ID A0A0R2HBD5_9FIRM Unreviewed; 511 AA.
AC A0A0R2HBD5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Sucrose-6-phosphate hydrolase {ECO:0000256|ARBA:ARBA00019623, ECO:0000256|RuleBase:RU362110};
DE EC=3.2.1.26 {ECO:0000256|ARBA:ARBA00012758, ECO:0000256|RuleBase:RU362110};
DE AltName: Full=Invertase {ECO:0000256|ARBA:ARBA00033367, ECO:0000256|RuleBase:RU365015};
GN ORFNames=IV49_GL000917 {ECO:0000313|EMBL:KRN49675.1};
OS Kandleria vitulina DSM 20405.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Kandleria.
OX NCBI_TaxID=1410657 {ECO:0000313|EMBL:KRN49675.1, ECO:0000313|Proteomes:UP000051841};
RN [1] {ECO:0000313|EMBL:KRN49675.1, ECO:0000313|Proteomes:UP000051841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20405 {ECO:0000313|EMBL:KRN49675.1,
RC ECO:0000313|Proteomes:UP000051841};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:RU362110};
CC -!- PATHWAY: Glycan biosynthesis; sucrose metabolism.
CC {ECO:0000256|ARBA:ARBA00004914, 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:RU362110}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRN49675.1}.
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DR EMBL; JQBL01000023; KRN49675.1; -; Genomic_DNA.
DR RefSeq; WP_031590130.1; NZ_KL370859.1.
DR AlphaFoldDB; A0A0R2HBD5; -.
DR PATRIC; fig|1410657.5.peg.955; -.
DR UniPathway; UPA00238; -.
DR Proteomes; UP000051841; Unassembled WGS sequence.
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; cd08996; GH32_FFase; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001362; Glyco_hydro_32.
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 NCBIfam; TIGR01322; scrB_fam; 1.
DR PANTHER; PTHR43101; BETA-FRUCTOSIDASE; 1.
DR PANTHER; PTHR43101:SF1; BETA-FRUCTOSIDASE; 1.
DR Pfam; PF08244; Glyco_hydro_32C; 1.
DR Pfam; PF00251; Glyco_hydro_32N; 2.
DR SMART; SM00640; Glyco_32; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU365015};
KW Cytoplasm {ECO:0000256|RuleBase:RU365015};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU362110};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362110};
KW Reference proteome {ECO:0000313|Proteomes:UP000051841}.
FT DOMAIN 12..162
FT /note="Glycosyl hydrolase family 32 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00251"
FT DOMAIN 197..352
FT /note="Glycosyl hydrolase family 32 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00251"
FT DOMAIN 355..503
FT /note="Glycosyl hydrolase family 32 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08244"
SQ SEQUENCE 511 AA; 59364 MW; E8D44DFD0C25B405 CRC64;
MNVNKKYMPT YHAHVSSGWS NDPNGLLYFN GKYHMFFQHY PHKAKWGIMH WGHFISDDLI
KWEEAPVALV PDQEYERQCG CCSGTAIERD GKLYLMYTAA QMDLQRQCIA YSEDGIHFSK
LDNPLIDARN LNTSDISPKD FRDPKVFKKD DTYYCIAGTR MMSEEDLQNY IDFVSNQNEN
KEITIDDVAS TNFYAHGYGN LVLLKSDDFN NWEYVGPLLT KQENIQEAFY RLNGVYECPD
YFEVDGQELL LASPQNLLQI GYRFQNLHSC VYIPGHLDFT TGDFHPEYIE EIDSGFDFYA
PQCMKMTDGR YVMIAWKEMW DRTYPTESDN WIGTYTLPRE LSYKDGQLIQ TPIRELENYR
QNEVVAKGMI LNGELRLEGV EGNKIELEVD MEITTASRAG IKLFKHGDHE VFIYYDQKEQ
LFVFDRSCSG IEIGGREIDT NIRKMPWENK RIQLRMFLDV SSLEIFIDGG KKTMTGNIYG
DPIKDTGVEF FSEDGECIIH SVKKYDIVVE A
//
