ID F0Z8X5_DICPU Unreviewed; 1068 AA.
AC F0Z8X5;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752, ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN ORFNames=DICPUDRAFT_96508 {ECO:0000313|EMBL:EGC39652.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC39652.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361199};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU361199};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792, ECO:0000256|RuleBase:RU361199}.
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DR EMBL; GL870954; EGC39652.1; -; Genomic_DNA.
DR RefSeq; XP_003283873.1; XM_003283825.1.
DR AlphaFoldDB; F0Z8X5; -.
DR EnsemblProtists; EGC39652; EGC39652; DICPUDRAFT_96508.
DR GeneID; 10509747; -.
DR KEGG; dpp:DICPUDRAFT_96508; -.
DR eggNOG; KOG1959; Eukaryota.
DR InParanoid; F0Z8X5; -.
DR OrthoDB; 11472at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004559; F:alpha-mannosidase activity; IBA:GO_Central.
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; cd00451; GH38N_AMII_euk; 1.
DR Gene3D; 2.60.40.1360; -; 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; 2.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 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 InterPro; IPR013780; Glyco_hydro_b.
DR PANTHER; PTHR11607; ALPHA-MANNOSIDASE; 1.
DR PANTHER; PTHR11607:SF39; ALPHA-MANNOSIDASE D-RELATED; 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:0000256|RuleBase:RU361199};
KW Hydrolase {ECO:0000256|RuleBase:RU361199};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361199};
KW Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361199};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT CHAIN 22..1068
FT /note="Alpha-mannosidase"
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT /id="PRO_5041015994"
FT TRANSMEM 1026..1046
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 347..428
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1068 AA; 126069 MW; 1D327052F9E2389B CRC64;
MKLGRVLFIL IFIKLFFSIN SYIINNSSDD KINNFKITKI KEEGYKIFII PHSHCDNSWL
KTKEEYYNGT VQYILTSVIK ELKNDPEKKF NWAEIGFFYE WYINQDNSTQ EIVKQLVLNK
QFEFLTGGWV QSDEATVSLD DVIDQMTQGH MWIKDTFNVT VQYGWQIDPF GYSSLTPTLF
SRMGIKGLII NRISYNVKNY MKKKREMEFL WKGSETLDTD SELLISTLDN HYDYPEMLNP
KNKYPISQRV KKYLEYLEQI SKTRISKTIL LQIGDDFTHY NAKKDFSASD EWLSYIKERK
EEYGIKEIKY ATLSEYFEQL KKDIESENIK LNVFNKDFFP YATSEKEYWT GYYTTRPTLK
RQIRDVGNLI RISDSMFSIL NIKNNITVSN SLYQDLNENR NVLSDAQHHD TITGTSRSYV
LFDFFLKLEK ARISSYNIIS NSYNLLNNIS NSEPLQYQNI IDLDDLKDEY YSVVFFNSLG
WSVKQHISIK IKTNNTIALS QISLLNSNLS IISDIQIVSL NYKNRCFEND DLYLLFAIIE
IPPMGYSTYY LSLNENKSNS NQIVHGKIIY FPNNLVFKTK EIEYEFSRNG YLKSIKNIKS
NKMTLINQAF YQYQSKESGP YIFNAGTIEN TLKKPSYFIL YEGSLVNQLT MVFDSGDCGT
ISMVNQRIYN NPNLNELSLI TEKYLETSYS FTGEMNKEKI IRYKVKSFSS NNNEFYTDNG
LETRKRVYRE GSTSSNYYPT LHYVNIKDKL KDEQYTLYVD RSVGVTYPSK GEIEIMLHRT
MENDDWKGVQ WPSKDISRID GKIYFNFDTI ENQKQHEKKL SLQIDHNPIY LIKKISNIKQ
LKNNPIQHQS QFILKDLPDN IHLQSLKTYS NNRIGLRLLK INQDNNNNNH STYLNYIKVN
PNHLVETGLS FLEISKDNFL NISKNNFKDN NFPIYSGQSE YIYKKTYQNN TNHFYPLEIK
SFIINLNNNN NNNNNLKVYN YNNHFTYDKN NISIYYQYDF SAIPLELSHY NDIGQYKQKS
HIWRNLFIIL TPTILLAIGI IVYIKYNQRF IFKEKSEYIM LNTIDYSI
//
