ID A0A0R1JZ24_9LACO Unreviewed; 1022 AA.
AC A0A0R1JZ24;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Glycoside hydrolase family 38 central domain-containing protein {ECO:0000259|SMART:SM00872};
GN ORFNames=FD02_GL001827 {ECO:0000313|EMBL:KRK73993.1};
OS Lacticaseibacillus nasuensis JCM 17158.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1291734 {ECO:0000313|EMBL:KRK73993.1, ECO:0000313|Proteomes:UP000051804};
RN [1] {ECO:0000313|EMBL:KRK73993.1, ECO:0000313|Proteomes:UP000051804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 17158 {ECO:0000313|EMBL:KRK73993.1,
RC ECO:0000313|Proteomes:UP000051804};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRK73993.1}.
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DR EMBL; AZDJ01000003; KRK73993.1; -; Genomic_DNA.
DR RefSeq; WP_056950214.1; NZ_AZDJ01000003.1.
DR AlphaFoldDB; A0A0R1JZ24; -.
DR STRING; 1291734.FD02_GL001827; -.
DR PATRIC; fig|1291734.4.peg.1876; -.
DR OrthoDB; 9772207at2; -.
DR Proteomes; UP000051804; 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:UP000051804}.
FT DOMAIN 503..578
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1022 AA; 114160 MW; 5B90A830AE3A097A CRC64;
MNEASFKRIS RIAEVLQEHI VTKSYPFTSA TLSDADGERT YHAGDYFGGE NANYDMTMTV
SVPDFDPANQ YVLTVGTRGY NDDNTRNPQI KLFIGTELVQ AFDVNHHDCP LDAAWFVDGV
LTFRLQIYAG RDDKKFPLDA VVNLIDPQTR TTYFDFMTYL GCWKNVTAEQ NLDNRYRAAL
EEAANHLDLR DIGSEAYQAS LTAASQILHD QLDEAPDPKN GTIYAIGHTH IDMAWLWPIE
QTVEKANRSF ATVLNLMKQY PEFQFMHSSP QLYKWIKEKY PSQYAEIKAA VMAGRWHPEG
AMWIEPDTNL PSGESLVRQL MYGKRFFKRE FDIDSKVLWL PDVFGYSASL PQLMKKAGVD
YFMTTKLAWN DTNIFPDTSF YWQGIDGTQV VAHIINTISE FWSLNEWYST YSGLVTPNVL
KKTWDKYRQK DVSDSVLVAY GWGDGGGGPT PEMMEYLNRF QHGIAGMPRV RQAGVREYFD
HLAGTMAANR DAVPVWMGEL YFEFHRGTYT SQAHSKHANR ALETQLQSTE KLLATTPSAG
AHREVLGPIW ERALLNQFHD VLPGSSIPQV YQQTDQDYAT AFSQLHDLQA EYAKGQLTPA
PGATTVYNPW GQTRSVAVEL PLTPEQGATV NGQPVATQQL SATTALVQVP QVAPFAFATI
TPVKQAAVAV PAAKPLGQTY ETAELKVKFD AAYNITSLYD KQAQREVVPA GGLLNQLVVY
QDLPTEYDAW NVDSTYHAKS WPVATVVSAT IEGQGALRDT LHIVRRFEHS TIDTRLHFIH
GTTKIQIDCD LDWHDDHTFL RCENAVAVNA TEASYDIQFG NLTRPVNKNT SWEQAKFEVP
AQKWADLSDN GYGLSILTDA KYGYDAGYQH LGVSLHRCPT FPDPQADTGH DRFTYTLFPH
AGGWREAGTM QAALALNTPA VVWSDVAAPA QRTEAWVSVA QPNIIIDTIK PAEDDAAIIL
RAYEYANAQT TATITFQQAL ASADLCNLLE QPESALTISP DGHTVTVPFG GFAVQTIRVT
LK
//
