ID A0A085F260_9BURK Unreviewed; 620 AA.
AC A0A085F260;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Alpha-amylase SusA {ECO:0000313|EMBL:KFC65555.1};
DE EC=3.2.1.135 {ECO:0000313|EMBL:KFC65555.1};
GN Name=susA_2 {ECO:0000313|EMBL:KFC65555.1};
GN ORFNames=FG94_03638 {ECO:0000313|EMBL:KFC65555.1};
OS Massilia sp. LC238.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1502852 {ECO:0000313|EMBL:KFC65555.1, ECO:0000313|Proteomes:UP000028601};
RN [1] {ECO:0000313|EMBL:KFC65555.1, ECO:0000313|Proteomes:UP000028601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC238 {ECO:0000313|EMBL:KFC65555.1,
RC ECO:0000313|Proteomes:UP000028601};
RA Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT isolate.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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:KFC65555.1}.
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DR EMBL; JNNN01000066; KFC65555.1; -; Genomic_DNA.
DR RefSeq; WP_036214447.1; NZ_JNNN01000066.1.
DR AlphaFoldDB; A0A085F260; -.
DR STRING; 1502852.FG94_03638; -.
DR PATRIC; fig|1502852.3.peg.3589; -.
DR eggNOG; COG0366; Bacteria.
DR OrthoDB; 9761577at2; -.
DR Proteomes; UP000028601; Unassembled WGS sequence.
DR GO; GO:0031216; F:neopullulanase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11340; AmyAc_bac_CMD_like_3; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR015171; Cyc-maltodext_N.
DR InterPro; IPR019492; Cyclo-malto-dextrinase_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 InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF234; INTRACELLULAR MALTOGENIC AMYLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF10438; Cyc-maltodext_C; 1.
DR Pfam; PF09087; Cyc-maltodext_N; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000313|EMBL:KFC65555.1};
KW Hydrolase {ECO:0000313|EMBL:KFC65555.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..620
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001789330"
FT DOMAIN 132..529
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 140..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 620 AA; 70101 MW; 58632D72FC984D8B CRC64;
MKLFFATLLV GSAALSPFAA QAQSPAIAHM EPPFWWVGMQ HKGLQLMVHG ERIADLEPSL
AYPGVRIASV TRVPSRNYLF IDLEIGQDAR PGKFDIVFKG AGRQASYAYQ LLAREPGSAQ
RQGFTSRDTI YQVMPDRFAN GNPGNDSTPD TLEKANRANG SGRHGGDIQG IIDRLDYIQG
MGFTQLWPTP LVENNMPAYS YHGYAATDHY RIDPRYGSNE DFRRLSNEAK KRGIGLIQDV
VLSHIGAEHW WMKDLPTPDW VNYGGKFVPT QHHRVAVQDP YASKEDADNF TRGWFVESMP
DLNQSNPLVA NYLIQNNIWW IEYAGLAGLR IDTFGYSDGA FLSEYTRRLM AEYPKLNMVG
EEWSKLVPVV ARWQRGKDNF DGYSASTPSL MDFPLAEAMR TALSDNKGGN VFTDVYETLS
LDYLYPEPGN LVLFEANHDV SRIWSVVGED FDRYRMMMVF LMTMPRIPQL YTGDEILMTS
ATRERDDASY RRDFPGGWAG DRIDAFTGKG LTAQQRAAQE LVRKLANWRK GQSVIHHGKL
MHYGPRDNTW VYFRYDGDKK VLVAFNNNPK EMVLDTHRFR EMLAGVAGGV DVLSGKRFEL
GKELRLPAKA SLILELEAAR
//