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Database: UniProt/TrEMBL
Entry: A6VL46_ACTSZ
LinkDB: A6VL46_ACTSZ
Original site: A6VL46_ACTSZ 
ID   A6VL46_ACTSZ            Unreviewed;       685 AA.
AC   A6VL46;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   24-JAN-2024, entry version 80.
DE   SubName: Full=Alpha amylase catalytic region {ECO:0000313|EMBL:ABR73693.1};
GN   OrderedLocusNames=Asuc_0315 {ECO:0000313|EMBL:ABR73693.1};
OS   Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS   130Z).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=339671 {ECO:0000313|EMBL:ABR73693.1, ECO:0000313|Proteomes:UP000001114};
RN   [1] {ECO:0000313|Proteomes:UP000001114}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z
RC   {ECO:0000313|Proteomes:UP000001114};
RX   PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA   McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA   Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA   Burkhart K.B., Harkins V., Vieille C.;
RT   "A genomic perspective on the potential of Actinobacillus succinogenes for
RT   industrial succinate production.";
RL   BMC Genomics 11:680-680(2010).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR036917-2};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR036917-2};
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DR   EMBL; CP000746; ABR73693.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6VL46; -.
DR   STRING; 339671.Asuc_0315; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; asu:Asuc_0315; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_022115_1_0_6; -.
DR   OMA; DKVMVVW; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000001114; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030980; P:alpha-glucan catabolic process; IEA:InterPro.
DR   GO; GO:0009313; P:oligosaccharide catabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR014635; A_amylase_MalS.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF209; PERIPLASMIC ALPHA-AMYLASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 2.
DR   PIRSF; PIRSF036917; Alph_amls_MalS; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PIRSR:PIRSR036917-2};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR036917-4};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR036917-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001114};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..685
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002701893"
FT   DOMAIN          195..647
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        461
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-1"
FT   ACT_SITE        503
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-1"
FT   BINDING         316
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-2"
FT   BINDING         465
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-2"
FT   SITE            565
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-3"
FT   DISULFID        59..77
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-4"
FT   DISULFID        123..537
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-4"
SQ   SEQUENCE   685 AA;  78800 MW;  F4825B25B3264E76 CRC64;
     MKKSLLYFCL FTSSVSFAQG WQHTHFRYFN DSAETNLFQS QTALEKGYYP LTFIFDNQCY
     QPQSAMKLNQ TVSLIPCFGE APHIRLFRRG NYIAQIDMRS GTPTLKIGVQ QQQSSDKNAL
     KSCPRWNKQP IEIDVSSTFA EGESVRDFYS NQIAEVKNGK VIMMPAANAD GLILLEKSAV
     EKTDVFDWKN ATVYFVLTDR FHNGNPANDN SYGRHKDGMQ EIGTFHGGDL QGLTEKLDYL
     QQLGVNALWI SSPLEQMHGW VGGGNKGDFP HYGYHGYYHL DWTKLDANMG TESDLRNLIQ
     QAHRRGIRVL FDIVMNHTGY ATLADMQEFK FGDFYLKPEE ITAVLGEKWT NWQPEKGQNW
     HSFNDFIKFG DSKAWQNWWG KDWVRADIGD YDSPKFDDLR MSLSALPDLK TESESAVELP
     RFFQHKNTNA KKLDNAKVRD YLIVWLTDWV RRYGVDGFRV DTAKHVEKST WLALKQASQR
     ALKEWQQKNP KESFGDDFWM TGEAWGHGVF KSDYYQNGFD AMINFDFQDQ AKNALDCFAR
     IEPVYQEMNN KLKDFNVLSY LSSHDTRLFF HSDSERNVAK QKIAANLLLL SSGAVQIYYG
     DESGREFGAT GSDPVQGTRS DMNWTDLQKD RSKQALHQHW QKLAQFRQRH QAVGAGVHQT
     LKSESYFAFS RTLGEDKVMV VWAGN
//
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