ID S5VD63_STRC3 Unreviewed; 1006 AA.
AC S5VD63;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:AGS73169.1};
GN ORFNames=B446_31825 {ECO:0000313|EMBL:AGS73169.1};
OS Streptomyces collinus (strain DSM 40733 / Tue 365).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1214242 {ECO:0000313|EMBL:AGS73169.1, ECO:0000313|Proteomes:UP000015423};
RN [1] {ECO:0000313|Proteomes:UP000015423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RA Ruckert C., Szczepanowski R., Goesmann A., Pross E.K., Musiol E.M.,
RA Blin K., Wohlleben W., Puhler A., Weber T., Kalinowski J.;
RT "The complete genome sequence of Streptomyces collinus Tu 365.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGS73169.1, ECO:0000313|Proteomes:UP000015423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RX PubMed=24140291; DOI=10.1016/j.jbiotec.2013.10.004;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Iftime D.,
RA Musiol E.M., Blin K., Wohlleben W., Puhler A., Kalinowski J., Weber T.;
RT "Complete genome sequence of the kirromycin producer Streptomyces collinus
RT Tu 365 consisting of a linear chromosome and two linear plasmids.";
RL J. Biotechnol. 168:739-740(2013).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792}.
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DR EMBL; CP006259; AGS73169.1; -; Genomic_DNA.
DR RefSeq; WP_020943578.1; NC_021985.1.
DR AlphaFoldDB; S5VD63; -.
DR STRING; 1214242.B446_31825; -.
DR KEGG; sci:B446_31825; -.
DR PATRIC; fig|1214242.5.peg.6522; -.
DR eggNOG; COG0383; Bacteria.
DR HOGENOM; CLU_003442_0_1_11; -.
DR Proteomes; UP000015423; Chromosome.
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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000015423}.
FT DOMAIN 519..597
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1006 AA; 110481 MW; 65BA8D9FCD5B75B4 CRC64;
MHDDRTLVEA RLRRVLDERI RPAVYPESVP LRVAVWHAPG EPVPVAQGLA AEPVPIEVGA
RWGAPWGTSW FTVTGTVPEA WAGRTVEALL DLGFDENMPG FQCEGLVYRP DGTPVKGLNP
RNQWVRVAAP AAGGEEVRLH VEAASNPVLL DYHPFRPTPL GDLDTAGHEP QYTLTRMDLA
VLDETVWQLV LDLEVLGELM AELPEDSARR HDILRAVDRA LDAVDLQDVN GTADRARERL
SGVLAAPAVP SAHRISAVGH AHIDSAWLWP LRETVRKVAR TTSNMTALLD DEPDFVFAMS
QAQQWAWVKE HRPEVWARVK KAVAGGRFVP AGGMWVESDT NMPGSEAMAR QFVHGKRFFL
DEFGIENEEA WLPDTFGFAA GLPQIIRAAG SKWLLTQKIS WSRTNRFPHH TFQWEGIDGT
RIFTHFPPVD TYNCSMKGAE IAHAARNFRD KGRARHSLAP TGWGDGGGGT TREMVAKAAR
LRDLEGSATV AWETPAAFFA KAEADYPDPP VWVGELYLEL HRATLTSQAK TKQGNRRSEH
LLYEAELWAA TAAVRTGFHY PYEDLDRIWK TVLLHQFHDI LPGSSIAWVH REARATYERV
AAELEGITGA AQRALAGEGD TPLVFNAAPH PRAGVPAGGA ATARTEGATT LRPRPDGGHV
LDNGLLRIEI DARGLVVSAR DLAAGRETIA PGAAANLLQL HADFPNMWDA WDVDEFYRNT
VTDLTDADAV TAGEDGSSVR VVRSFGASRV TQVLSLPPGE GRLVLDTEVD WHETEKFLKL
AFPLDLHAER YASETQFGHF HRPTHTNTSW EAAKFEACNH RFVHLEEPGW GVAVVNDSTY
GHDVTRTVRT RGDRGTTTTV RVSLLRAPRF PDPETDQGVH RFRHALVPGA GIADAVREGW
RINVPERRAT GAGAVSPLVT VDNPAVVVTA VKLADDGSGD VVIRFHEAHG GRATATLELG
FPAADCTVTD LLERPGAEGQ PPALDGDRLT VRLRPFELTT LRLRRA
//
