MANB_DICDI
ID MANB_DICDI Reviewed; 1035 AA.
AC Q54YF7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Alpha-mannosidase B;
DE EC=3.2.1.24;
DE Flags: Precursor;
GN Name=manB; ORFNames=DDB_G0278259;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family. {ECO:0000305}.
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DR EMBL; AAFI02000023; EAL68302.1; -; Genomic_DNA.
DR RefSeq; XP_642245.1; XM_637153.1.
DR AlphaFoldDB; Q54YF7; -.
DR SMR; Q54YF7; -.
DR STRING; 44689.DDB0231612; -.
DR PaxDb; Q54YF7; -.
DR EnsemblProtists; EAL68302; EAL68302; DDB_G0278259.
DR GeneID; 8621454; -.
DR KEGG; ddi:DDB_G0278259; -.
DR dictyBase; DDB_G0278259; manB.
DR eggNOG; KOG1959; Eukaryota.
DR HOGENOM; CLU_004690_3_0_1; -.
DR InParanoid; Q54YF7; -.
DR OMA; HHEVNVQ; -.
DR PhylomeDB; Q54YF7; -.
DR Reactome; R-DDI-8853383; Lysosomal oligosaccharide catabolism.
DR PRO; PR:Q54YF7; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
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 Gene3D; 1.20.1270.50; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.20.110.10; -; 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 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; SSF74650; SSF74650; 1.
DR SUPFAM; SSF88688; SSF88688; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Glycosidase; Hydrolase; Metal-binding; Reference proteome;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1035
FT /note="Alpha-mannosidase B"
FT /id="PRO_0000327841"
FT ACT_SITE 161
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 446
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 710
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 719
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 735
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 792
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 852
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 863
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 880
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 962
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 993
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1035 AA; 119087 MW; A48F295BD41AA936 CRC64;
MGKVLILFLF VLLLITFINC TNNKILNNEN SSNEDNVINV FLIPHSHCDL GWVQTLEEYY
SENVTVILDN VINTLIKDSS KKFNWAEIYY FETWWNEQSS FLQAQVRNLV NNGQLYFVGG
GWAQNDEGAT HYQAVINQMT LGHQFLLSEF GVVPEIGWQI DPFGPSTLTA TLFSLMGFKY
HVINRIDERI KYIYNDTPDI VGSGWMTTDR SFEFQWYPSH NDQELSIFTH VLDHHYNSPY
LIYPNASNPN QSLTTGFDFE SDPTQNPPIN QSNIYERAAV FVEIMQQRSQ LYRHNNLLIP
FGNDFRFQNA SLEFDNMDKL ITYINSNSSW GVTIQYATLN EYFEKVESIE PPVEYADIVG
QDLFVYTMCL ASDYQAFNTC ANWWSGYYTS YPLLKQTARD SDSLLRVGEM LYSLSCFYSN
GFDFDFNIGF YALSMHRNVS GILTHHDAIT GTAKEYVRVN YFQMLNEAQS LTLDYNIPDF
VGFLLSNKSL NIDYQSNGSS ILNSTNPGDI IAISFTNSIA WDRIETVSIE IPFVNMAVYD
YQLNPIQSQI VQRFDKSNNW YLYFQVATPA LGISTYFIVI LSTDGEILND NSKNLPTPIQ
SILSISNELL FNDNDDETTT TTIGNSNFNL NFKFDRDNNN LLTLNSYDDL FNNKIGIPIS
QHLIEYTSLS DDAYKFRVQG LPIPLTPINP QFYLTIGPVV QIVTIIYNNN CSQSYLIYND
TTSFNPFETD NDNNNNSRLI KNDQYFEIDN IVASGWDKEI SMKFTTNINN QNIFYTNNGL
EIMKRQWEIH WNDTFIWSEI TSNFYPMINT GYIVDQQVSD YQQQLTILSK QTFGASSQTN
GEFEVLLIRR SNYTQWSVHE PMNDTSNPSL RVLCIFGDPN FSNEIRTPHS ILFENPLQPV
YSLIPNSIPI EKYIDTYNTL FKPLQTSLPY NLHLLTFTKQ WIDSPSIIMR LINIYEIGQS
INFSKSINFN IGSGDNNNNN NNNNNNGFLT HYNISQIIET TLSANSELSN PTNNLVITLE
PLEIKTFLLT LSPKQ
