ID H3SII0_9BACL Unreviewed; 591 AA.
AC H3SII0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Alpha amylase {ECO:0000313|EMBL:EHQ61106.1};
GN ORFNames=PDENDC454_16768 {ECO:0000313|EMBL:EHQ61106.1};
OS Paenibacillus dendritiformis C454.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1131935 {ECO:0000313|EMBL:EHQ61106.1, ECO:0000313|Proteomes:UP000003900};
RN [1] {ECO:0000313|EMBL:EHQ61106.1, ECO:0000313|Proteomes:UP000003900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C454 {ECO:0000313|EMBL:EHQ61106.1,
RC ECO:0000313|Proteomes:UP000003900};
RX PubMed=22461558; DOI=10.1128/JB.00158-12;
RA Sirota-Madi A., Olender T., Helman Y., Brainis I., Finkelshtein A.,
RA Roth D., Hagai E., Leshkowitz D., Brodsky L., Galatenko V., Nikolaev V.,
RA Gutnick D.L., Lancet D., Ben-Jacob E.;
RT "Genome Sequence of the Pattern-Forming Social Bacterium Paenibacillus
RT dendritiformis C454 Chiral Morphotype.";
RL J. Bacteriol. 194:2127-2128(2012).
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:EHQ61106.1}.
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; AHKH01000047; EHQ61106.1; -; Genomic_DNA.
DR RefSeq; WP_006677844.1; NZ_AHKH01000047.1.
DR AlphaFoldDB; H3SII0; -.
DR STRING; 1131935.PDENDC454_16768; -.
DR PATRIC; fig|1131935.3.peg.3489; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000003900; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11338; AmyAc_CMD; 1.
DR CDD; cd02857; E_set_CDase_PDE_N; 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; IPR022567; DUF3459.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004185; Glyco_hydro_13_lg-like_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR045857; O16G_dom_2.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF234; INTRACELLULAR MALTOGENIC AMYLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02903; Alpha-amylase_N; 1.
DR Pfam; PF11941; DUF3459; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000003900}.
FT DOMAIN 135..493
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 591 AA; 68380 MW; FA2BA0D104B56254 CRC64;
MLREAVYHRS KQNWSYAYDR ETIHLRLRTK RDDAVKVEAI VVDKYAFKDS TEFIPMHIFA
SDALFDYWEA AYRPPYRRLR YAFRIQGKDE QVYLTERGFF EDLPWDYFES FEYPFLHPND
MFEAPAWVKE AVFYQIFPER FANGDPANDP EKTEAWGGEP KPGNFFGGDL QGVLDHLDYL
TELGINAIYF TPVFEATTNH KYDTRDYLKV DRHFGTNEKL KELIMACHER GIRVLLDAVF
NHAGRTFPPF VDVMEKGSES PYADWFYVRD YPLRVVDGKP TYETFSFEPL MPKLNTSHPE
VKRYLLEVAR YWVEEIGIDG WRLDVANEVD HQFWREFRQV VKQANPDAYI LGEIWHDSMM
WLQGDQFDAV MNYPFTDAVL NFFARQTTDA RAFADSIGSI LASYPQPVTE VSFNLLDSHD
TPRLLTLCEG DVRPMKLAAL FQFTYPGTPC IYYGDEIGLE GGPDPGCRKC MVWDEAEQDR
GLFAFYQRII ALRRKHEALR SARIRFLHAE AEGRTLMYEL TGADGSFLIA MNAGDAPAEL
RLETGTVAEG SWSLEYGEGI RIAAQPDTLE VALDGFGFAV FRMKSDIDNA Q
//
