位置:首页 > 蛋白库 > GLAA_BACTN
GLAA_BACTN
ID   GLAA_BACTN              Reviewed;         568 AA.
AC   Q8A2Z5;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Alpha-1,3-galactosidase A;
DE            EC=3.2.1.n1;
DE   AltName: Full=BtGal110A;
DE   AltName: Full=Exo-alpha-galactosidase A;
DE            EC=3.2.1.22;
DE   Flags: Precursor;
GN   Name=glaA; OrderedLocusNames=BT_3160;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=17401360; DOI=10.1038/nbt1298;
RA   Liu Q.P., Sulzenbacher G., Yuan H., Bennett E.P., Pietz G., Saunders K.,
RA   Spence J., Nudelman E., Levery S.B., White T., Neveu J.M., Lane W.S.,
RA   Bourne Y., Olsson M.L., Henrissat B., Clausen H.;
RT   "Bacterial glycosidases for the production of universal red blood cells.";
RL   Nat. Biotechnol. 25:454-464(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
RN   [3]
RP   ENZYME ACTIVITY.
RX   PubMed=18227066; DOI=10.1074/jbc.m709020200;
RA   Liu Q.P., Yuan H., Bennett E.P., Levery S.B., Nudelman E., Spence J.,
RA   Pietz G., Saunders K., White T., Olsson M.L., Henrissat B.,
RA   Sulzenbacher G., Clausen H.;
RT   "Identification of a GH110 subfamily of alpha1,3-galactosidases: novel
RT   enzymes for removal of the alpha3Gal xenotransplantation antigen.";
RL   J. Biol. Chem. 283:8545-8554(2008).
CC   -!- FUNCTION: Alpha-galactosidase that specifically removes branched alpha-
CC       1,3-linked galactose residues present in blood group B antigens. Has no
CC       activity toward linear alpha-1,3-linked galactose residues.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing branched (1->3)-alpha-D-
CC         galactosidic residues, producing free D-galactose.; EC=3.2.1.n1;
CC         Evidence={ECO:0000269|PubMed:18227066};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose
CC         residues in alpha-D-galactosides, including galactose
CC         oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22;
CC         Evidence={ECO:0000269|PubMed:18227066};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 110 family. A subfamily.
CC       {ECO:0000305}.
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; AM109956; CAJ33352.1; -; Genomic_DNA.
DR   EMBL; AE015928; AAO78266.1; -; Genomic_DNA.
DR   RefSeq; NP_812072.1; NC_004663.1.
DR   RefSeq; WP_008767406.1; NC_004663.1.
DR   AlphaFoldDB; Q8A2Z5; -.
DR   SMR; Q8A2Z5; -.
DR   STRING; 226186.BT_3160; -.
DR   CAZy; GH110; Glycoside Hydrolase Family 110.
DR   PaxDb; Q8A2Z5; -.
DR   PRIDE; Q8A2Z5; -.
DR   EnsemblBacteria; AAO78266; AAO78266; BT_3160.
DR   GeneID; 60924339; -.
DR   KEGG; bth:BT_3160; -.
DR   PATRIC; fig|226186.12.peg.3220; -.
DR   eggNOG; COG5434; Bacteria.
DR   HOGENOM; CLU_017693_0_0_10; -.
DR   OMA; HYMHGLG; -.
DR   Proteomes; UP000001414; Chromosome.
DR   GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.160.20.10; -; 2.
DR   InterPro; IPR039448; Beta_helix.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF13229; Beta_helix; 1.
DR   SMART; SM00710; PbH1; 6.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; Reference proteome; Repeat; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..568
FT                   /note="Alpha-1,3-galactosidase A"
FT                   /id="PRO_0000348473"
FT   REPEAT          87..125
FT                   /note="PbH1 1"
FT   REPEAT          243..265
FT                   /note="PbH1 2"
FT   REPEAT          299..321
FT                   /note="PbH1 3"
FT   REPEAT          409..431
FT                   /note="PbH1 4"
FT   REPEAT          432..454
FT                   /note="PbH1 5"
FT   REPEAT          465..486
FT                   /note="PbH1 6"
SQ   SEQUENCE   568 AA;  65147 MW;  BF1CE1BFEAD9EEF3 CRC64;
     MMSVWFIQLA IFAQSRIIEV FPEQGKDIEN IALALKKAAD CKGRPVTVKF SPGIYQLDRA
     KSSQVLYYIS NTTSELDDPD PTKHIGLYLN TLKNITIDGC GSTLLMNGEM TSFVLDKCEG
     IVLKNFNIDY KHPTQTEVEV LEEGNDYLIV QVHPTSQYRI VDAQLEWYGD GWSFKNGIAQ
     SYDRISEMTW RSWSPMENLL RTVELRPNVL YLQYKEKPQV GLHTIFQMRD SFRDEVSGFV
     NRSKGILLEN INFYYLGNFG VVCQYSENIT VDRCNFAPRP GSGRTNAGFA DFIQVSGCRG
     MIDIKNSRFI GAHDDPINIH GTHLRVIEFL SDNRLKLRFM HDQTFGFEAF FKGDDIELVD
     SRSLLVVGKC KVKEAKLVTP REMELTLSSP LSSEVMQQKD LVIENVTWTP EVRITNNYFA
     RVPTRGILIT TRRKSLIEGN TFYGMQMSGI FVADDGLSWY ESGPVHDLTI RQNTFLNCGE
     PIISIDPENR EYKGAVHKNI TIEENYFYMR KNSSCAIRAK AVDGLMIRHN LIYSLDTEKN
     KESDFIQMYN CNEVTIKENR VQLHHLFK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024