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Database: UniProt
Entry: A0A0Q3WVH2_9BACI
LinkDB: A0A0Q3WVH2_9BACI
Original site: A0A0Q3WVH2_9BACI 
ID   A0A0Q3WVH2_9BACI        Unreviewed;       909 AA.
AC   A0A0Q3WVH2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:KQL52919.1};
GN   ORFNames=AN964_04935 {ECO:0000313|EMBL:KQL52919.1};
OS   Heyndrickxia shackletonii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX   NCBI_TaxID=157838 {ECO:0000313|EMBL:KQL52919.1, ECO:0000313|Proteomes:UP000051888};
RN   [1] {ECO:0000313|EMBL:KQL52919.1, ECO:0000313|Proteomes:UP000051888}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 18435 {ECO:0000313|EMBL:KQL52919.1,
RC   ECO:0000313|Proteomes:UP000051888};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQL52919.1}.
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DR   EMBL; LJJC01000004; KQL52919.1; -; Genomic_DNA.
DR   RefSeq; WP_055738630.1; NZ_LJJC01000004.1.
DR   AlphaFoldDB; A0A0Q3WVH2; -.
DR   STRING; 157838.AN964_04935; -.
DR   PATRIC; fig|157838.3.peg.1094; -.
DR   OrthoDB; 9764050at2; -.
DR   Proteomes; UP000051888; Unassembled WGS sequence.
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; cd10814; GH38N_AMII_SpGH38_like; 1.
DR   Gene3D; 2.60.40.2210; -; 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   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR041509; GH38_beta-1.
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:SF2; MANNOSYLGLYCERATE HYDROLASE; 1.
DR   Pfam; PF09261; Alpha-mann_mid; 1.
DR   Pfam; PF17677; Glyco_hydro38C2; 1.
DR   Pfam; PF18438; Glyco_hydro_38; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051888}.
FT   DOMAIN          298..371
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   909 AA;  104120 MW;  69717B5CBB0A3CD0 CRC64;
     MEKKKHIHII SHTHWDREWY LPYEKHHVLL VKLVDQLLET LDRDEHFRSF HLDGQTIILD
     DYLQVRPEMR EKLQKYIKDG RIQIGPWYIL QDEFLTSSEA NIRNLQYGMK DALQWGGISK
     VGYFPDSFGN MGQAPQILKQ AGIEAAVFGR GVKPTGFNNM VSDVDMYESP YSEMFWRSPD
     GSAVLGVLFA NWYCNGIEIP ADKEEAAVYW EQKIAALEKY ASTNHHLMMN GCDHQPIQTN
     LSKAIQTAEQ LYPDIQFVHS NFNDYLAELM TTLPKDLKYI DGELRSQQTD GWGTLVNTAS
     ARIYLKQMNQ RGQVLLEKVA EPLATFAYMT GEEYPHHLFT YAWKTLMQNH PHDSICGCSV
     DEVHREMETR FEKSKHVAEM IVDEKLTQIS DKIDTTGFAP FGAEAVPFTV FNTTGWERTG
     VVSVTVDVKS EYFSEGVNKE ALKSFPLNDR EIVDQDGNVI PFTMEDLGIA FDYDLPNDRF
     RQPYMARRVQ LSFEAHAVPA LGYKTYAFVK KETTLPETES LIVNDREAEN EWLHVKIEEN
     GSLTVTDKTM NRTFTDLLIY EDSGDIGNEY MYKQPDGEEN LTTKNSKAKV HILKDTPFEA
     AFEIIHEWEL PRGANELLAQ EQKEVIPFMN RIAQRVEETV PFKIKTVLTI EKNSKGITVS
     TTFNNQAKDH RLRALFPTDV ETSVHYADSI FEIAKRNNVP ADEWTNPSNC QHQQAFVSVC
     NQSEGLTIAN LGLNEYEVLQ DGRNTIALTL LRAVGELGDW GYFPTPEAQC LGEHTVTFRI
     YPHTGDCIET NAYQDAYQFQ IPWVAKQTGI HEGTLPTVHS FIEWNAEHLS LSSVKVAEGS
     GDIMVRWFNT ANQEDQLTIH SCGREQCYRS NVIEENVEML PLNENGNWQA PVQPYEIITV
     GLERKEYHQ
//
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