Y2006_MYCTO
ID Y2006_MYCTO Reviewed; 1327 AA.
AC P9WN14; L0T8I0; Q10850;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Uncharacterized glycosyl hydrolase MT2062;
DE EC=3.2.1.-;
GN OrderedLocusNames=MT2062;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
RN [2]
RP INDUCTION BY NITRIC OXIDE (NO) AND BY HYPOXIA, AND DORMANCY REGULON.
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12953092; DOI=10.1084/jem.20030205;
RA Voskuil M.I., Schnappinger D., Visconti K.C., Harrell M.I., Dolganov G.M.,
RA Sherman D.R., Schoolnik G.K.;
RT "Inhibition of respiration by nitric oxide induces a Mycobacterium
RT tuberculosis dormancy program.";
RL J. Exp. Med. 198:705-713(2003).
CC -!- INDUCTION: A member of the dormancy regulon. Induced in response to
CC reduced oxygen tension (hypoxia) and low levels of nitric oxide (NO).
CC {ECO:0000269|PubMed:12953092}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the trehalose
CC phosphatase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the glycosyl
CC hydrolase 65 family. {ECO:0000305}.
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DR EMBL; AE000516; AAK46339.1; -; Genomic_DNA.
DR PIR; D70759; D70759.
DR RefSeq; WP_003410063.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WN14; -.
DR SMR; P9WN14; -.
DR CAZy; GH65; Glycoside Hydrolase Family 65.
DR EnsemblBacteria; AAK46339; AAK46339; MT2062.
DR KEGG; mtc:MT2062; -.
DR PATRIC; fig|83331.31.peg.2220; -.
DR HOGENOM; CLU_006285_1_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProt.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IEA:UniProt.
DR GO; GO:0005992; P:trehalose biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.70.98.40; -; 1.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR005194; Glyco_hydro_65_C.
DR InterPro; IPR005195; Glyco_hydro_65_M.
DR InterPro; IPR005196; Glyco_hydro_65_N.
DR InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR InterPro; IPR003337; Trehalose_PPase.
DR Pfam; PF03633; Glyco_hydro_65C; 1.
DR Pfam; PF03632; Glyco_hydro_65m; 1.
DR Pfam; PF03636; Glyco_hydro_65N; 1.
DR Pfam; PF02358; Trehalose_PPase; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF56784; SSF56784; 2.
DR SUPFAM; SSF74650; SSF74650; 1.
DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
DR TIGRFAMs; TIGR00685; T6PP; 1.
PE 2: Evidence at transcript level;
KW Glycosidase; Hydrolase.
FT CHAIN 1..1327
FT /note="Uncharacterized glycosyl hydrolase MT2062"
FT /id="PRO_0000427206"
FT ACT_SITE 1023
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT BINDING 884..885
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT BINDING 1143..1144
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
SQ SEQUENCE 1327 AA; 145784 MW; 21F3BBC2F4CF9D91 CRC64;
MRCGIVVNVT GPPPTIDRRY HDAVIVGLDN VVDKATRVHA AAWTKFLDDY LTRRPQRTGE
DHCPLTHDDY RRFLAGKPDG VADFLAARGI RLPPGSPTDL TDDTVYGLQN LERQTFLQLL
NTGVPEGKSI ASFARRLQVA GVRVAAHTSH RNYGHTLDAT GLAEVFAVFV DGAVTAELGL
PAEPNPAGLI ETAKRLGANP GRCVVIDSCQ TGLRAGRNGG FALVIAVDAH GDAENLLSSG
ADAVVADLAA VTVGSGDAAI STIPDALQVY SQLKRLLTGR RPAVFLDFDG TLSDIVERPE
AATLVDGAAE ALRALAAQCP VAVISGRDLA DVRNRVKVDG LWLAGSHGFE LVAPDGSHHQ
NAAATAAIDG LAEAAAQLAD ALREIAGAVV EHKRFAVAVH YRNVADDSVD NLIAAVRRLG
HAAGLRVTTG RKVVELRPDI AWDKGKALDW IGERLGPAEV GPDLRLPIYI GDDLTDEDAF
DAVRFTGVGI VVRHNEHGDR RSAATFRLEC PYTVCQFLSQ LACDLQEAVQ HDDPWTLVFH
GYDPGQERLR EALCAVGNGY LGSRGCAPES AESEAHYPGT YVAGVYNQLT DHIEGCTVDN
ESLVNLPNWL SLTFRIDGGA WFNVDTVELL SYRQTFDLRR ATLTRSLRFR DAGGRVTTMT
QERFASMNRP NLVALQTRIE SENWSGTVDF RSLVDGGVHN TLVDRYRQLS SQHLTTAEIE
VLADSVLLRT QTSQSGIAIA VAARSTLWRD GQRVDAQYRV ARDTNRGGHD IQVTLSAGQS
VTLEKVATIF TSRDAATLTA AISAQRCLGE AGRYAELCQQ HVRAWARLWE RCAIDLTGNT
EELRLVRLHL LHLLQTISPH TAELDAGVPA RGLNGEAYRG HVFWDALFVA PVLSLRMPKV
ARSLLDYRYR RLPAARRAAH RAGHLGAMYP WQSGSDGSEV SQQLHLNPRS GRWTPDPSDR
AHHVGLAVAY NAWHYYQVTG DRQYLVDCGA ELLVEIARFW VGLAKLDDSR GRYLIRGVIG
PDEFHSGYPG NEYDGIDNNA YTNVMAVWVI LRAMEALDLL PLTDRRHLIE KLGLTTQERD
QWDDVSRRMF VPFHDGVISQ FEGYSELAEL DWDHYRHRYG NIQRLDRILE AEGDSVNNYQ
ASKQADALML LYLLSSDELI GLLARLGYRF APTQIPGTVD YYLARTSDGS TLSAVVHAWV
LARANRSNAM EYFRQVLRSD IADVQGGTTQ EGIHLAAMAG SIDLLQRCYS GLELRDDRLV
LSPQWPEALG PLEFPFVYRR HQLSLRISGR SATLTAESGD AEPIEVECRG HVQRLRCGHT
IEVGCSR
