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SACB_ZYMMO
ID   SACB_ZYMMO              Reviewed;         423 AA.
AC   P0DJA3; Q06487; Q5NQK6; Q60114; Q60116;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Levansucrase;
DE            EC=2.4.1.10;
DE   AltName: Full=Beta-D-fructofuranosyl transferase;
DE   AltName: Full=Sucrose 6-fructosyl transferase;
GN   Name=sacB; Synonyms=levU, sucE2; OrderedLocusNames=ZMO0374;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 29191 / DSM 3580 / JCM 10190 / CECT 560 / NBRC 13756 / NCIMB
RC   11199 / NRRL B-4490 / ZM6;
RX   PubMed=7766026; DOI=10.1271/bbb.59.289;
RA   Kyono K., Yanase H., Tonomura K., Kawasaki H., Sakai T.;
RT   "Cloning and characterization of Zymomonas mobilis genes encoding
RT   extracellular levansucrase and invertase.";
RL   Biosci. Biotechnol. Biochem. 59:289-293(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RA   Ahn J.Y., Kang H.S.;
RT   "Sequence analysis of 44B6 fosmid clone of Zymomonas mobilis ZM4.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA   Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA   Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA   Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[6)-beta-D-fructofuranosyl-(2->](n) alpha-D-glucopyranoside +
CC         sucrose = [6)-beta-D-fructofuranosyl-(2->](n+1) alpha-D-
CC         glucopyranoside + D-glucose; Xref=Rhea:RHEA:13653, Rhea:RHEA-
CC         COMP:13093, Rhea:RHEA-COMP:13094, ChEBI:CHEBI:4167,
CC         ChEBI:CHEBI:17992, ChEBI:CHEBI:134464; EC=2.4.1.10;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: Does not seem to be N-terminally processed.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 68 family. {ECO:0000305}.
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DR   EMBL; D17524; BAA04475.1; -; Genomic_DNA.
DR   EMBL; AF313764; AAG29870.1; -; Genomic_DNA.
DR   EMBL; AE008692; AAV88998.1; -; Genomic_DNA.
DR   PIR; JC2519; JC2519.
DR   RefSeq; WP_011240294.1; NZ_CP035711.1.
DR   AlphaFoldDB; P0DJA3; -.
DR   SMR; P0DJA3; -.
DR   STRING; 264203.ZMO0374; -.
DR   CAZy; GH68; Glycoside Hydrolase Family 68.
DR   EnsemblBacteria; AAV88998; AAV88998; ZMO0374.
DR   GeneID; 58026222; -.
DR   KEGG; zmo:ZMO0374; -.
DR   eggNOG; COG1621; Bacteria.
DR   HOGENOM; CLU_031862_1_0_5; -.
DR   OMA; DPWFFED; -.
DR   OrthoDB; 1622507at2; -.
DR   BRENDA; 2.4.1.10; 14380.
DR   Proteomes; UP000001173; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050053; F:levansucrase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009758; P:carbohydrate utilization; IEA:InterPro.
DR   CDD; cd08997; GH68; 1.
DR   Gene3D; 2.115.10.20; -; 1.
DR   InterPro; IPR003469; Glyco_hydro_68.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   Pfam; PF02435; Glyco_hydro_68; 1.
DR   SUPFAM; SSF75005; SSF75005; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosyltransferase; Reference proteome;
KW   Secreted; Transferase.
FT   CHAIN           1..423
FT                   /note="Levansucrase"
FT                   /id="PRO_0000057721"
FT   ACT_SITE        48
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q74K42"
FT   ACT_SITE        278
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q74K42"
FT   SITE            194
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:Q74K42"
FT   CONFLICT        39
FT                   /note="V -> I (in Ref. 1; BAA04475)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        200..203
FT                   /note="NPED -> TPKI (in Ref. 2; AAG29870)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        217
FT                   /note="E -> Q (in Ref. 1; BAA04475)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        220
FT                   /note="T -> A (in Ref. 1; BAA04475)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        244
FT                   /note="C -> Y (in Ref. 1; BAA04475)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        379
FT                   /note="I -> V (in Ref. 1; BAA04475)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   423 AA;  46762 MW;  19A4691DA3EB9FE3 CRC64;
     MLNKAGIAEP SLWTRADAMK VHTDDPTATM PTIDYDFPVM TDKYWVWDTW PLRDINGQVV
     SFQGWSVIFA LVADRTKYGW HNRNDGARIG YFYSRGGSNW IFGGHLLKDG ANPRSWEWSG
     CTIMAPGTAN SVEVFFTSVN DTPSESVPAQ CKGYIYADDK SVWFDGFDKV TDLFQADGLY
     YADYAENNFW DFRDPHVFIN PEDGKTYALF EGNVAMERGT VAVGEEEIGP VPPKTETPDG
     ARYCAAAIGI AQALNEARTE WKLLPPLVTA FGVNDQTERP HVVFQNGLTY LFTISHHSTY
     ADGLSGPDGV YGFVSENGIF GPYEPLNGSG LVLGNPSSQP YQAYSHYVMT NGLVTSFIDT
     IPSSDPNVYR YGGTLAPTIK LELVGHRSFV TEVKGYGYIP PQIEWLAEDE SSNSAAALSL
     LNK
 
 
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