ID A0A1Q5DAW8_9ACTN Unreviewed; 1018 AA.
AC A0A1Q5DAW8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:OKI93023.1};
GN ORFNames=AMK18_29895 {ECO:0000313|EMBL:OKI93023.1};
OS Streptomyces sp. CB01249.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703929 {ECO:0000313|EMBL:OKI93023.1, ECO:0000313|Proteomes:UP000186839};
RN [1] {ECO:0000313|EMBL:OKI93023.1, ECO:0000313|Proteomes:UP000186839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01249 {ECO:0000313|EMBL:OKI93023.1,
RC ECO:0000313|Proteomes:UP000186839};
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:OKI93023.1}.
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DR EMBL; LISW01000009; OKI93023.1; -; Genomic_DNA.
DR RefSeq; WP_073865307.1; NZ_LISW01000009.1.
DR AlphaFoldDB; A0A1Q5DAW8; -.
DR OrthoDB; 9772207at2; -.
DR Proteomes; UP000186839; 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:UP000186839}.
FT DOMAIN 529..607
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
FT REGION 645..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1018 AA; 112251 MW; AD0F5915CBD2E297 CRC64;
MHHDRTVTES RLARVLDLRL RPAVYRESLP LDIAVRPVTG EPVPVAEGIG APYEPVRTGD
LWGPAWSTTW FRISGTVPAG WAGQRVEAVL DLGFGTTQPG FSAEGLVHRP DGSPVKALNP
RNAWLPITER AEGGEEFVYY IEAAANPVIF DSGSGDDPFV PTRAGGAPPW LGGETAPDTP
LYRLNRMDLA VFDPTVWELV QDLDVLSGLM HQLPEDSTRR WQLTHAVDRA LDAIDLQDIG
GTATRAREVL APALASPAHA GAHRVSAVGH AHIDTAWLWP VRETVRKAAR TVSNVTALMD
DHPGFRFVMS QAQQLAWLKE QRPEVFARVV EKVRTGQFIP TGSLWIEPDT NLSGGESLVR
QFVHGKRFYL EEFGVETEDM WLPDTFGYNA ALPQIMKLAG IKWFLTQKIS WNATNPFPHH
TFWWEGIDGT RIFSHFPPVD SYNGDLSGAD IAHTERNFRD KGAANRSLVP FGYGDGGGGP
TREMLARARR LENLEGSARV EMESPEEFFT KAQAEYTDAP VWSGELYLEL HRGTLTSQLA
TKQGNRRSEH LLREAELWSA TAALRTGLPY PYELLDRVWK TVLLHQFHDI LPGTSIAWVH
REAETVYAET ARELGEVIDS AQRALAASGA EGTARETVFN AAPHTRDGIP ALGGSPRARA
ARPVEPHPAD GCGFVLDNGL VRITVDSRGL ITSAYDLTVG REALAPGTVG NLLQLHQDFP
NQWDAWDVDA FYRNTVRDLT DADEVVAVPG GVRVVRGFNA SRITQVLRLE ENSRRLDVET
DVDWQECEKI LKAAFPLDIR AAESSAEIPF GHVRRPTHTN TSWDSARFEV CAHRYLHVEE
PGWGAALVND SNYGHDVTRD VRPDGGTTTT VRLSLLRAPL FPDPDCDRGE HRLRYGLVIG
AGLRDAVREG YRFNLSERVV PGGAPVEPLV RASGGDVVIE TVKLADDRSG RVIVRLYESA
GGRARTTLRT GFPLAGARIT DLLERELTDE PAPAVDGQDI HLTLRPFQIL TLCLTPGA
//
