ID Q92EN4_LISIN Unreviewed; 875 AA.
AC Q92EN4;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE SubName: Full=Lin0424 protein {ECO:0000313|EMBL:CAC95657.1};
GN OrderedLocusNames=lin0424 {ECO:0000313|EMBL:CAC95657.1};
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626 {ECO:0000313|EMBL:CAC95657.1, ECO:0000313|Proteomes:UP000002513};
RN [1] {ECO:0000313|EMBL:CAC95657.1, ECO:0000313|Proteomes:UP000002513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262 {ECO:0000313|Proteomes:UP000002513};
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.D.,
RA Fsihi H., Portillo F.G., Garrido P., Gautier L., Goebel W., Gomez-Lopez N.,
RA Hain T., Hauf J., Jackson D., Jones L.M., Kaerst U., Kreft J., Kuhn M.,
RA Kunst F., Kurapkat G., Madueno E., Maitournam A., Vicente J.M., Ng E.,
RA Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.C.,
RA Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA Vazquez-Boland J.A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792}.
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DR EMBL; AL596164; CAC95657.1; -; Genomic_DNA.
DR PIR; AI1485; AI1485.
DR AlphaFoldDB; Q92EN4; -.
DR STRING; 272626.gene:17564751; -.
DR CAZy; GH38; Glycoside Hydrolase Family 38.
DR KEGG; lin:lin0424; -.
DR eggNOG; COG0383; Bacteria.
DR HOGENOM; CLU_003442_2_1_9; -.
DR OrthoDB; 9764050at2; -.
DR Proteomes; UP000002513; 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; cd10815; GH38N_AMII_EcMngB_like; 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:SF2; MANNOSYLGLYCERATE HYDROLASE; 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 277..355
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 875 AA; 100131 MW; EF304A498F605DD5 CRC64;
MAKTKVHVIP HSHWDREWYF TSSRSTIYLV KHLKEVIETL EAKDNYHFYL MDAQSSLIED
YLRYCPEDKT RLEKLIAEKR LITGPWYTQT DQLVISQESI VRNLLYGTRI AREMGHSMAV
GYVPDAFGQG GNMPQIYKEF GISKFLFWRG VADNRLKQTE FIWRGDDGTE MLAEQIPFGY
YYGANIPENE AELKTYLDEQ IGALEEKAST PNVYFPNGLD QAPVRKNLPE LVAKFNELDH
SREYQIASPE TFFADLEKDV TDLPVIAGEL TEGKHSRLHK SIFSTRADLK QANNEIENFL
SNVLEPVLSI SYSLGNRYPH NELAEIWKLM FENAAHDSIG GCNSDTTNRD VKHRYKLASD
LATNLLDLNM RLISEKIAQK QPFQFTVFNP LPYEKSGVIK MTAYIPEDNF TIEDTRGNTL
EYTILEKKDL TEYVLNQHIY LNPSKPVYLP EKVFLATMLV DVNSIPALGY DTIYFNLEKE
VAEQQPKQSA ETKIENEFYK IQLADNNSLT IHDKKSGRTY TDQMIFVENG DDGDSYNYSP
PRKDLLISSK EAIIDSVEAS VSGINQTLTI SFKLNVPYNL EERANGEKTK EMTIKTLISL
RKNEELIRFD VQVINQVLSH RLCVTFATEI ASKFSTADQL FAPINRPVRL PEMDVWEAEE
WQEAPISIEA MQSFVSLHDE SHGVAVMTEG VREYEIIGEN YDTISLTLFR TFSHMGKTDL
LYRPGRASGE SIVETPDAQL LGEINATFAL TLFESSFDEA NIAKKAKEYL SNPPVYQMSD
FLNGRLIYVY RDEEKTLDST YSLGLPVIDG AIISAVKKAE DSDAFITRFF NPYLQKEIAI
PEIFQGKERH LDESNEAETK TTLTHAKVQT YLFEK
//
