TREA_XANAC
ID TREA_XANAC Reviewed; 568 AA.
AC Q8PPT1;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Periplasmic trehalase {ECO:0000255|HAMAP-Rule:MF_01060};
DE EC=3.2.1.28 {ECO:0000255|HAMAP-Rule:MF_01060};
DE AltName: Full=Alpha,alpha-trehalase {ECO:0000255|HAMAP-Rule:MF_01060};
DE AltName: Full=Alpha,alpha-trehalose glucohydrolase {ECO:0000255|HAMAP-Rule:MF_01060};
DE Flags: Precursor;
GN Name=treA {ECO:0000255|HAMAP-Rule:MF_01060}; OrderedLocusNames=XAC0604;
OS Xanthomonas axonopodis pv. citri (strain 306).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190486;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=306;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
CC -!- FUNCTION: Provides the cells with the ability to utilize trehalose at
CC high osmolarity by splitting it into glucose molecules that can
CC subsequently be taken up by the phosphotransferase-mediated uptake
CC system. {ECO:0000255|HAMAP-Rule:MF_01060}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-
CC glucose; Xref=Rhea:RHEA:32675, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903,
CC ChEBI:CHEBI:16551, ChEBI:CHEBI:17925; EC=3.2.1.28;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01060};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01060}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family.
CC {ECO:0000255|HAMAP-Rule:MF_01060}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE008923; AAM35493.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8PPT1; -.
DR SMR; Q8PPT1; -.
DR STRING; 190486.XAC0604; -.
DR CAZy; GH37; Glycoside Hydrolase Family 37.
DR EnsemblBacteria; AAM35493; AAM35493; XAC0604.
DR KEGG; xac:XAC0604; -.
DR eggNOG; COG1626; Bacteria.
DR HOGENOM; CLU_006451_3_1_6; -.
DR OMA; TNGVLIW; -.
DR PHI-base; PHI:6630; -.
DR Proteomes; UP000000576; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071474; P:cellular hyperosmotic response; IEA:InterPro.
DR GO; GO:0005993; P:trehalose catabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.10; -; 1.
DR HAMAP; MF_01060; Peripl_trehalase; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR001661; Glyco_hydro_37.
DR InterPro; IPR018232; Glyco_hydro_37_CS.
DR InterPro; IPR023720; Trehalase_periplasmic.
DR PANTHER; PTHR23403; PTHR23403; 1.
DR Pfam; PF01204; Trehalase; 1.
DR PRINTS; PR00744; GLHYDRLASE37.
DR SUPFAM; SSF48208; SSF48208; 1.
DR PROSITE; PS00927; TREHALASE_1; 1.
DR PROSITE; PS00928; TREHALASE_2; 1.
PE 3: Inferred from homology;
KW Glycosidase; Hydrolase; Periplasm; Signal.
FT SIGNAL 1..39
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT CHAIN 40..568
FT /note="Periplasmic trehalase"
FT /id="PRO_0000012049"
FT ACT_SITE 329
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT ACT_SITE 511
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT BINDING 176..177
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT BINDING 222..224
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT BINDING 294..296
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT BINDING 526
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
SQ SEQUENCE 568 AA; 63261 MW; ADF8A2C3D4DD5196 CRC64;
MPYATARSGD VMSSAAPPCC TSLLGLSLSM FVAPGTLTAA PLDAPVVNAP APTPPTPDLA
YPELFQAVQR GELFDDQKHF VDFLPLRDPA LINADYLAQH DHPGFDLRKF VDANFEESPP
VQTDAIRQDT ALREHIDLLW PKLVRSQNHV PPHSSLLALP HPYVVPGGRF REVYYWDSYF
TMLGLVKSGE TTLSRQMLDN FAYLIDTYGH IPNGNRTYYL SRSQPPFFSY MVELQAGVEG
EAVYQRYLPQ LQKEYAYWMQ GSDDLQPGQA ARHVVRLADG SVLNRYWDER DTPRPEAWLH
DTRTAAEVTD RPAAEVYRDL RAGAESGWDY TSRWLADGQN LRTIRTTAIL PIDLNSLLYH
LERTLALACA QPGAECTRDY AALAQQRKQA IDAHLWNTAG YYADYDWQTR TLSNQVTAAA
LYPLFAGLAS DDHAKRTAST VRKTLLRPGG LATTAVKTGQ QWDEPNGWAP LQWVAVDGLR
RYGEDALART IGERFLAQVQ ALFAREHKLV EKYGLETDAA GGGGGEYALQ DGFGWTNGVT
LMLLNLYPGK DTKAAPAKRV RKPEAAAR
