ID A0A3N6E6V0_9ACTN Unreviewed; 1037 AA.
AC A0A3N6E6V0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Mannosylglycerate hydrolase {ECO:0000313|EMBL:RPK56318.1};
DE EC=3.2.1.170 {ECO:0000313|EMBL:RPK56318.1};
GN Name=mngB {ECO:0000313|EMBL:RPK56318.1};
GN ORFNames=EES43_25060 {ECO:0000313|EMBL:RPK56318.1};
OS Streptomyces sp. ADI96-02.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1522760 {ECO:0000313|EMBL:RPK56318.1, ECO:0000313|Proteomes:UP000273170};
RN [1] {ECO:0000313|EMBL:RPK56318.1, ECO:0000313|Proteomes:UP000273170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ADI96-02 {ECO:0000313|EMBL:RPK56318.1,
RC ECO:0000313|Proteomes:UP000273170};
RA Guerrero-Garzon J.F., Zehl M., Urban E., Schneider O., Ruckert C.,
RA Busche T., Kalinowski J., Zotchev S.B.;
RT "Streptomyces spp. from the marine sponge Antho dichothoma: analyses of
RT secondary metabolite biosynthesis gene clusters and some of their
RT products.";
RL Submitted (NOV-2018) 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:RPK56318.1}.
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; RPGW01000160; RPK56318.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N6E6V0; -.
DR OrthoDB; 9772207at2; -.
DR Proteomes; UP000273170; Unassembled WGS sequence.
DR GO; GO:0004559; F:alpha-mannosidase activity; IEA:InterPro.
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; cd10789; GH38N_AMII_ER_cytosolic; 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; IPR041147; GH38_C.
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:SF1; ALPHA-MANNOSIDASE 2C1; 1.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF17677; Glyco_hydro38C2; 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:RPK56318.1};
KW Hydrolase {ECO:0000313|EMBL:RPK56318.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000273170}.
FT DOMAIN 519..598
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1037 AA; 114065 MW; DA887A2AFA10EECE CRC64;
MHDDRTLVEG RLERALHQFI RPARYAARAP LAVSVWHVPG EPVPVAEALK AAYAPFSAGT
EWGSPWSTSW FRLEGAVPRE WAGRRVEMVV DPGFTGQGPG FQAEGMLYDR LGVPLKGVHP
RNRHLPVADP AEGGEPVDVL LEAAANPAVL EHGFEPTALG DVLTAGDRPL YRFTSADLAV
LDEEVWHLEL DIEVLSELMA ELPADRSRRH EILRALESML DALDLHDVSG TAVAGRAALA
GVLARPASAS AHRISAAAHA HIDSAWLWPL RETVRKASRT FANVTALAED YPELVFACSQ
AQQYAWVKEH QPHIWQRIRQ AVAAGRWAPV GSMWVESDAN MPGGEALARQ LVHGKRFFRE
ELGVETEEIW LPDSFGYTAA FPQLARLAGV RWFLTQKLSW NQHNKMPHHT FWWEGIDGTR
VFTHFPPVDT YNSQLHGREL AHAERNFADK GRATRSLVPF GWGDGGGGPT REMLEKARRL
RDLEGSPRVE IEKPSAFFAA AEEEYGQQAP VWSGELYLEL HRATYTTQAK TKQGNRRSEH
LLREAELWST AAALRSPGHR YPHERLDRLW KTVLLHQFHD ILPGSSIAWV HREAGDTYEE
VRAELADVVA AAVAALGAPD GLVALNASPY GREQVVELDA EAAGVLPSGA RTQELGEGRV
AVFAHSPALG AGLLDGAARP EHPVAAETAS GDGIVLDNGL LRVTVDRDGL VARVRDLVAG
REVLVPGARA NLLQLHPDHP NQWDAWDIDG HYRRTRTDLT GAQEVTLVED GPLRAAVRVV
RVFGRSTVVQ ELRLAAGSRQ LDIETEVDWQ ESEKVLKAAF PLDVHAERST SEIQFGHVHR
PTHDNTGWDA ARFEICAHRW LRVAEPGYGV ALLNDSTYGH DVTRTPHPTG LGTTVRLTLL
RAPHSPDPDT DLGTHRFRYS LAPGAEVTDA VREGLALNLP LRAAVAPAVP SLVRTGHPAV
TVESVKQADD RSGDVIVRLY ESAGGRARTR LTSSFPAVRA QITDLLERPL HEAVTDEDGV
VLELRPFQIL TVRLTPA
//
