ID A0A4R7TA59_9ACTN Unreviewed; 948 AA.
AC A0A4R7TA59;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase {ECO:0000256|ARBA:ARBA00030238};
GN ORFNames=EV138_1679 {ECO:0000313|EMBL:TDU88138.1};
OS Kribbella voronezhensis.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Kribbellaceae; Kribbella.
OX NCBI_TaxID=2512212 {ECO:0000313|EMBL:TDU88138.1, ECO:0000313|Proteomes:UP000295151};
RN [1] {ECO:0000313|EMBL:TDU88138.1, ECO:0000313|Proteomes:UP000295151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-2575 {ECO:0000313|EMBL:TDU88138.1,
RC ECO:0000313|Proteomes:UP000295151};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-2019) 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|ARBA:ARBA00000548};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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:TDU88138.1}.
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DR EMBL; SOCE01000001; TDU88138.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R7TA59; -.
DR OrthoDB; 176168at2; -.
DR Proteomes; UP000295151; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase 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; cd14752; GH31_N; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR002044; CBM20.
DR InterPro; IPR033403; DUF5110.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR017853; GH.
DR InterPro; IPR048395; Glyco_hydro_31_C.
DR InterPro; IPR000322; Glyco_hydro_31_TIM.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR051816; Glycosyl_Hydrolase_31.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR43863; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G03140)-RELATED; 1.
DR PANTHER; PTHR43863:SF2; MALTASE-GLUCOAMYLASE; 1.
DR Pfam; PF00686; CBM_20; 1.
DR Pfam; PF17137; DUF5110; 1.
DR Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361185};
KW Hydrolase {ECO:0000256|RuleBase:RU361185};
KW Reference proteome {ECO:0000313|Proteomes:UP000295151};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..948
FT /note="alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5020809718"
FT DOMAIN 842..948
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
SQ SEQUENCE 948 AA; 102389 MW; 6E5D33C6641F30D7 CRC64;
MKRLAAFLLL IPLLVVLPTQ TAQAAVQRVQ FTAGGNYLVV EFLDDDLVHF ELGAGAGPGS
GSPIFSTDQI GKTNYTGPTT FNQTGNTLTT AGLKVDVNAT TLCATVTDIT RSPQLLLNTT
CPRNLSQAWK GLSFTKSSMQ NAYGLGEQFF MGGSADGDWV GRQRTSGAYG NAMLYDTDNG
PVGNAQIPVL FAVGANTTNY GMFVDQVYKQ DWNLTGDPWT MDTYGDQLRW YVMSGPDLPD
LRKDYLELTG RPPVPPKKAF GLWMSEYGYD NWNEIDTTLS GLRANKFPTD GVMLDVNWFG
GVTAGSDNTR MGTLDWDPVN FPNAAAKLAT YKNTNGVGVM TIEESYVGKN LPEHTDMASG
GYLIRAGCSS CSPSYLTGND WWGRGGMIDW TQPAASAHWH TTQRQPLIND GVMGHWLDLG
EPEMYDSNDW TSGVLAGKHA HSDYHNLYNL EWAKGIAKGY TDNAVQQRPF MLARSAAGGI
QRTGTAMWSG DIGSKLTALA DQQNVQMQMS MSGIDYFGSD IGGFRREMLN SDLNELYTQW
FANSSWFDVP IRPHTENLCN CAETSPDSIG DVPSNLANLR QRYELTPYYY SLAHKAYTTG
EPLMPPLVYQ YQNDPNVRET GHEKLIGKDL LVGVAAGANQ RKRDVYLPAG TWYDYYTNTK
TVSTGQNLTD VPLWRNGKFQ LPAYARAGAI IPKMYVDDQT MNVMGKRADG TTRNELVARV
YSDPTASSFT LAEDDGSTIG YQTGSKRTTD LTQSRSGSTA TVGIAAASGT YTGAPSSRSN
VVELVADTQA SAVTLNGSAL TQYANKAAFD AAASGWYNAG GNLVVAKSAS LAVSTAKSFV
FTLGQAVVSK TFSCSNGTTT TGQSVYVVGN VPQLGAWSVA SAVKLAPTSY PTWTGTISNL
PPNISVEWKC IKRQEANYPA TADLWGPDPN ITFTTPATGS GGTTTGGF
//
