ID A0A139NG83_9STRE Unreviewed; 876 AA.
AC A0A139NG83;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:KXT74814.1};
DE EC=3.2.1.24 {ECO:0000313|EMBL:KXT74814.1};
GN ORFNames=STRDD10_00654 {ECO:0000313|EMBL:KXT74814.1};
OS Streptococcus sp. DD10.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1777878 {ECO:0000313|EMBL:KXT74814.1, ECO:0000313|Proteomes:UP000072050};
RN [1] {ECO:0000313|EMBL:KXT74814.1, ECO:0000313|Proteomes:UP000072050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD10 {ECO:0000313|EMBL:KXT74814.1,
RC ECO:0000313|Proteomes:UP000072050};
RA Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I.,
RA Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.;
RT "Highly variable Streptococcus oralis are common among viridans
RT streptococci isolated from primates.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792}.
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:KXT74814.1}.
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; LQRE01000065; KXT74814.1; -; Genomic_DNA.
DR RefSeq; WP_067193099.1; NZ_KQ969158.1.
DR AlphaFoldDB; A0A139NG83; -.
DR STRING; 1777878.STRDD10_00654; -.
DR PATRIC; fig|1777878.3.peg.728; -.
DR OrthoDB; 9764050at2; -.
DR Proteomes; UP000072050; Unassembled WGS sequence.
DR GO; GO:0004559; F:alpha-mannosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR CDD; cd10814; GH38N_AMII_SpGH38_like; 1.
DR Gene3D; 2.60.40.2210; -; 1.
DR Gene3D; 2.60.40.2220; -; 1.
DR Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR Gene3D; 1.20.1270.50; Glycoside hydrolase family 38, central domain; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR041509; GH38_beta-1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR011682; Glyco_hydro_38_C.
DR InterPro; IPR015341; Glyco_hydro_38_cen.
DR InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR InterPro; IPR000602; Glyco_hydro_38_N.
DR InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR PANTHER; PTHR46017; ALPHA-MANNOSIDASE 2C1; 1.
DR PANTHER; PTHR46017:SF2; MANNOSYLGLYCERATE HYDROLASE; 1.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF18438; Glyco_hydro_38; 1.
DR Pfam; PF07748; Glyco_hydro_38C; 1.
DR Pfam; PF01074; Glyco_hydro_38N; 1.
DR SMART; SM00872; Alpha-mann_mid; 1.
DR SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:KXT74814.1};
KW Hydrolase {ECO:0000313|EMBL:KXT74814.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000072050}.
FT DOMAIN 297..367
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 876 AA; 100034 MW; B58F4F147E5C5D05 CRC64;
MENIVVHIIS HSHWDREWYQ SFESHRMQLV ELFDDLFELF ETDPDFKSFH LDGQIIVLDD
YLAIRPENRD RLQRYIDEGK LKIGPFYILQ DDYLISSEAN VRNTLIGQQE CAKWGKSTQI
GYFPDTFGNM GQAPQILQKS GLHVAAFGRG VKPIGFDNQV LEGEQFTSQF SEMYWQGADG
SRILGILFAN WYSNGNEIPV EKEEALTFWK QKLADVRDYA STNQWLIMNG CDHQPVQKNL
SEAIRVANEL FPDVTFVHSS FDDYIKAVEG ALPEQLSTVS GELTSQETDG WYTLANTASS
RLYLKQAFQK NSNLLEQVVE PLTIITGGKN HKDQLTYAWK TLLQNAPHDS ICGCSVDEVH
REMETRYAKV EQVASFVKEN LLHDWKSKLH SQSAKSDLLF TVINTGLHEK MDTVSVDMTI
EMCDFHSTHP TEAYKKMSAL SLPSYVVQDM EGQLIEAKVE DLGAHFHYEL PKDKFRQAYI
ARQVRVTLPI RLAPLSWQSF QLLEGKMQES SGLYQNGVID TPYLTVSLDE GVTVYDKTTN
EAYEDFMLFE DCGDIGNEYI YFQPKNSQPI YAQLVENQVL VNNARYSTVL LKHELTIPVS
ADEVLDAEQR GLVEFMHRRA GRSSQYTTLH LETEMTVFAD CPQIRFKTRF TNNAKDHRIR
VLFKTHNSSQ TNDSESIYEV VRRPNQPASV WVNPENPQHQ QSFVSLYDQE KAVTVSNIGL
NEYEILGNDT IAVTILRASG ELGDWGYFPT PEAQCLRDFE VEFAVECHQP DERFAAYRRA
KALATPFTGL QIKRQEGEVA LAGQALKHPA LSLPQVCPTA FKLAEDGSGR VLRYYNMSQE
NVRVTESQQC QLDLLERPYP VHSGLLAPQE IRTELL
//
