ID   A2CCI5_PROM3            Unreviewed;      1004 AA.
AC   A2CCI5;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   02-SEP-2026, entry version 82.
DE   SubName: Full=Glycoside hydrolase family 38 {ECO:0000313|EMBL:ABM79195.1};
DE            EC=3.2.1.24 {ECO:0000313|EMBL:ABM79195.1};
GN   OrderedLocusNames=P9303_24641 {ECO:0000313|EMBL:ABM79195.1};
OS   Prochlorococcus marinus (strain MIT 9303).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=59922 {ECO:0000313|EMBL:ABM79195.1, ECO:0000313|Proteomes:UP000002274};
RN   [1] {ECO:0000313|EMBL:ABM79195.1, ECO:0000313|Proteomes:UP000002274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9303 {ECO:0000313|EMBL:ABM79195.1,
RC   ECO:0000313|Proteomes:UP000002274};
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792}.
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DR   EMBL; CP000554; ABM79195.1; -; Genomic_DNA.
DR   RefSeq; WP_011827046.1; NC_008820.1.
DR   AlphaFoldDB; A2CCI5; -.
DR   STRING; 59922.P9303_24641; -.
DR   KEGG; pmf:P9303_24641; -.
DR   HOGENOM; CLU_003442_1_2_3; -.
DR   BioCyc; PMAR59922:G1G80-2155-MONOMER; -.
DR   Proteomes; UP000002274; Chromosome.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR   GO; GO:0009313; P:oligosaccharide catabolic process; IEA:TreeGrafter.
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; 2.70.98.30; Golgi alpha-mannosidase II, domain 4; 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, ECO:0000313|EMBL:ABM79195.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABM79195.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002274}.
FT   DOMAIN          477..559
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1004 AA;  113106 MW;  ECF2AAA7A7DCF74F CRC64;
     MQEQLQARRL AWIETFRSRS RWDLKPGWYR VGDRDRRSLL QDDWAQIHRP DWVGRGLLVW
     PRGGLWLQLQ QEILCPEDWR QAQASCLRLV LGWWADQMRL WVDGVLVHEG DLFDTTCRWS
     LPESIGWERP LTLLLELRSP SHDDGALINS ELVLEPRAGA VDLDQVLLPE ALALYLEVAE
     VLPEAWLELD PHSQEATVAV DQQLRNAARP PGLIHWIGHA HLDLAWLWSV ADTWQAAERT
     FRSVLHLMQR FPDFHFSHSS PALYQWVEHH RPTLFAALQD ASRAGRWEPI NGPWVETDCV
     LVSTASLWRQ FTLGQQYSRS AFPEWSHHLA WLPDSFGFAA GLPAVATQTG IRWFCTHKLA
     WNASNPFPHR LFRWCSRGQA EVLALMLPPI GTDGNPMAML REQRSWQAST AVEEALWVPG
     VGDHGGGPTA EMLEQLQLWE DHPQALPQKP GTVRSYLETL EAHIETLPVW RDELYLELHR
     GCATTRPDQK RQNRHLERLL READLAIALL ACHLGDRADI PGTSASSLPD WRPLLFQQFH
     DILPGTSIPE VFEQAKPVWR SSCRESRRSR DQHLQQLFRS GVSCSDRFDP ESSAGCWVWM
     GLQPLQRWSP VLRLPRDQWG SAGRKLPCQE AKGGGTWVQL PVQQGVTAVP LQRSVSKALD
     VVDGLPVRGA VQIQPLDQGG WRIGNGLLEA DFGAEGLQQL WDRNGTPQLA GPLIWGRFRD
     RGEFWDAWDL ATDYRQHPLD LNWNGSIELV ERGPLVARLV LRGWAGSSAL RLDVQLRADC
     PWLELRLGVD WRQSHELLRL EVPLACSAVR WAADTSGGVI ERPAEAMTAR EKARWEVPLI
     SWLASESAAP GGGLAVLLDG PQGVQVCPDR LGVSLLRGAT WPDPSADRGW HRQQLALMPV
     PDGWSREAVP QAALAFREPG WLGPSDLKVS WSGLPSLPSK LVPLAVTYAE VRQLKLSVLN
     AGATRQSWAV GKTWRVGSAH ESCLGEAVEL KPGELAELLL ERVD
//