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Database: UniProt
Entry: A0A126ZW22_9MICC
LinkDB: A0A126ZW22_9MICC
Original site: A0A126ZW22_9MICC 
ID   A0A126ZW22_9MICC        Unreviewed;       712 AA.
AC   A0A126ZW22;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=SA2016_0461 {ECO:0000313|EMBL:AMM31157.1};
OS   Sinomonas atrocyanea.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Sinomonas.
OX   NCBI_TaxID=37927 {ECO:0000313|EMBL:AMM31157.1, ECO:0000313|Proteomes:UP000070134};
RN   [1] {ECO:0000313|EMBL:AMM31157.1, ECO:0000313|Proteomes:UP000070134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 3377 {ECO:0000313|EMBL:AMM31157.1,
RC   ECO:0000313|Proteomes:UP000070134};
RA   Kim K.M.;
RT   "Complete genome of Sinomonas atrocyanea KCTC 3377.";
RL   Submitted (FEB-2016) 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|RuleBase:RU361134};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR   EMBL; CP014518; AMM31157.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A126ZW22; -.
DR   STRING; 37927.SA2016_0461; -.
DR   KEGG; satk:SA2016_0461; -.
DR   PATRIC; fig|37927.3.peg.474; -.
DR   Proteomes; UP000070134; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProt.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11334; AmyAc_TreS; 1.
DR   CDD; cd03528; Rieske_RO_ferredoxin; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 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; IPR045857; O16G_dom_2.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
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; PF00355; Rieske; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF50022; ISP domain; 1.
DR   PROSITE; PS51296; RIESKE; 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   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070134}.
FT   DOMAIN          612..699
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
SQ   SEQUENCE   712 AA;  79515 MW;  1223C2189E2B3947 CRC64;
     MRITDTSDLW WKTGIIYCLD VETFYDSNGD GCGDLAGLAE RVDYLAELGI TCLWLMPFYP
     TPRRDDGYDV TDLFGVDRRL GHHGDLVEFI RMAQDRGLRV IVDLVVNHTS DQHPWFKAAR
     SSKDSPYRDF YIWRSDPPPD TSGDVVFPDQ ETSIWTLDEA TGEWYLHHFY KEQPDLNVAN
     PKVRDEIAKV IGFWLHLGIS GFRVDAVPYF LSMEGVRKEE LHKVHNPHDY LRALRKFMGR
     RAGDSILLGE VNLPYHEQMD YFGGPDGDEL TMLFDFVVMQ KMYLSLARQD ARPLADALRD
     RPPLPPDNQW ATFVRNHDEL TLDKLTDEER QEVFAAFGPE PQMQVYGRGL KRRVPPMLDG
     DPRRIRLVYS LLFALPGTPV LYYGEEIGMG EDLAAEGRMA VRTPMQWTAE PSAGFSTAPP
     ADLVSPLPEG GYGPQHVNVA SARRDPDSLL NFIILLTQRY RECPELGWGT CRVLDPPHHA
     VLAHLNTWED ACMLALHNLS PEAVTVPLNL GQPPGRPDRP DRPDGESGWS GFLLLDLLKS
     GTFPQEGLGV SDDGDVEISL GSYGHAWLRV QPPASGACCE LRPDSIRALA RVEPMSEGIV
     VGGTDEIEEG TAKVVEPEES GFDEPIAVFH TETGCFFALN DTCTHEDASL AEGWIEGETV
     ECPLHSSSFS LRTGKVLCLP ATEDTRTHRV EVRDGQVVLF PGTGADPDAC AQ
//
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