ID F9VKA2_ARTSS Unreviewed; 1043 AA.
AC F9VKA2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:BAK56560.1};
GN OrderedLocusNames=SFBM_0790 {ECO:0000313|EMBL:BAK56560.1};
OS Arthromitus sp. (strain SFB-mouse-Japan).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Candidatus Arthromitus.
OX NCBI_TaxID=1029718 {ECO:0000313|EMBL:BAK56560.1, ECO:0000313|Proteomes:UP000001636};
RN [1] {ECO:0000313|EMBL:BAK56560.1, ECO:0000313|Proteomes:UP000001636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SFB-mouse-Japan {ECO:0000313|Proteomes:UP000001636};
RX PubMed=21791478; DOI=10.1093/dnares/dsr022;
RA Kuwahara T., Ogura Y., Oshima K., Kurokawa K., Ooka T., Hirakawa H.,
RA Itoh T., Nakayama-Imaohji H., Ichimura M., Itoh K., Ishifune C.,
RA Maekawa Y., Yasutomo K., Hattori M., Hayashi T.;
RT "The lifestyle of the segmented filamentous bacterium: a non-culturable
RT gut-associated immunostimulating microbe inferred by whole-genome
RT sequencing.";
RL DNA Res. 18:291-303(2011).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792}.
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DR EMBL; AP012202; BAK56560.1; -; Genomic_DNA.
DR RefSeq; WP_005806236.1; NC_015913.1.
DR AlphaFoldDB; F9VKA2; -.
DR STRING; 1029718.SFBM_0790; -.
DR KEGG; asf:SFBM_0790; -.
DR eggNOG; COG0383; Bacteria.
DR HOGENOM; CLU_003442_0_1_9; -.
DR OrthoDB; 9772207at2; -.
DR Proteomes; UP000001636; Chromosome.
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}.
FT DOMAIN 515..592
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1043 AA; 121038 MW; C29841584F5C4264 CRC64;
MTYLLERIDK ICREIQKHIY KNTINIDNFM YVDGNYHNIE LIKEVSEDKW RKFKSGDLWG
GRDCHGWFKF SVVVPENFTG QTIALNLSTF EEGWDATNPQ FIIYVDGEHI QGVDINHREI
ILTHNAIAGK KYDIDLHAYA GMLADKKATL NGKFTVIDMN ARELYWNLKV PLDVCKELDK
EDKNRVDMIT VLNDAINIID LRKPYSKEYD DSIKKANEFL NTKFYGELCG HEDVIATCVG
HTHIDIAWLW TVAQTREKVA RSFSTVLKLM EEYPEYIFMS SQPQLYKMLK EDHPKVYKRV
KEKIKQGVWE PEGAMWVESD CNVTSGESLI RQIVHGKRFF KEEFEVDNKI LWLPDVFGYS
AAIPQILKKS GIKYFMTTKI SWNQFNKIPN DAFMWQGIDG SEVLTYFITT SGPGQDKLSF
FTTYNGHIQP DAVMGSWRRF QNKNLTNDVL ISFGWGDGGG GATLEMLENG RRLAKGIPGA
PRVKMGTSLE FFQKLENKIS NHKKLPKWVG ELYLEYHRGT YTSMARNKRD NRKCENLYLA
LEKLNSLSMI FGDNYTQKEI NDAWETILLN QFHDIIPGSS IKDVYDVTKV EYKELLDKVT
QLIDKTIDSI SDKINLKNQS VVVFNTLGFE RDDIVEFDIP KNIKNPLLID DNGNEIVCQL
ISESKAIFFA KAIPANGYKT FKIIESMNKE IKTDIILTID FAENRFFKIK FDNKGQITSF
INKMQNREII KIGHIGNQLQ AFEDKPMCFD NWDIDIYYKE KMWLIDDIQD IEVIENGPVR
STLRIKRKFL DSIIIQYVYI YNDIERVDFN TYVDWKENDI LVKVSFPIEV NAKDATYEIQ
YGNVTRPTHN NTSWDLAAFE VCGHKWVDLS EGNFGVSLLN DSKYGHDIKN GNMRLTLLKS
TGDPNPDADK EEHFFTYSIY AHDKTWQEAK TVQLAYNLNT KLFSKVCNAH SGELNNNLSL
AKLNKENVMI EVIKKAEDSD YLIVRLYEFH NKRTSVSIEF IKNIQLAYEC DLLENNLEII
TPNANKFDFE IKPFEIKTFK IKL
//
