ID A0A1S9ACW4_9BURK Unreviewed; 613 AA.
AC A0A1S9ACW4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Alpha-amlyase {ECO:0000313|EMBL:OON61301.1};
GN ORFNames=B0920_18045 {ECO:0000313|EMBL:OON61301.1};
OS Massilia sp. KIM.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1955422 {ECO:0000313|EMBL:OON61301.1, ECO:0000313|Proteomes:UP000190838};
RN [1] {ECO:0000313|EMBL:OON61301.1, ECO:0000313|Proteomes:UP000190838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM {ECO:0000313|EMBL:OON61301.1,
RC ECO:0000313|Proteomes:UP000190838};
RA Vikram S., Kabwe M.H., Bezuidt O., Govender N., Makhalanyane T.P.;
RT "Genome sequence of Massilia sp. KIM isolated from grassland biome soil in
RT South Africa.";
RL Submitted (FEB-2017) 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:OON61301.1}.
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DR EMBL; MVAD01000002; OON61301.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9ACW4; -.
DR STRING; 1955422.B0920_18045; -.
DR OrthoDB; 9761577at2; -.
DR Proteomes; UP000190838; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 Lyase {ECO:0000313|EMBL:OON61301.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000190838};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..613
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012006659"
FT DOMAIN 129..525
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 134..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 613 AA; 69306 MW; FEA109A9F26B116F CRC64;
MRHVLASLLL GASFAAHAQT SAIAHMEPPF WWAGMQHKEL QLMVHGERIA ELEPSLSYPG
VRIASVTRVP NKNYLFIDLV VGADARPGSF EIRFAGAGGR SASYNYRLLA REPGSANRAG
FSSKDAIYQI MPDRFANGDP SNDSTPDMLE KGDRKNGGGR HGGDIAGIIG KLDYIAGLGF
TQLWPTPLVE NNMPSYSYHG YAATDHYRID PRYGSNEDFV RLSREAKQRG IGIIQDVVLS
HIGSHHWWMK DLPTPDWVNY GKFVPTQHHR TAVQDPYASQ EDSDNFTRGW FVQSMPDLNQ
SNPLVANYLI QNNIWWIEYA GLSGLRIDTF GYSDGAFLSQ YTKRLMQEYP KLNLVGEEWS
TKVPVVARWQ RGKQNFDGYT ASTPSLMDFP LSEAMRNALA DKEGRNVFNE VYETLSLDYL
YPEPGNLVLF ADNHDMSRIY SVVGEDLDKY KMDLVFIMTM PRIPQFYVGD EILMTSATKE
RNDISYRSDF PGGWAGDRID AFAGKGLTAR QREAQEFVRK LVNWRKGQPV IHHGKLMHYG
PRDNTYVYFR YDGSKKVLVA FNNNPKEMVL DVDRFREMLS GVASGKDVLS GKTFDLRSEL
RLPAKASLVL ELQ
//