ID K9P702_CYAGP Unreviewed; 1007 AA.
AC K9P702;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:AFY29187.1};
GN OrderedLocusNames=Cyagr_2066 {ECO:0000313|EMBL:AFY29187.1};
OS Cyanobium gracile (strain ATCC 27147 / PCC 6307).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Cyanobium.
OX NCBI_TaxID=292564 {ECO:0000313|EMBL:AFY29187.1, ECO:0000313|Proteomes:UP000010388};
RN [1] {ECO:0000313|Proteomes:UP000010388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27147 / PCC 6307 {ECO:0000313|Proteomes:UP000010388};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792}.
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DR EMBL; CP003495; AFY29187.1; -; Genomic_DNA.
DR AlphaFoldDB; K9P702; -.
DR STRING; 292564.Cyagr_2066; -.
DR KEGG; cgc:Cyagr_2066; -.
DR PATRIC; fig|292564.3.peg.1957; -.
DR eggNOG; COG0383; Bacteria.
DR HOGENOM; CLU_459855_0_0_3; -.
DR Proteomes; UP000010388; 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; 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; 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; 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}.
FT DOMAIN 439..511
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1007 AA; 110439 MW; 6909F46044749406 CRC64;
MPRPLDLQPL WQADQPGGGS GPALGGEWGL RHRPDWAARG LIIWPRGGQW CRLRLRCPCP
QGWAPLAAGA RARLALRWWA DSAELWVDGQ RIHSGDLFDT ACRWPLPERW WRGEALDLEL
RLRSPLHDDG ALISSRIELE PLDPTDPLGL LAATAAELQE LRREHRRDGA PGEGVLQVLG
HAHLDLAWLW PVADTWQAAE RTFTSALDLM ERFDTLHFGH STPALYAWLE RHRPALFARV
RRAMEAGRFE PLNGPWVESD CVLLSTTSLL RQFQEGQAYS LRSFPEWSHR LAWLPDSFGF
AAGLPALAAA TGVRWFCTHK LAWNATNPFP HRLFRWRSRC GAEVLALMTA PIGTDGDPVA
MERYRLQWQR ASGCADALWL PGVGDHGGGP TAEMLEQLAL WQDQPVAAGQ RHGTLRSYLA
PLESLAGQLP VWRDELYLEL HRGCPTSRPD QKRHNRTLER LLREADLAAA LFGRPAPAAT
DDWRTLLFQQ FHDILPGTAI PEVFEQAEPQ WRGARRRASR RRDRALRLGL AAPATSGGTA
AAPSSAAEPW CVVQLQPLPA QPRTLRLPAG DWWLAAADGE RRLAGQPAPG AASWLQIPGL
EGVGVRRLRR QPTPAGSDGA AAPVAGAVRL ERVAGEGPDR WRLGNGLVSA LIGPAGVEQL
FDGDGTPQLG GPLAWCRWRD RGEFWDAWDL AADYRQHPLA WSWQGLPQWL ETGPLCARFV
WRGRCGESPV RLDGRLLAGS PWLELVLGTQ WRQRHELLRL EIPLADPACR WAADTAGGVI
ERPATARTAR ERARWEVSAI SWMAAVGPGR GDGLAVLLDG PQGVSAKAES LGVSLLRAPT
WPDPGADNGW QRQRLALLPC PGGWRAAAAP QQATRLREPL WCRPMEPSAG AGVEAVGAAD
RLFPSLGEDL QLVALRPLPA EENATGDGLE AGAVLLSVQN LGPCRRRFSA GPDWSVLGCC
DALGQPQAAG REHPDDQGPE PLALGPWQLG HWRLRRAPAG SAAAQSS
//
