SCR_ZYMMO
ID SCR_ZYMMO Reviewed; 512 AA.
AC P0DJA7; P22632; P35636; Q5NNZ4; Q84CM3;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Sucrose-6-phosphate hydrolase;
DE Short=Sucrase;
DE EC=3.2.1.26;
DE AltName: Full=Invertase;
GN Name=sacA; Synonyms=invA; OrderedLocusNames=ZMO0942;
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 PROTEIN SEQUENCE OF 1-20.
RC STRAIN=Z6C;
RX PubMed=1368686; DOI=10.1271/bbb1961.55.1383;
RA Yanase H., Fukushi H., Ueda N., Maeda Y., Toyoda A., Tonomura K.;
RT "Cloning, sequencing, and characterization of the intracellular invertase
RT gene from Zymomonas mobilis.";
RL Agric. Biol. Chem. 55:1383-1390(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA O'Mullan P.J., Chase T. Jr., Eveleigh D.E.;
RT "Sequence of a probable nucleotide sugar epimerase and guanine deaminase
RT from Zymomonas mobilis.";
RL Submitted (OCT-2002) 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=Hydrolysis of terminal non-reducing beta-D-fructofuranoside
CC residues in beta-D-fructofuranosides.; EC=3.2.1.26;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10067};
CC -!- PATHWAY: Glycan biosynthesis; sucrose metabolism.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR EMBL; D10465; BAA01258.1; -; Genomic_DNA.
DR EMBL; AY171597; AAO38865.1; -; Genomic_DNA.
DR EMBL; AE008692; AAV89566.1; -; Genomic_DNA.
DR PIR; JU0460; JU0460.
DR RefSeq; WP_011240801.1; NZ_CP035711.1.
DR AlphaFoldDB; P0DJA7; -.
DR SMR; P0DJA7; -.
DR STRING; 264203.ZMO0942; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR EnsemblBacteria; AAV89566; AAV89566; ZMO0942.
DR GeneID; 58026740; -.
DR KEGG; zmo:ZMO0942; -.
DR eggNOG; COG1621; Bacteria.
DR HOGENOM; CLU_001528_7_0_5; -.
DR OMA; YKAGSGH; -.
DR OrthoDB; 1622507at2; -.
DR UniPathway; UPA00238; -.
DR Proteomes; UP000001173; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004564; F:beta-fructofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005985; P:sucrose metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001362; Glyco_hydro_32.
DR InterPro; IPR018053; Glyco_hydro_32_AS.
DR InterPro; IPR013189; Glyco_hydro_32_C.
DR InterPro; IPR013148; Glyco_hydro_32_N.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR006232; Suc6P_hydrolase.
DR Pfam; PF08244; Glyco_hydro_32C; 1.
DR Pfam; PF00251; Glyco_hydro_32N; 1.
DR SMART; SM00640; Glyco_32; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
DR TIGRFAMs; TIGR01322; scrB_fam; 1.
DR PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Direct protein sequencing; Glycosidase;
KW Hydrolase; Reference proteome.
FT CHAIN 1..512
FT /note="Sucrose-6-phosphate hydrolase"
FT /id="PRO_0000169880"
FT ACT_SITE 43
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 40..43
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 102..103
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 165..166
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 24
FT /note="L -> V (in Ref. 1; BAA01258)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="S -> L (in Ref. 2; AAO38865)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="V -> I (in Ref. 1; BAA01258)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="L -> P (in Ref. 1; BAA01258 and 2; AAO38865)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="V -> I (in Ref. 1; BAA01258)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="A -> P (in Ref. 1; BAA01258)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="N -> D (in Ref. 1; BAA01258 and 2; AAO38865)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="H -> R (in Ref. 1; BAA01258)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="A -> D (in Ref. 1; BAA01258)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="M -> I (in Ref. 1; BAA01258)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="G -> D (in Ref. 1; BAA01258)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="S -> L (in Ref. 1; BAA01258)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 58575 MW; 3EFBF2499FFD8CAD CRC64;
MESPSYKNLI KAEDAQKKAG KRLLSSEWYP GFHVTPLTGW MNDPNGLIFF KGEYHLFYQY
YPFAPVWGPM HWGHAKSRDL VHWETLPVAL APGDSFDRDG CFSGCAVDNN GVLTLIYTGH
IVLSNDSLDA IREVQCMATS IDGIHFQKEG IVLEKAPMPQ VAHFRDPRVW KENNHWFMVV
GYRTDDEKHQ GIGHVALYRS ENLKDWIFVK TLLGDNSQLP LGKRAFMWEC PDFFSLGNRS
VLMFSPQGLK ASGYKNRNLF QNGYILGKWQ APQFTPETSF QELDYGHDFY AAQRFEAKDG
RQILIAWFDM WENQKPSQRD GWAGCMTLPR KLDLIDNKIV MTPVREMEIL RQSEKIESVV
TLSDAEHPFT MDSPLQEIEL IFDLEKSSAY QAGLALRCNG KGQETLLYID RSQNRIILDR
NRSGQNVKGI RSCPLPNTSK VRLHIFLDRS SIEIFVGDDQ TQGLYSISSR IFPDKDSLKG
RLFAIEGYAV FDSFKRWTLQ DANLAAFSSD AC
