ID A0A1Y5KDR6_9BACL Unreviewed; 1066 AA.
AC A0A1Y5KDR6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:OUS76781.1};
GN ORFNames=B1748_09315 {ECO:0000313|EMBL:OUS76781.1};
OS Paenibacillus sp. MY03.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=302980 {ECO:0000313|EMBL:OUS76781.1, ECO:0000313|Proteomes:UP000195591};
RN [1] {ECO:0000313|EMBL:OUS76781.1, ECO:0000313|Proteomes:UP000195591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MY03 {ECO:0000313|EMBL:OUS76781.1,
RC ECO:0000313|Proteomes:UP000195591};
RA Liu H., Cheng Y., Gu J.Y., Han W.J.;
RT "Draft genome of a polysaccharide-degrading bacterium Paenibacillus sp.
RT MY03.";
RL Submitted (MAR-2017) 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:OUS76781.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MXQD01000008; OUS76781.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5KDR6; -.
DR OrthoDB; 9772207at2; -.
DR Proteomes; UP000195591; 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; cd10789; GH38N_AMII_ER_cytosolic; 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; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000195591}.
FT DOMAIN 520..599
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1066 AA; 121692 MW; 7486DEEA0DFC8857 CRC64;
MLLTVEKLER RVKELSPFRY TNRQEIGQFL FWKDEAAEVA AMPPQDAEWT EVGLGYRWGD
RDVTAWLRTE VTLPAHQGRN IVGLFNFGKT GPGHTSGFES LLFIDGTPFQ GVGTFHQEVF
FPEELAGRKI ELLFKVWSGL PGFGPLSELR HILQQAELTL LQQQTDDLYF TASAAMETIK
VLDSNSWERH ALVKAVDRAF LLVDYRNPGS AAFYESVTAA AVKLHEEIES IPKNNEVTVR
AIGHTHIDVA WLWRLKHTRE KSARSFSTVL RLMERYPEYA FLQTQPQLYD DLSRDYPVLF
EQIKKRVKEG RWEAGGAMWL ESDCNIPNGE SLVRQLMYGM RYYEQTFGVS CDYLWLPDVF
GYSWALPQIL KKSGINYFMT TKISWNVYNR FPHDTFYWRG IDGTEVLTHY ITTPEPGQAA
DSLTKYYTYN GQVLAETVNG IWKNYRDKEV NDELLLAYGW GDGGGGPTRH MLEMRRRLEH
MPGLPRVTTG RVDEFFHQLE HTVDKSDRYV HRWNGELYLE LHRGTYTSQG YVKRMNREME
SLLHTAEAAG VLHGIVSGFK DYPKDTLDES WKIVLRNQFH DILPGSSIAE VYEDCHVEYG
EAERLAREAL GTSLSGLAGR LPLAPAGEQC WIVVNSLGMA RDELVELAWQ EDFAIGGSWT
DADGNHLTAE AVVKESGERS VLVRIPNIPA FGYKTISYSS AVESAVSVAE PSIIVKEQGL
STPFYELTWN SHGQLDRLYD KRTERELIAP GEAANRFDVH EDKPTAHDNW EIDIFYYEKH
RQINGLQSVV IAENNPLRTV VRMTWNDGET TIKQDMIVYP DNPRIDFVTW VNWQEREQLL
KVAFPLNVSS TYATHEIQFG NVRRPTHWNT SWDFAQFETC AQRWIDLSER GCGVSLLNNC
KYGHDVRDNV MRLTLIKSSN DPDPTCDLGE HVFTYSLLPH DGDWFEAGTL EQAARLNTKP
ETLKLSNLAQ GSAEAIPLTF GLLAIEGGHV VVDTVKRAED SDALIVRCYE YAGMRGNVSL
RFNASVAEVA EVNLMEREAR EIAHQSNQFA VHFTPYELKT FRVVLS
//