ID D2NRJ1_ROTMD Unreviewed; 513 AA.
AC D2NRJ1;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Sucrose-6-phosphate hydrolase {ECO:0000256|RuleBase:RU365015};
DE EC=3.2.1.26 {ECO:0000256|RuleBase:RU365015};
DE AltName: Full=Invertase {ECO:0000256|RuleBase:RU365015};
GN OrderedLocusNames=RMDY18_04350 {ECO:0000313|EMBL:BAI64267.1};
OS Rothia mucilaginosa (strain DY-18) (Stomatococcus mucilaginosus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=680646 {ECO:0000313|EMBL:BAI64267.1, ECO:0000313|Proteomes:UP000001883};
RN [1] {ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Nambu T., Mashimo C., Sugimori C., Yamanaka T., Leung K.,
RA Fukushima H.;
RT "Complete genome sequence of Rothia mucilaginosa DJ.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAI64267.1, ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|EMBL:BAI64267.1,
RC ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Yoshida M., Fujihira T., Baba T., Tsuji N., Hayashi H.,
RA Sugimori C., Yamanaka T., Mashimo C., Nambu T., Kawai H., Fukushima H.;
RT "Isolation and identification of Rothia mucilaginosa from persistent apical
RT periodontitis lesions.";
RL J Osaka Dent Univ 44:93-98(2010).
RN [3] {ECO:0000313|EMBL:BAI64267.1, ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|EMBL:BAI64267.1,
RC ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Nambu T., Yamanaka T., Mashimo C., Sugimori C., Leung K.-P.,
RA Fukushima H.;
RT "Complete Genome Sequence of Rothia mucilaginosa DY-18: A Clinical Isolate
RT with Dense Meshwork-Like Structures from a Persistent Apical Periodontitis
RT Lesion.";
RL Sequencing 2010:457236-457236(2010).
CC -!- FUNCTION: Enables the bacterium to metabolize sucrose as a sole carbon
CC source. {ECO:0000256|RuleBase:RU365015}.
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:0000256|RuleBase:RU365015};
CC -!- PATHWAY: Glycan biosynthesis; sucrose metabolism.
CC {ECO:0000256|RuleBase:RU365015}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU365015}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family.
CC {ECO:0000256|ARBA:ARBA00009902, ECO:0000256|RuleBase:RU365015}.
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DR EMBL; AP011540; BAI64267.1; -; Genomic_DNA.
DR RefSeq; WP_012903016.1; NC_013715.1.
DR AlphaFoldDB; D2NRJ1; -.
DR STRING; 680646.RMDY18_04350; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR KEGG; rmu:RMDY18_04350; -.
DR eggNOG; COG1621; Bacteria.
DR HOGENOM; CLU_001528_7_1_11; -.
DR UniPathway; UPA00238; -.
DR Proteomes; UP000001883; 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 CDD; cd18623; GH32_ScrB-like; 1.
DR InterPro; IPR001362; Glyco_hydro_32.
DR InterPro; IPR018053; Glyco_hydro_32_AS.
DR InterPro; IPR013148; Glyco_hydro_32_N.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR006232; Suc6P_hydrolase.
DR NCBIfam; TIGR01322; scrB_fam; 1.
DR PANTHER; PTHR43101; BETA-FRUCTOSIDASE; 1.
DR PANTHER; PTHR43101:SF1; BETA-FRUCTOSIDASE; 1.
DR Pfam; PF00251; Glyco_hydro_32N; 1.
DR SMART; SM00640; Glyco_32; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU365015};
KW Cytoplasm {ECO:0000256|RuleBase:RU365015};
KW Glycosidase {ECO:0000256|RuleBase:RU365015};
KW Hydrolase {ECO:0000256|RuleBase:RU365015};
KW Reference proteome {ECO:0000313|Proteomes:UP000001883}.
FT DOMAIN 44..366
FT /note="Glycosyl hydrolase family 32 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00251"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 513 AA; 58148 MW; 2D9B235CC3FA80B2 CRC64;
MSEQKKKKKS ATERPDRDLA AEAQQILDAF GAGVREDRDY PALHLAPPVG RLNDPNGLVF
DGKRYHAFYQ YSPLHPERMV YWRHAVSEDL THWTDEGTAL VPDSRYDSHG CYSGSGIKVP
GGFEFFYTGN VKDEKSNRET YQILATAGED AKPTRQLPPL ISGPEKGYTA HYRDPHVFER
NGEWWMVIGA QREDKTGAVV VYTSADRREW AFRGELDIKD KSLKGTYMYE CPSLLSMRDE
LTGEIRDVLI FSPQGMHPLG EKYNNIFQSG YIVGSLDNKT LKFTVETPFT ELDAGFEFYA
PQTISGTGLT ADPEAPHTVS GDAPVMIAWL GNADQDDLPS WSHRWVHMFT YPRELHLRNG
KLFQRPVPQL NDAMEMKPLY REEEKGKLVE LKNALTFRLR GRVNVSDERV KLKIKDTHGV
ALSIVLDKDF VQMDRGGTRY TEGGSLRRRT LKRSKIREFD LLVDGSATEL YVGGKLVASM
GAEVMTARTF FKGDKRRVRL TGGEVLSLEY GRL
//
