INVB_ZYMMA
ID INVB_ZYMMA Reviewed; 413 AA.
AC F8DT27; Q5NQK5; Q60115; Q60117; Q60125;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Extracellular sucrase;
DE EC=3.2.1.26;
DE AltName: Full=Beta-fructofuranosidase;
DE AltName: Full=Invertase;
DE AltName: Full=Protein B46;
DE AltName: Full=Saccharase;
GN Name=sacC; Synonyms=invB, sucE3; OrderedLocusNames=Zmob_0915;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 10988 / DSM 424 / LMG 404 /
OS NCIMB 8938 / NRRL B-806 / ZM1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=555217;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 10988 / DSM 424 / CCUG 17860 / LMG 404 / NCIMB 8938 / NRRL
RC B-806 / ZM1;
RX PubMed=8086457; DOI=10.1016/0167-4781(94)90262-3;
RA Song K.B., Lee S.K., Joo H.K., Rhee S.-K.;
RT "Nucleotide and derived amino acid sequences of an extracellular sucrase
RT gene (invB) of Zymomonas mobilis ZM1 (ATCC10988).";
RL Biochim. Biophys. Acta 1219:163-166(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 10988 / DSM 424 / CCUG 17860 / LMG 404 / NCIMB 8938 / NRRL
RC B-806 / ZM1;
RX PubMed=7778976; DOI=10.1007/bf00305353;
RA Kannan R., Mukundan G., Ait-Abdelkader N., Augier-Magro V., Baratti J.,
RA Gunasekaran P.;
RT "Molecular cloning and characterization of the extracellular sucrase gene
RT (sacC) of Zymomonas mobilis.";
RL Arch. Microbiol. 163:195-204(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10988 / DSM 424 / CCUG 17860 / LMG 404 / NCIMB 8938 / NRRL
RC B-806 / ZM1;
RX PubMed=21725006; DOI=10.1128/jb.05395-11;
RA Pappas K.M., Kouvelis V.N., Saunders E., Brettin T.S., Bruce D., Detter C.,
RA Balakireva M., Han C.S., Savvakis G., Kyrpides N.C., Typas M.A.;
RT "Genome sequence of the ethanol-producing Zymomonas mobilis subsp. mobilis
RT lectotype strain ATCC 10988.";
RL J. Bacteriol. 193:5051-5052(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-fructofuranoside
CC residues in beta-D-fructofuranosides.; EC=3.2.1.26;
CC Evidence={ECO:0000269|PubMed:7778976};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7778976,
CC ECO:0000269|PubMed:8086457}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 68 family. {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; AF081588; AAA61488.1; -; Genomic_DNA.
DR EMBL; L33403; AAC36942.1; -; Genomic_DNA.
DR EMBL; CP002850; AEH62750.1; -; Genomic_DNA.
DR PIR; JC2520; JC2520.
DR PIR; S47527; S47527.
DR RefSeq; WP_012817354.1; NC_017262.1.
DR AlphaFoldDB; F8DT27; -.
DR SMR; F8DT27; -.
DR STRING; 555217.Zmob_0915; -.
DR CAZy; GH68; Glycoside Hydrolase Family 68.
DR EnsemblBacteria; AEH62750; AEH62750; Zmob_0915.
DR GeneID; 58026223; -.
DR KEGG; zmm:Zmob_0915; -.
DR eggNOG; COG1621; Bacteria.
DR HOGENOM; CLU_031862_1_0_5; -.
DR OMA; NGWSVIV; -.
DR Proteomes; UP000001494; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004564; F:beta-fructofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0050053; F:levansucrase activity; IEA:InterPro.
DR GO; GO:0009758; P:carbohydrate utilization; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
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; Glycosidase; Hydrolase; Secreted.
FT CHAIN 1..413
FT /note="Extracellular sucrase"
FT /id="PRO_0000414234"
FT ACT_SITE 44
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT ACT_SITE 276
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT SITE 192
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT CONFLICT 85
FT /note="G -> A (in Ref. 2; AAC36942)"
FT /evidence="ECO:0000305"
FT CONFLICT 404..407
FT /note="PVWP -> LGMA (in Ref. 2; AAC36942)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 46100 MW; BACC12D167332E47 CRC64;
MFNFNASRWT RAQAMKVNKF DLTTSMPEIG TDFPIMRDDL WLWDTWPLRD INGNPVSFKG
WNVIFSLVAD RNIPWNDRHS HARIGYFYSK DGKSWVYGGH LLQESANTRT AEWSGGTIMA
PGSRNQVETF FTSTLFDKNG VREAVAAVTK GRIYADSEGV WFKGFDQSTD LFQADGLFYQ
NYAENNLWNF RDPHVFINPE DGETYALFEA NVATVRGEDD IGEDEIGPVP ANTVVPKDAN
LCSASIGIAR CLSPDRTEWE LLPPLLTAFG VNDQMERPHV IFQNGLTYLF TISHDSTYAD
GLTGSDGLYG FVSENGIFGP YEPLNGSGLV LGGPASQPTE AYAHYIMNNG LVESFINEII
DPKSGKVIAG GSLAPTVRVE LQGHETFATE VFDYGYIPAS YAWPVWPFPD RRK