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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//