ID A0A1Q4Z979_9ACTN Unreviewed; 1002 AA.
AC A0A1Q4Z979;
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:OKI43244.1};
GN ORFNames=A6A29_07730 {ECO:0000313|EMBL:OKI43244.1};
OS Streptomyces sp. TSRI0281.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1718998 {ECO:0000313|EMBL:OKI43244.1, ECO:0000313|Proteomes:UP000186952};
RN [1] {ECO:0000313|EMBL:OKI43244.1, ECO:0000313|Proteomes:UP000186952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSRI0281 {ECO:0000313|EMBL:OKI43244.1,
RC ECO:0000313|Proteomes:UP000186952};
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:OKI43244.1}.
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DR EMBL; LWLE01000012; OKI43244.1; -; Genomic_DNA.
DR RefSeq; WP_073721301.1; NZ_LWLE01000012.1.
DR AlphaFoldDB; A0A1Q4Z979; -.
DR STRING; 1718998.A6A29_07730; -.
DR OrthoDB; 9772207at2; -.
DR Proteomes; UP000186952; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000186952}.
FT DOMAIN 515..593
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1002 AA; 110104 MW; 8367D9BAAEE48BDD CRC64;
MHDDRTLTEE RLDRVLRERI RPAVHPRTAP LDIEVWHAPG EPVPFTEAVS APYKPGAVGD
DWGPAWGTSW FKVTGRVPAD WAGLTVEAVI DLGFARDRPG FSAEALAHRP DGSVVKALNP
RNTWLRVGER VSGGEEFTYY LEAAANPELL EGVSALGDRE TAGSEPLYRV ERMEVAVFDR
QVWELVQDLE VLDQLMRQLP VGSARRWEIL RAVERCLDAL DLDGVNATAT AAREQLRQVL
ASPANASAHR LSAVGHAHID SAWLWPLRET VRKVARTTSN VVALMDDHPE FVFAMSQAQQ
LDWLREHQPA LYERVKEKVA AGQFVPVGGM WVESDTNMPG SEALARQFVY GKRFFLEEFG
VETQEVWLPD SFGYSAALPQ LVALSGSRWF LTQKISWNTT NPFPHHSFLW EGLDGTRVFT
HFPPVDTYVA ELSGEELAHA EENFRDKGSA TRSLVPFGWG DGGGGPTREM LARAERLADL
EGSPRVTIET PAEFFAAAEA EYTGPPVWLG ELYLELHRGT YTSQARTKQG NRRSEHLLRE
AELWAATAAV RTGFRYPRAE LDRIWKSVLL HQFHDILPGS SIAWVHREAE ATYARIAEEL
EAVIDAAQRA LAGSSDGGGT VVFNGAPHAR AGIAAGGGTL REPVEEPVEI EEYDGGFRLD
NGLLRVIVDA RGLVVSAVDL ATGRESVAPG CAANLLQIHP DLPNRWDAWD VDSFYRNTVT
DLTGADSVRR VGGGVEVVRG FGSSRVTQLL TLRAGARRLD IDTEVDWHER EKFLKAAFPL
DVRADHSTAE TQFGHVQRPT HTNTSWEAAK FEICAHRFLH VGEPGWGAAL LNDSTYGHDV
TRTVREDGST TTTVRLSLLR APRYPDPATD QGVHRLRYAL LPGATIGDAV REGWQFSLPE
RRVPGTGEVA PLVSLDSDAV VATAVKLADD GSGDVVVRVH EAHGGRAAAR LSAGFPLASA
TVTDLLERPL DGERVTVQGD VVELVLRPFQ ILTLRLAVAA TG
//
