ID D9ULY7_STRS3 Unreviewed; 1004 AA.
AC D9ULY7;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:EFL03886.1};
GN ORFNames=SSLG_05944 {ECO:0000313|EMBL:EFL03886.1};
OS Streptomyces sp. (strain SPB78).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=591157 {ECO:0000313|EMBL:EFL03886.1, ECO:0000313|Proteomes:UP000005781};
RN [1] {ECO:0000313|EMBL:EFL03886.1, ECO:0000313|Proteomes:UP000005781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPB78 {ECO:0000313|EMBL:EFL03886.1,
RC ECO:0000313|Proteomes:UP000005781};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces sp. strain SPB78.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792}.
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DR EMBL; GG657742; EFL03886.1; -; Genomic_DNA.
DR RefSeq; WP_009070430.1; NZ_GG657742.1.
DR AlphaFoldDB; D9ULY7; -.
DR STRING; 591157.SSLG_05944; -.
DR eggNOG; COG0383; Bacteria.
DR HOGENOM; CLU_003442_0_1_11; -.
DR Proteomes; UP000005781; 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; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 519..597
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1004 AA; 109676 MW; F7FB6E54F0A601D9 CRC64;
MHDDRALVEA RLARVLEERI RPAVYAETVP LDVAIWTAPG EPVPVAEGLA APYEPITPNT
PWGPPWGTSW FKVTGTVPAA WAGRTVEAVL DLGFSRHTPG FQCEGLVHTP EGTPLKGIHP
RNRYVRVGDP ARGGEEIDFR VEAASNPLIQ GDRPFEPTDM GDPATAGSAP QYVLGRMDLA
VFDDNVFQLV IDLEVLGEMM PELPADSARR WEVLRTIDRA LDALDLQDIA GTAAAARALL
APALAVPAQA SAHRISAVGH AHIDSAWLWP LRETVRKVAR TSSNMVSLLE EAPEFVFAMS
QAQQWAWLKE HRPEVWGKVV EAVADGRFVP AGGMWVESDT NMPGSEAMAR QFVHGKRFFL
DEFGVDNDEA WLPDTFGFAA GLPQIIKAAG SKYLLTQKIS WSKVNNFPHH TFRWEGIDGT
RIFTHFPPVD SYNCEMLGSQ LGHAARNFKE KGRATRSLAP TGFGDGGGGT TREMVAKAAR
LKNTEGPARV DWETPSAFFA KAEAEYPEPP VWVGELYLEL HRATLTSQAK TKQGNRRGEH
LLREAELWSA TAAVRAGFPY PYDRLDRLWK TLLLHQFHDI LPGSSIAWVH REAERTYAEL
AGELREIIGA AQQALAGEGD TEVRFNSAPH ADAGIAAGAA GTAPAPAVVA PVARTGGGFV
LDNGVVRIEI DARGLVVSAL RHDSGREAVA PGQAANLLQL HTDFPNQWDA WDVDSFYRNT
VTDLTDVEEL SAAPEGVRIV RAFGDSRVVQ TLSLAEGAAR LDIDTEVDWH ETEKFLKLAF
PLDVHAERYA SETQFGHFYR PTHTNTTWET AKFEACNHRF VHLGEPGFGV AVVNDSTYGH
DVSRTVRADG GTTTTVRASL LRAPRFPDPE TDQGMHRFRH GLVAGATIDD AVREGWRVNL
PRRVVRGAAA EIAPLVTVGQ DSVVVTAVKL ADDGSGDVVV RFHEARGGRV VASLRPGFEV
AEVLVTDLLE RDLSEGAAEV VAVEGELRVA LRPFQLVTLR LRRG
//
