ID K9VDB1_9CYAN Unreviewed; 1283 AA.
AC K9VDB1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:AFZ05235.1};
DE EC=3.2.1.24 {ECO:0000313|EMBL:AFZ05235.1};
GN ORFNames=Osc7112_0642 {ECO:0000313|EMBL:AFZ05235.1};
OS Oscillatoria nigro-viridis PCC 7112.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Oscillatoria.
OX NCBI_TaxID=179408 {ECO:0000313|EMBL:AFZ05235.1, ECO:0000313|Proteomes:UP000010478};
RN [1] {ECO:0000313|EMBL:AFZ05235.1, ECO:0000313|Proteomes:UP000010478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7112 {ECO:0000313|EMBL:AFZ05235.1,
RC ECO:0000313|Proteomes:UP000010478};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Oscillatoria sp. PCC 7112.";
RL Submitted (MAY-2012) 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; CP003614; AFZ05235.1; -; Genomic_DNA.
DR RefSeq; WP_015174566.1; NC_019729.1.
DR STRING; 179408.Osc7112_0642; -.
DR KEGG; oni:Osc7112_0642; -.
DR PATRIC; fig|179408.3.peg.802; -.
DR eggNOG; COG0383; Bacteria.
DR HOGENOM; CLU_003442_1_2_3; -.
DR OrthoDB; 9772207at2; -.
DR Proteomes; UP000010478; Chromosome.
DR GO; GO:0004559; F:alpha-mannosidase activity; IEA:UniProtKB-EC.
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 Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 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 InterPro; IPR013780; Glyco_hydro_b.
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, ECO:0000313|EMBL:AFZ05235.1};
KW Hydrolase {ECO:0000313|EMBL:AFZ05235.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000010478}.
FT DOMAIN 702..780
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
FT REGION 258..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1283 AA; 142497 MW; 6C99D1351CDAA68E CRC64;
MSASVSPASN NIFATVEKLR RLSQVEVQSG WRYCDSDSAV SSVNICNGPV AELNGKGHIA
WPSGKQVLYL GQQFVIPDNL HGYPVVGLRL LLGLTWWAED AQIFVNGELV GRGDLFDFAD
RVLLSSSANP GDEFLVILRL VSPGHDSGAL VRSICLYEAA DSSCFDPGFV AAELEILQNS
LTLNLDFINS QYLSTEIIAN NPMFVKGELL KSEIDLALGS IDWSAVRDRE KFDRSLSVLR
HNLLGYLRAF SGDLDEGTAE GAEAAEGGRR EEVSEVGENS NATSIYIGES GDRRYFSGDL
DEGTAEAAEA AEGGRREEVS QVGENSNATS IYIGESGDRR YFSGDLDEGT AEAAEAAEGG
RREEVSEVGE NGNATSIYIG ESGELTSIYT GKIYLVGHAH LDLAWLWPVP ETWEAAKRTF
ESVLKLQSEF PDLIFCHSTP ALYAWMEQHR PDLFAAIKKQ VAVGCWEVVG GMWLEPDLNL
ISAESMVRQV FYGQRYAKEN FGELMRVAWL PDTFGFGWQL PQILRQGGVD YFVTQKLRWN
DTTEFPHGVF WWEGLDGTKI FSMMSAPIGE SIEAVKMASY AFDWQVKTGL QDALWLPGVG
DHGGGPTRDM LEVAKRWKMS PFFPKLEFAK AVDYLSLIES QFLPEVATTR PESDVPESDN
QENLRAREFS NLSAISDANS PISQLKTIPR TLPIWKDELY LEFHRGCYTT RADQKRQNRR
CEELLYQAEL LSSLATICTG AVYPKSELES AWKQILFNQF HDILPGSAIA QVYTDANLAF
AEVDRACREI LLKSLDAISA QISLPNPPAP DAQPILIFNT LNWSRSEVVA VPLPDAADSA
WQIYDFSRRR LVSQIVRGDR PQSQSTLLFW ANHLPAVGYR VFWLCREDAQ TVDNASASPE
TEKKTELSQL TYGIAQKNTP CQETHFAAAQ MVVENEFIRA TVDGQSGNLS SIWDKVNNRE
VLNAAGGNQL QAFQDSGQYW DAWNIDPNYE KHQLPAPILK DISWIAQGEI RQSLRVVRQI
GKSEFCQDYI VEIGSPLLKI KTVVDWQEKH VLVKAAFGLN VEADLATCEI PGGAIARTTK
PQTPAEKAKW EVPILRWTDI SNDGFGVSLL NDCKYGCDLQ PNRIRLTLLR GSTWPDGQAD
VGVSEFTCAV YPHSGNWQEA GTVRRGCELN LPLLVKVLPQ LGENRNKSLP AVGKFLDLSA
DNLVLMAFKQ SEDDSNVWIL RCCESEGKET VLEFNSDLGL EIVEPVDLLE RPANLSEKLP
EGRGFKIEPW KIASFAVVPK TDT
//
