shimizu T., Nakamura-isaki S., Aono E.,
RA   Sakamoto K., Ichikawa N., Nakazawa H., Sekine M., Yamazaki S., Fujita N.,
RA   Shimada K., Hanada S., Nagashima K.V.P.;
RT   "Complete genome sequence of phototrophic betaproteobacterium Rubrivivax
RT   gelatinosus IL144.";
RL   J. Bacteriol. 194:3541-3542(2012).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR   EMBL; AP012320; BAL93604.1; -; Genomic_DNA.
DR   RefSeq; WP_014426493.1; NC_017075.1.
DR   AlphaFoldDB; I0HKR7; -.
DR   STRING; 983917.RGE_02590; -.
DR   KEGG; rge:RGE_02590; -.
DR   PATRIC; fig|983917.3.peg.255; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_022115_1_0_4; -.
DR   Proteomes; UP000007883; Chromosome.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
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   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   4: Predicted;
KW   Glycosidase {ECO:0000313|EMBL:BAL93604.1};
KW   Hydrolase {ECO:0000313|EMBL:BAL93604.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007883};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..562
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003628216"
FT   DOMAIN          40..476
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   562 AA;  61987 MW;  E4EDDDCF0393F687 CRC64;
     MMFRRTVAAL AAALALGSAA AADEPVARPG RFADNPIVYF VVTDRFANGN PANDGSYGRK
     REAKPQDDIG SFHGGDLAGL TAKLREGWFR ELGVNAIWIT APYEQIHGWV VGGSKEFKHY
     GYHGYFALDY TKLDANMGTP AELRELVATA HAQGIRILFD VVMNHPGYGD IQSLSEYVTE
     PETDKKRGML WKGYEAATLR DYHSWIDYND PAWLQWWGPD WIRSGLRGYT EGGSDDLTKQ
     LAFLPDFKTE SDKPVGLPPF LKKKADTEAV ELPNTTVRGY LVAWLSRWVR DYGIDGFRAD
     TVKHVEYPSW TALKDASTKA LAEWKAANPK AAIDDAPFWM TGENWGQGIE RTRHYDIGFD
     NMINFDFQRR AEAKGAELDK VYAEYARTLA APATHNVLSY ISSHDTKLFD RKAILDGATA
     LMLAPGGVQI YYGDESARPD GPAAYGDPQQ STRSDMNWAS LDSAALAHWR KLGQFRARHV
     AVARGKHWQI AAQPYTFARV LPEDRIVAAV GARGTVTISV ADVFADGTRV HDAYGGGSAT
     VAGGKVTLDA DPRGVVLLEA LK
//