ID   A0A136MYH6_9BACT        Unreviewed;       899 AA.
AC   A0A136MYH6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Mannosylglycerate hydrolase {ECO:0000313|EMBL:KXK38941.1};
DE            EC=3.2.1.170 {ECO:0000313|EMBL:KXK38941.1};
GN   Name=mngB_1 {ECO:0000313|EMBL:KXK38941.1};
GN   ORFNames=UZ16_OP3001000613 {ECO:0000313|EMBL:KXK38941.1};
OS   Candidatus Hinthialibacteria bacterium OLB16.
OC   Bacteria; Candidatus Hinthialibacterota.
OX   NCBI_TaxID=1617433 {ECO:0000313|EMBL:KXK38941.1, ECO:0000313|Proteomes:UP000070296};
RN   [1] {ECO:0000313|EMBL:KXK38941.1, ECO:0000313|Proteomes:UP000070296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB16 {ECO:0000313|EMBL:KXK38941.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (NOV-2015) 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:KXK38941.1}.
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DR   EMBL; LMZT01000031; KXK38941.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136MYH6; -.
DR   STRING; 1617433.UZ16_OP3001000613; -.
DR   PATRIC; fig|1617433.3.peg.658; -.
DR   Proteomes; UP000070296; 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   Gene3D; 2.60.40.2210; -; 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; 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; 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:KXK38941.1};
KW   Hydrolase {ECO:0000313|EMBL:KXK38941.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          301..374
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   899 AA;  101754 MW;  BBCB4AABBB133831 CRC64;
     MGKEVRKVHF VVSTHWDREW YESFQGFRVR LVNMFDELLE VMEKDPRFKY FQTDGQSIVL
     EDYLEIRPER AAKVRALVEE GRLETGPWYV LPDEFLVSGE SLIRNIQEGI RVADGFGRSS
     RAGFVCDIFG HNSQIPQILS GFGIHSFFMW RGMNEKVCSA DFRWRSPDGS EVLVHRFGPM
     WGYCDYDFRV RKANKIDAHP SHEELVQGLI EEVKLLAGRT PAQTLLVFDG GDHIEIEPST
     PDLIEEANRH LAADGFQIEF STLSRFAADI VKEAERITDV VSGELREPGS GVDEQWVIPG
     VLSSRIDLKM ANRDCEDLLC YWAEPFSAIA KRYGLSPCET YLRTAWRFLL QNHPHDSICG
     CSIEQVHKDM EYRFDQSREI ARLVTRDSLR RIAGSVPGEA TAARFPVVVA NPLTFDRSES
     IDLTIELPSD CPAYQEFFGF ERKPGFRVYD SGGGEIPYQL VHQSLDRTRF IHKVRKFPHA
     FRRHLVDISL RLDLPALGTR TLWVETVAGP TRHPGKGLAT GQSRMENEFL SVEIHGNGTL
     TIQDLESGMV FSSLLTLEDC ADIGDGWYHG VAVNDEVFLS EGSSASISMV HNGPHKATFR
     VEVSFEVPAC FDFSQMVRSG QREILKVTHW ITLRQGARRI EVTTEVNNTI RDHRLRVLFP
     TLLEAGTYLA DSPFDVVERP IELRADNYTY KELEVEAKPQ YTWTAVSGGH EFSDEDEDYG
     LAVVSKGLPE SAVLDTEDRE IALTLLRAFK KAVMTDGCEA GQIQGKHCFN YWIIPFSGRP
     DAVRLGREGQ MLAAGLRSMQ VHPLDDRPEE RNYPDRFSLL KVQGEALVTS IRANEDGGMT
     ARLYNPTEYP TEVVISSEDL QRARLCDFLD QPFQDLPVSA GSATFSLDGK KILSVLLNR
//