ID A0A1Q5GSV8_9ACTN Unreviewed; 1011 AA.
AC A0A1Q5GSV8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:OKJ35688.1};
GN ORFNames=AMK22_16490 {ECO:0000313|EMBL:OKJ35688.1};
OS Streptomyces sp. CB01580.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703933 {ECO:0000313|EMBL:OKJ35688.1, ECO:0000313|Proteomes:UP000186318};
RN [1] {ECO:0000313|EMBL:OKJ35688.1, ECO:0000313|Proteomes:UP000186318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01580 {ECO:0000313|EMBL:OKJ35688.1,
RC ECO:0000313|Proteomes:UP000186318};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKJ35688.1}.
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; LIXJ01000010; OKJ35688.1; -; Genomic_DNA.
DR RefSeq; WP_073785858.1; NZ_LIXJ01000010.1.
DR AlphaFoldDB; A0A1Q5GSV8; -.
DR STRING; 1703933.AMK22_16490; -.
DR OrthoDB; 9772207at2; -.
DR Proteomes; UP000186318; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000186318}.
FT DOMAIN 515..593
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1011 AA; 111243 MW; 0729EA92474B1314 CRC64;
MHDDRTLTEE RLDRVLRERV RPAVHPRAVP LRFEVWHAPG EPVPFDEAVG AGYGPGSVGD
AWGPAWGTSW FRVTGRVPED WAGETVEAVI DLGFARDRPG FSAEALAHRP DGSVVKALNP
RNTWLRIGER VTGGEEFTYY LEAAANPEIL DGVSALGDRE TAGDEPLYRV ERMDLAVFDR
QVWELVQDLE VLDQLMRQLP VGSARRWEIL RAVERALDAL DLDAVGASAP AAREILRPVL
SSPAHASAHR ISAIGHAHID SAWLWPVRET VRKVARTTSN VLALMDDHPE FVFAMSQAQQ
LDWLREHHPG LYARVKEKVA SGQFVPVGGM WVESDTNMPG SEALARQFVH GKRFFLEEFG
IETEEVWLPD SFGYSAALPQ LVALSGSRWF LTQKISWNTT NRFPHHSFLW EGLDGTRVFT
HFPPVDTYVA ELSGEELAHA ERNFRDKGHA TRSLVPFGWG DGGGGPTREM LARADRLADL
EGSPRVTVEK PADFFTAAEA EYRRVPVWLG ELYLELHRGT YTSQARTKQG NRRSEHLLRE
AELWAATAAV RTAFRYPHEE LDRIWRTVLL HQFHDILPGS SIAWVHREAE ATYARIAEEL
ESVIGAAQRA LSGSPDEGGT VVFNAAPHER SGIAAGGAAL AANRPEEPRA PIVVEAVDGG
FRLDNGLLRV TVDARGLVVS VVDLVAGRET IAPGCAANLL QVHPDLPNHW DAWDVDAFYR
NTVTDLTGVE AVRRVGDGVE VVRAFGASRV TQVLSLPPGA RRLDIDTEVD WHEREKFLKA
AFPIDVRAEH STAETQFGHV RRPTHTNTSW EAAKFEICAH RFLHVGEPGW GAALVNDSTY
GHDVTRTVRE DGGTTTTVRL SLLRAPRYPD PETDQGVHRL RYALLPGATV GDAVREGWWF
NLPERRVPGS AAVVPLVSVD DDAVVVTAVK LADDGSGDVV VRLHEAHGGR ASARLTTGFA
LAGAAVTDLL ERPLADTSDG SGAASAEGDG VRLRLRPFQI LTLRLTPGDD A
//
