ID T1ZF02_STRIT Unreviewed; 877 AA.
AC T1ZF02;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 05-FEB-2025, entry version 48.
DE SubName: Full=Putative hydrolase protein {ECO:0000313|EMBL:AGU76430.1};
DE EC=3.2.1.- {ECO:0000313|EMBL:AGU76430.1};
GN ORFNames=SIR_1069 {ECO:0000313|EMBL:AGU76430.1};
OS Streptococcus intermedius B196.
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus; Streptococcus anginosus group.
OX NCBI_TaxID=862967 {ECO:0000313|EMBL:AGU76430.1, ECO:0000313|Proteomes:UP000016233};
RN [1] {ECO:0000313|EMBL:AGU76430.1, ECO:0000313|Proteomes:UP000016233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B196 {ECO:0000313|EMBL:AGU76430.1,
RC ECO:0000313|Proteomes:UP000016233};
RX PubMed=24341328; DOI=10.1186/1471-2164-14-895;
RA Olson A.B., Kent H., Sibley C.D., Grinwis M.E., Mabon P., Ouellette C.,
RA Tyson S., Graham M., Tyler S.D., Van Domselaar G., Surette M.G.,
RA Corbett C.R.;
RT "Phylogenetic relationship and virulence inference of Streptococcus
RT Anginosus Group: curated annotation and whole-genome comparative analysis
RT support distinct species designation.";
RL BMC Genomics 14:895-895(2013).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792}.
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DR EMBL; CP003857; AGU76430.1; -; Genomic_DNA.
DR RefSeq; WP_021002909.1; NC_022246.1.
DR AlphaFoldDB; T1ZF02; -.
DR KEGG; sib:SIR_1069; -.
DR PATRIC; fig|862967.3.peg.1077; -.
DR eggNOG; COG0383; Bacteria.
DR HOGENOM; CLU_003442_2_1_9; -.
DR OrthoDB; 9764050at2; -.
DR Proteomes; UP000016233; 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 GO; GO:0009313; P:oligosaccharide catabolic process; IEA:TreeGrafter.
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 Gene3D; 2.70.98.30; Golgi alpha-mannosidase II, domain 4; 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, ECO:0000313|EMBL:AGU76430.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AGU76430.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000016233}.
FT DOMAIN 297..367
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 877 AA; 100159 MW; 50EC90F2EBD3D03E CRC64;
MENITVHIIS HSHWDREWYL PFESHRMQLV ELFDNLFYLF ENDPDFKSFH LDGQTIVLDD
YLEICPENQN KVQRYIDEGK LKIGPFYILQ DDYLISSEAN VRNTLIGQQE CKKWGKSTQI
GYFPDTFGNM GQAPQLLQQS GIHVAAFGRG VKPIGFDNQV LEDEQFTSQY SEMYWQGADG
SKILGILFAN WYSNGNEIPA NPEEAKVFWE KKLADVKSYA STNQWLMMNG CDHQPVQRNL
SEAIRVANEL YPHINFVHSS FDDYVKAVEA ALPEELSIVQ GELTSQETDG WYTLANTSSA
RIYLKQAFQE NSNLLEQVVE PLTVITGGHN HKDQLTYAWK TLLQNAPHDS ICGCSVDEVH
REMETRFAKV NQVGEFIKGN LLEEWKQKLD SRQAESDLLF TVVNTGLHDK VDTVSVDVTF
ATCDFKEAHP TEAYQRMANL TIPDFIVKDL DGRSIEAKIE DLGANFQYDL PKDRFRQAYI
ARQLRVTLPI HLAPLTWKTF QLLPGAKEEH EGLYRNGVID TPFVTVSFDK YLTVYDKTTH
EAYENFLRFE DRGDIGNEYI YFQPKNTEPI YAKLADVKVL ENNARYAKVE LSHELTLPVS
ADELLEQEQK GIVEFMTRSA GRSSELTSMI LTTELTVFAD SPQLRFKTRF TNTAKDHRIR
VLFRTHNSSK TNDSDSIYEV VRRNNRPASS WENPENPQHQ QAFVSLYDDQ KAVTVANKGL
NEYEILGDDT IAVTILRATG ELGDWGYFPT PEAQCLRDFQ VEYTAECHQP QERFAAYRRA
KAFQTPLTAF QISKQEGSVA AAGQALEHPA LNLAEICPTA LKVAEDESGI VLRYYNMSQE
EQEVISDSKT LVNLLEEVVS EKLGALGPQE IRTELLK
//
