ID   A7NMZ2_ROSCS            Unreviewed;      1061 AA.
AC   A7NMZ2;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   02-SEP-2026, entry version 81.
DE   RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE            EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
GN   OrderedLocusNames=Rcas_2851 {ECO:0000313|EMBL:ABU58921.1};
OS   Roseiflexus castenholzii (strain DSM 13941 / HLO8).
OC   Bacteria; Bacillati; Chloroflexota; Chloroflexia; Chloroflexales;
OC   Roseiflexineae; Roseiflexaceae; Roseiflexus.
OX   NCBI_TaxID=383372 {ECO:0000313|EMBL:ABU58921.1, ECO:0000313|Proteomes:UP000000263};
RN   [1] {ECO:0000313|EMBL:ABU58921.1, ECO:0000313|Proteomes:UP000000263}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13941 / HLO8 {ECO:0000313|Proteomes:UP000000263};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Bryant D.A., Hanada S., Tsukatani Y., Richardson P.;
RT   "Complete sequence of Roseiflexus castenholzii DSM 13941.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing alpha-D-mannose residues
CC         in alpha-D-mannosides.; EC=3.2.1.24;
CC         Evidence={ECO:0000256|ARBA:ARBA00000365};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792}.
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DR   EMBL; CP000804; ABU58921.1; -; Genomic_DNA.
DR   RefSeq; WP_012121345.1; NC_009767.1.
DR   AlphaFoldDB; A7NMZ2; -.
DR   STRING; 383372.Rcas_2851; -.
DR   KEGG; rca:Rcas_2851; -.
DR   eggNOG; COG0383; Bacteria.
DR   HOGENOM; CLU_003442_0_1_0; -.
DR   OrthoDB; 9772207at2; -.
DR   Proteomes; UP000000263; 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   FunFam; 1.20.1270.50:FF:000004; alpha-mannosidase 2C1 isoform X1; 1.
DR   FunFam; 3.20.110.10:FF:000002; alpha-mannosidase 2C1 isoform X1; 1.
DR   FunFam; 2.70.98.30:FF:000001; alpha-mannosidase 2C1 isoform X2; 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   Gene3D; 2.70.98.30; Golgi alpha-mannosidase II, domain 4; 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, ECO:0000313|EMBL:ABU58921.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABU58921.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000263}.
FT   DOMAIN          536..613
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
FT   REGION          34..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1061 AA;  121072 MW;  6F22FA6F4DF4C80D CRC64;
     MLFFTVEKLK ARLEEMRAAI IRDTRPITDV FTCPVPGAPS EHAMSPPPPP DDPSWRPLKV
     GERWGGDPHN PDKPDEPLPW GMPVDGGHTH WLRAIIRIPE EWRGRQVLMR MRWSAEGHAG
     IEGIAYLDGT TLAGIDEPHP AILLPEHAHE GDHELLIRCY TPYRRSFGGL ELQLRSDIIA
     RLAAVMYAIL DALPTYRDSD PEKHALLDRI NRAYNLLDLR EGWQSERFEI SAGAALTFLR
     ETLTANLAPG QRPIILATGH AHMDVAWLWP LWRTHQKIAH TVATALHLME RYPEYHFSMS
     QPQTYAFLKQ DDPELYERLR QRVAEGRFEP VGAMWLEPDC NVTGGESLVR QVIHGIRFFE
     NEFGPIEHIV WLPDVFGYSA ALPQIMRLAG ISCFMTTKIS WNQFNRMPYD TFRWRGIDGS
     EVLAHFVTAT SAPVKPNPTE AQFYTYNGSM LPSEVFGTWN HYRQKDINDE VLYIYGHGDG
     GGGPTEEMLE LARVMADLPG FPVVQPGRVE QYFQRLRQRV WNNPRLPVWV GELYLEYHRG
     TYTSQARTKQ NNRQAELLLR EAEWLNAWAV THGAINRQAD LDAAWRTVLL NQFHDILPGS
     SVPLVYVESE QQFAEVRDTV ETVRHAAITD LTGSHSNGAA PHLAVFNGLA WDRTECVAIP
     LEDLRQPLIE GPTQVVEQID GTRTLLVEAT VPAFGYAALR AARHPSPPAQ FITRRDYLAS
     DEFRIEFDAN GEIGSLYDAR YEREIIAEGA TGNQLVLYED RPMFWDAWDI DPFYLEKPYP
     IHNISEWRVI EEGPLRATVE IARRFGRSTI RQRISLWHNN RRIDFETEVD WQERQNLLRV
     LFPLRLNAAR ATCEIQFGAV ERPTHRNTSW DWARFEVCAH RWIDLSEGGY GVALLNNGKY
     GHSLLHNTLG ISLLKSAVIP DPQADRGLHR FIYSLLPHAG DWREAQVTRR AYELNAPLRP
     VTVAGEIPAE GRSFLHVDSD HVIVETIKTA DDGDGLIVRM YEAHNQRGQV RLEFGQPVES
     AVEVDLLERE TGPVTVDGRT VRCNVRPFEI KTIRVRLKPP L
//