ID A0A0R2GVT0_9LACO Unreviewed; 750 AA.
AC A0A0R2GVT0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Glycosyl hydrolase family 65 protein {ECO:0000313|EMBL:KRN44219.1};
GN ORFNames=IV41_GL000622 {ECO:0000313|EMBL:KRN44219.1};
OS Limosilactobacillus ingluviei.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=148604 {ECO:0000313|EMBL:KRN44219.1, ECO:0000313|Proteomes:UP000051639};
RN [1] {ECO:0000313|EMBL:KRN44219.1, ECO:0000313|Proteomes:UP000051639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14792 {ECO:0000313|EMBL:KRN44219.1,
RC ECO:0000313|Proteomes:UP000051639};
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family.
CC {ECO:0000256|ARBA:ARBA00006768}.
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:KRN44219.1}.
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DR EMBL; JQBA01000019; KRN44219.1; -; Genomic_DNA.
DR RefSeq; WP_056994425.1; NZ_JQBA01000019.1.
DR AlphaFoldDB; A0A0R2GVT0; -.
DR STRING; 1203076.GCA_000312405_01758; -.
DR PATRIC; fig|148604.4.peg.629; -.
DR eggNOG; COG1554; Bacteria.
DR OrthoDB; 9758855at2; -.
DR Proteomes; UP000051639; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.70.98.40; Glycoside hydrolase, family 65, N-terminal domain; 1.
DR Gene3D; 2.60.420.10; Maltose phosphorylase, domain 3; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR005194; Glyco_hydro_65_C.
DR InterPro; IPR005195; Glyco_hydro_65_M.
DR InterPro; IPR005196; Glyco_hydro_65_N.
DR InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR InterPro; IPR017045; Malt_Pase/Glycosyl_Hdrlase.
DR PANTHER; PTHR11051; GLYCOSYL HYDROLASE-RELATED; 1.
DR PANTHER; PTHR11051:SF14; MALTOSE PHOSPHORYLASE; 1.
DR Pfam; PF03633; Glyco_hydro_65C; 1.
DR Pfam; PF03632; Glyco_hydro_65m; 1.
DR Pfam; PF03636; Glyco_hydro_65N; 1.
DR PIRSF; PIRSF036289; Glycosyl_hydrolase_malt_phosph; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KRN44219.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051639}.
FT DOMAIN 14..265
FT /note="Glycoside hydrolase family 65 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03636"
FT DOMAIN 322..678
FT /note="Glycoside hydrolase family 65 central catalytic"
FT /evidence="ECO:0000259|Pfam:PF03632"
FT DOMAIN 688..749
FT /note="Glycoside hydrolase family 65 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03633"
FT ACT_SITE 486
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-50"
FT BINDING 357..358
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
FT BINDING 591..592
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
SQ SEQUENCE 750 AA; 85594 MW; D27E14B2E257C07F CRC64;
MKQTFDIAPW HVKTTKWSPE DKRLQESMTS LANENLGMRG FFEEGYSADK MEGVYLGGVW
FPDKTRVGWW KNGYPKYFGK MINAVNFLKL PITVNGEALD LAKQTPSDFS LDLDMQRGTF
TRTFTATVGG AKMRFEFVRF VSAVQKELVG QQVTLTNLSD QAVQLEVTSA IDGDVYNEDA
NYDEQFWDVL DRQASGQHAL LVSKTKPNDF GTPQFTVAMK TTTLTALPHT TDHVADKEVA
NVFAGELAPQ TSLTVEKRTV VATSRDFATE AELLARVDEL TTSLADQSFA DLLKAHEAEW
QARWDKSDVK INGDEGAQQG IRFNLFQLFS TYYGNDYRLN ISPKGFTGEK YGGATYWDTE
AYCLPVYLGV ANPEISRNLL MYRYNQLDGA YINAQEQGLK GALYPMVTFN GIECHNEWEI
TFEEIHRNGD VAYAIYNYTN YTGDKSYVLH EGAKVLTEIS RFWADRVHYS QRANKYMLHG
VTGPDEYDNN VNNDWYTNLL CQWTLKYTLE VLAEVDAEVA ADLAVTEDEK RHWKSIVDNM
YLPYDEERRI FPENDGFMDK DLIPVGEIPS DQLPLNQNWS WDKILRSPYV KQGDVIQGIW
DFMDDFTPEE KKRNFDFYEQ FTVHESSLSA SVYSVIAADI GYEDKAVEMY ERSARLDLDN
YNNDTADGLH ITSMTGSWID IVQGFAGMRV RDGQLHYAPF LPKKWDSYQF RQQFRGRVIE
VTVDKNGAKA ELISGEPLTI DLAGEKLELK
//
