GenomeNet

Database: UniProt/TrEMBL
Entry: B8CZ54_HALOH
LinkDB: B8CZ54_HALOH
Original site: B8CZ54_HALOH 
ID   B8CZ54_HALOH            Unreviewed;       623 AA.
AC   B8CZ54;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   28-FEB-2018, entry version 66.
DE   SubName: Full=Alpha amylase {ECO:0000313|EMBL:ACL70573.1};
DE            EC=3.2.1.98 {ECO:0000313|EMBL:ACL70573.1};
GN   OrderedLocusNames=Hore_18240 {ECO:0000313|EMBL:ACL70573.1};
OS   Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562).
OC   Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halothermothrix.
OX   NCBI_TaxID=373903 {ECO:0000313|EMBL:ACL70573.1, ECO:0000313|Proteomes:UP000000719};
RN   [1] {ECO:0000213|PDB:3BC9, ECO:0000213|PDB:3BCD, ECO:0000213|PDB:3BCF}
RP   X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 25-623 IN COMPLEX WITH
RP   CALCIUM AND GLUCOSE.
RX   PubMed=18387632; DOI=10.1016/j.jmb.2008.02.041;
RA   Tan T.C., Mijts B.N., Swaminathan K., Patel B.K., Divne C.;
RT   "Crystal structure of the polyextremophilic alpha-amylase AmyB from
RT   Halothermothrix orenii: details of a productive enzyme-substrate
RT   complex and an N domain with a role in binding raw starch.";
RL   J. Mol. Biol. 378:852-870(2008).
RN   [2] {ECO:0000313|EMBL:ACL70573.1, ECO:0000313|Proteomes:UP000000719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H 168 / OCM 544 / DSM 9562 {ECO:0000313|Proteomes:UP000000719};
RX   PubMed=19145256; DOI=10.1371/journal.pone.0004192;
RA   Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D.,
RA   Sun H., Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.;
RT   "Genome analysis of the anaerobic thermohalophilic bacterium
RT   Halothermothrix orenii.";
RL   PLoS ONE 4:E4192-E4192(2009).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001098; ACL70573.1; -; Genomic_DNA.
DR   RefSeq; WP_015923543.1; NC_011899.1.
DR   PDB; 3BC9; X-ray; 1.35 A; A=25-623.
DR   PDB; 3BCD; X-ray; 2.20 A; A=25-623.
DR   PDB; 3BCF; X-ray; 2.30 A; A=25-623.
DR   PDBsum; 3BC9; -.
DR   PDBsum; 3BCD; -.
DR   PDBsum; 3BCF; -.
DR   ProteinModelPortal; B8CZ54; -.
DR   SMR; B8CZ54; -.
DR   STRING; 373903.Hore_18240; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; ACL70573; ACL70573; Hore_18240.
DR   KEGG; hor:Hore_18240; -.
DR   eggNOG; ENOG4105E5K; Bacteria.
DR   eggNOG; COG0366; LUCA.
DR   HOGENOM; HOG000094847; -.
DR   OMA; GEFWKDS; -.
DR   OrthoDB; POG091H0HQ3; -.
DR   BioCyc; HORE373903:GHB1-1889-MONOMER; -.
DR   EvolutionaryTrace; B8CZ54; -.
DR   Proteomes; UP000000719; Chromosome.
DR   GO; GO:0033927; F:glucan 1,4-alpha-maltohexaosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR015237; Alpha-amylase_C_pro.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF09154; DUF1939; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0000213|PDB:3BC9, ECO:0000213|PDB:3BCD,
KW   ECO:0000213|PDB:3BCF};
KW   Calcium {ECO:0000213|PDB:3BC9, ECO:0000213|PDB:3BCD,
KW   ECO:0000213|PDB:3BCF};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000719};
KW   Glycosidase {ECO:0000313|EMBL:ACL70573.1};
KW   Hydrolase {ECO:0000313|EMBL:ACL70573.1};
KW   Metal-binding {ECO:0000213|PDB:3BC9, ECO:0000213|PDB:3BCD,
KW   ECO:0000213|PDB:3BCF};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000719}.
FT   DOMAIN      147    525       Aamy. {ECO:0000259|SMART:SM00642}.
FT   REGION      260    263       Glucose binding. {ECO:0000213|PDB:3BC9}.
FT   REGION      328    335       Glucose binding. {ECO:0000213|PDB:3BC9}.
FT   REGION      372    378       Glucose binding. {ECO:0000213|PDB:3BC9,
FT                                ECO:0000213|PDB:3BCD}.
FT   REGION      404    406       Glucose binding. {ECO:0000213|PDB:3BC9,
FT                                ECO:0000213|PDB:3BCD}.
FT   REGION      470    474       Glucose binding. {ECO:0000213|PDB:3BC9,
FT                                ECO:0000213|PDB:3BCD}.
FT   REGION      479    487       Glucose binding. {ECO:0000213|PDB:3BC9,
FT                                ECO:0000213|PDB:3BCD}.
FT   METAL       101    101       Calcium 1. {ECO:0000213|PDB:3BC9,
FT                                ECO:0000213|PDB:3BCD, ECO:0000213|PDB:
FT                                3BCF}.
FT   METAL       256    256       Calcium 2. {ECO:0000213|PDB:3BC9,
FT                                ECO:0000213|PDB:3BCD, ECO:0000213|PDB:
FT                                3BCF}.
FT   METAL       307    307       Calcium 3. {ECO:0000213|PDB:3BC9,
FT                                ECO:0000213|PDB:3BCF}.
FT   METAL       327    327       Calcium 3; via carbonyl oxygen.
FT                                {ECO:0000213|PDB:3BC9, ECO:0000213|PDB:
FT                                3BCD, ECO:0000213|PDB:3BCF}.
FT   METAL       329    329       Calcium 3. {ECO:0000213|PDB:3BC9,
FT                                ECO:0000213|PDB:3BCD, ECO:0000213|PDB:
FT                                3BCF}.
FT   METAL       337    337       Calcium 2. {ECO:0000213|PDB:3BC9,
FT                                ECO:0000213|PDB:3BCD, ECO:0000213|PDB:
FT                                3BCF}.
FT   METAL       343    343       Calcium 2. {ECO:0000213|PDB:3BC9,
FT                                ECO:0000213|PDB:3BCD, ECO:0000213|PDB:
FT                                3BCF}.
FT   METAL       345    345       Calcium 3. {ECO:0000213|PDB:3BC9,
FT                                ECO:0000213|PDB:3BCD, ECO:0000213|PDB:
FT                                3BCF}.
FT   METAL       347    347       Calcium 3. {ECO:0000213|PDB:3BC9,
FT                                ECO:0000213|PDB:3BCD, ECO:0000213|PDB:
FT                                3BCF}.
FT   METAL       378    378       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000213|PDB:3BC9, ECO:0000213|PDB:
FT                                3BCD, ECO:0000213|PDB:3BCF}.
FT   METAL       392    392       Calcium 4. {ECO:0000213|PDB:3BCD}.
FT   METAL       395    395       Calcium 4; via carbonyl oxygen.
FT                                {ECO:0000213|PDB:3BCD}.
FT   METAL       397    397       Calcium 4; via carbonyl oxygen.
FT                                {ECO:0000213|PDB:3BCD}.
FT   METAL       438    438       Calcium 5. {ECO:0000213|PDB:3BCD}.
FT   METAL       441    441       Calcium 5. {ECO:0000213|PDB:3BCD}.
FT   METAL       442    442       Calcium 5; via carbonyl oxygen.
FT                                {ECO:0000213|PDB:3BCD}.
FT   METAL       443    443       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000213|PDB:3BC9}.
FT   METAL       541    541       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000213|PDB:3BC9, ECO:0000213|PDB:
FT                                3BCD, ECO:0000213|PDB:3BCF}.
FT   METAL       542    542       Calcium 1. {ECO:0000213|PDB:3BC9,
FT                                ECO:0000213|PDB:3BCD, ECO:0000213|PDB:
FT                                3BCF}.
FT   METAL       551    551       Calcium 6; via carbonyl oxygen.
FT                                {ECO:0000213|PDB:3BC9, ECO:0000213|PDB:
FT                                3BCD, ECO:0000213|PDB:3BCF}.
FT   METAL       554    554       Calcium 6; via carbonyl oxygen.
FT                                {ECO:0000213|PDB:3BC9, ECO:0000213|PDB:
FT                                3BCD, ECO:0000213|PDB:3BCF}.
FT   METAL       557    557       Calcium 6. {ECO:0000213|PDB:3BC9,
FT                                ECO:0000213|PDB:3BCD, ECO:0000213|PDB:
FT                                3BCF}.
FT   METAL       565    565       Calcium 1. {ECO:0000213|PDB:3BC9,
FT                                ECO:0000213|PDB:3BCD, ECO:0000213|PDB:
FT                                3BCF}.
FT   BINDING     284    284       Glucose. {ECO:0000213|PDB:3BC9}.
FT   BINDING     512    512       Glucose. {ECO:0000213|PDB:3BCD}.
FT   BINDING     612    612       Glucose. {ECO:0000213|PDB:3BCD}.
SQ   SEQUENCE   623 AA;  71348 MW;  8604C1348DDF33A6 CRC64;
     MVFIKLFIKY KIYAALILLI LLLSGCSNIS EDVNNPNRSL FLIESEPSTG ASVSKNLTEI
     ILIFSNDINK VSQLALTDLI TDSDIQGIDY NIEGNKVIIN NFSLEPTCNY RLSYEVIDIY
     DNHLQGYIEF LVNQSNYPQI PDQEVNHTIL QAFYWEMNTG EYATEHPEEA NLWNLLAERA
     PELAEAGFTA VWLPPANKGM AGIHDVGYGT YDLWDLGEFD QKGTVRTKYG TKGELENAID
     ALHNNDIKVY FDAVLNHRMG ADYAETVLLD ENSRDKPGQY IKAWTGFNFP GRNGEYSNFT
     WNGQCFDGTD WDDYSKESGK YLFDEKSWDW TYNWDEDYLM GADVDYENEA VQNDVIDWGQ
     WIINNIDFDG FRLDAVKHID YRFIDKWMSA VQNSSNRDVF FVGEAWVEDV DDLKGFLDTV
     GNPDLRVFDF PLRSFFVDML NGAYMADLRN AGLVNSPGYE NRAVTFVDNH DTDRDEGSYT
     VSIYSRKYQA YAYILTRAEG VPTVYWKDYY IWEMKEGLDK LLTARRYYAY GPGYEVDNND
     ADIYSYVRSG FPDVAGDGLV LMISDGTSGN VAGKWINSRQ PDTEFYDLTG HIKEHVTTDS
     EGYGNFKVIK SEDKGWSIWV PVE
//
DBGET integrated database retrieval system