MALA_HALJT
ID MALA_HALJT Reviewed; 663 AA.
AC L8B068; M0LJ23;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=Alpha-amylase MalA {ECO:0000303|PubMed:23391916};
DE EC=3.2.1.1 {ECO:0000269|PubMed:23391916};
GN Name=malA {ECO:0000312|EMBL:BAM75337.1};
GN ORFNames=C444_04352 {ECO:0000312|EMBL:EMA33637.1};
OS Haloarcula japonica (strain ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032
OS / NCIMB 13157 / TR-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=1227453;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-12, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1;
RX PubMed=23391916; DOI=10.1271/bbb.120693;
RA Onodera M., Yatsunami R., Tsukimura W., Fukui T., Nakasone K.,
RA Takashina T., Nakamura S.;
RT "Gene analysis, expression, and characterization of an intracellular alpha-
RT amylase from the extremely halophilic archaeon Haloarcula japonica.";
RL Biosci. Biotechnol. Biochem. 77:281-288(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- FUNCTION: Alpha-amylase that cleaves starch into oligosaccharides, the
CC first step in starch degradation (By similarity). Endo-acting enzyme
CC which prefers a linear polysaccharide to branched polysaccharides
CC hydrolyzing alpha-1,4 glucosidic bonds efficiently. Has also
CC transglycosylation activity, but does not act on alpha-1,6 bonds.
CC Higher activities of 100%, 79% and 67.8% against amylose, soluble
CC starch and amylopectin, respectively. Lower activity of 22% against
CC glycogen and faint or no activity against alpha-, beta- and gamma-
CC cyclodextrin. {ECO:0000250|UniProtKB:Q8A1G3,
CC ECO:0000269|PubMed:23391916}.
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:0000269|PubMed:23391916};
CC -!- ACTIVITY REGULATION: Stable and active over a broad range of NaCl
CC concentrations (0.5 to 4.2 M NaCl), with maximal activity at 2.6 M
CC NaCl. 83% and 94% of the maximum activity at 0.6 and 4.2 M NaCl,
CC respectively. Active and stable also in KCl.
CC {ECO:0000269|PubMed:23391916}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5 in 2.0 M NaCl. Stable over a range of pH 5.7-9.2.
CC {ECO:0000269|PubMed:23391916};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius in 2.0 M NaCl and at pH
CC 6.5. Relatively stable up to 55 degrees Celsius.
CC {ECO:0000269|PubMed:23391916};
CC -!- PATHWAY: Glycan degradation; starch degradation.
CC {ECO:0000250|UniProtKB:Q8A1G3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23391916}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000303|PubMed:23391916}.
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DR EMBL; AB743840; BAM75337.1; -; Genomic_DNA.
DR EMBL; AOLY01000007; EMA33637.1; -; Genomic_DNA.
DR RefSeq; WP_004591161.1; NZ_AOLY01000007.1.
DR AlphaFoldDB; L8B068; -.
DR SMR; L8B068; -.
DR STRING; 1227453.C444_04352; -.
DR EnsemblBacteria; EMA33637; EMA33637; C444_04352.
DR PATRIC; fig|1227453.3.peg.875; -.
DR eggNOG; arCOG02948; Archaea.
DR OrthoDB; 5581at2157; -.
DR BRENDA; 3.2.1.1; 13658.
DR UniPathway; UPA00153; -.
DR Proteomes; UP000011524; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0004558; F:alpha-1,4-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0004556; F:alpha-amylase activity; IDA:UniProtKB.
DR GO; GO:0043169; F:cation binding; IEA:InterPro.
DR GO; GO:2000897; P:amylopectin catabolic process; IDA:UniProtKB.
DR GO; GO:0016052; P:carbohydrate catabolic process; IDA:UniProtKB.
DR GO; GO:0005980; P:glycogen catabolic process; IDA:UniProtKB.
DR GO; GO:0005977; P:glycogen metabolic process; IDA:UniProtKB.
DR GO; GO:0005983; P:starch catabolic process; IDA:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
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 Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Direct protein sequencing; Glycosidase;
KW Hydrolase; Polysaccharide degradation.
FT CHAIN 1..663
FT /note="Alpha-amylase MalA"
FT /id="PRO_0000434886"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 411
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q08751"
FT ACT_SITE 440
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q08751"
FT SITE 503
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q8A1G3"
SQ SEQUENCE 663 AA; 72027 MW; 500D8E7C6FA3656F CRC64;
MHHPGPPRFV ATGDEVELAP RDPDPTATYT WRLTQAPAQS TVSLGDDPVE HFVPDAPGRY
VVRLTAPDGE HDLTVRAFPG TLESSGTHTS GRSGGHSGGV SGGRSGPGRS GSGEYTQAGD
GSDGGGGGQP RLTLRPDIEG DEAVVRADCS PHPEGTETAA DLAVEFLLDD RDDVDADAVT
RDGTALRIPL DALPERARIH AVAVGNHGYS VPDAVEFTRG GDGVETVTSG AGVAARRPYD
APAWAEDSVI YEIYVRTFAG ERDESPFDAI TDRLDYLDSL GVDAIWLTPV LQNDHAPHGY
NITDFFEIAS DLGTRADYER FIEAAHDRGF KVLFDLVCNH SARTHPYFES AVEGPDADYR
EWYEWRSDTE PETYFEWEHI ANFNFDHLPV RRHLLDAVAQ WADLVDGFRC DMAWAVPNGF
WREIHDYCKD RDSEFLLLDE TIPYIPDFQA GLFDMHFDST TYAALRQVGG GGDAEAILGA
IEGRAEIGFP EHASFMLYAE NHDETRYIVD YGREAAEAAA GALFTLPGAP LLYAGQEFGQ
RGRRDDLAWD HADETLQSFV SDLASARHDQ PALSADADLV RIPYEVRDGP SDRVVAYART
TENDAAVVVL NFGSEPTTVG LPAGTDGTDL VSGEYRGAAG DGDATVTVDS VSVFPADEND
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