ID A0A2W5WW18_9MICO Unreviewed; 604 AA.
AC A0A2W5WW18;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN Name=treS {ECO:0000313|EMBL:PZR52025.1};
GN ORFNames=DNL40_13480 {ECO:0000313|EMBL:PZR52025.1};
OS Xylanimonas oleitrophica.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Xylanimonas.
OX NCBI_TaxID=2607479 {ECO:0000313|EMBL:PZR52025.1, ECO:0000313|Proteomes:UP000248783};
RN [1] {ECO:0000313|EMBL:PZR52025.1, ECO:0000313|Proteomes:UP000248783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PW21 {ECO:0000313|EMBL:PZR52025.1,
RC ECO:0000313|Proteomes:UP000248783};
RA Nagkirti P., Shaikh A., Gowdaman V., Engineer A.E., Dagar S.,
RA Dhakephalkar P.K.;
RT "Whole genome sequencing of a novel hydrocarbon degrading bacterial strain,
RT PW21 isolated from oil contaminated produced water sample.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-maltose = alpha,alpha-trehalose; Xref=Rhea:RHEA:15145,
CC ChEBI:CHEBI:16551, ChEBI:CHEBI:17306; EC=5.4.99.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001595};
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. TreS
CC subfamily. {ECO:0000256|ARBA:ARBA00005496}.
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:PZR52025.1}.
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DR EMBL; QKWH01000013; PZR52025.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W5WW18; -.
DR Proteomes; UP000248783; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0047471; F:maltose alpha-D-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11334; AmyAc_TreS; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
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; IPR032091; Malt_amylase_C.
DR InterPro; IPR045857; O16G_dom_2.
DR InterPro; IPR012810; TreS/a-amylase_N.
DR NCBIfam; TIGR02456; treS_nterm; 1.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF219; MALTOSE ALPHA-D-GLUCOSYLTRANSFERASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF16657; Malt_amylase_C; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW Glycosidase {ECO:0000256|RuleBase:RU361134};
KW Hydrolase {ECO:0000256|RuleBase:RU361134};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:PZR52025.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000248783};
KW Transferase {ECO:0000313|EMBL:PZR52025.1}.
FT DOMAIN 53..454
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 604 AA; 68475 MW; 37DEA6DC5317FE31 CRC64;
MSTSTRPADV PRPTTQALPV QALPPRREPD VPGLGRPGLT DDPDWYRKAV FYEVIVRAFS
DSQGAGSGDL RGIIQRLDYL QWLGIDCLWL PPFYPSPLRD GGYDVADYTA IAPQYGTTAD
FTELIEEAHA RGIRVVVDLV MNHTSDQHPW FQSSRADPDG PYGDFYVWSD DSTRYQDARI
IFVDTETSNW TFDPVRRQYY WHRFFSHQPD LNFENPRVVD AMLDVARFWL GIGVDGFRLD
AVPYLFEAEG TNCENLPETH AFLRKVRRMI DAEFPGRIML AEANQWPQDV VDYFGTDDEP
ECHMCFHFPV MPRIFYAMRD QRARQILDIM ADTPPIPARG GQWSTFLRNH DELTLEMVST
EERASMYGWY AQDPRMRANV GIRRRLAPLL DNSRKEIELA HALLLSLPGS PCLYYGDEIA
MGDNIWLPDR DAVRTPMQWT PDRNAGFSTA DPGKLYLPLV QSLVHHYEQY NVEAQLAQPT
SLLHWVHGML AVRRLHPTFG TGDFVARDCD EEAILAFTRS SEDETLLVAA NMAATAHSAT
IELPGYEGWT LTDVFGGGRF PTVGADGRVT MTWGSRDFYW LRLDPPAGSS GRGGPAHDEA
GEPR
//
