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Database: UniProt
Entry: A0A1H0VQ13_9PSEU
LinkDB: A0A1H0VQ13_9PSEU
Original site: A0A1H0VQ13_9PSEU 
ID   A0A1H0VQ13_9PSEU        Unreviewed;       778 AA.
AC   A0A1H0VQ13;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Alpha,alpha-trehalose phosphorylase {ECO:0000313|EMBL:SDP80453.1};
GN   ORFNames=SAMN05192558_11517 {ECO:0000313|EMBL:SDP80453.1};
OS   Actinokineospora alba.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinokineospora.
OX   NCBI_TaxID=504798 {ECO:0000313|EMBL:SDP80453.1, ECO:0000313|Proteomes:UP000199651};
RN   [1] {ECO:0000313|Proteomes:UP000199651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBRC-M 10655 {ECO:0000313|Proteomes:UP000199651};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family.
CC       {ECO:0000256|ARBA:ARBA00006768}.
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DR   EMBL; FNJB01000015; SDP80453.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0VQ13; -.
DR   STRING; 504798.SAMN05421871_104368; -.
DR   OrthoDB; 9816160at2; -.
DR   Proteomes; UP000199651; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.70.98.40; Glycoside hydrolase, family 65, N-terminal domain; 1.
DR   Gene3D; 2.60.420.10; Maltose phosphorylase, domain 3; 1.
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; IPR017045; Malt_Pase/Glycosyl_Hdrlase.
DR   PANTHER; PTHR11051; GLYCOSYL HYDROLASE-RELATED; 1.
DR   PANTHER; PTHR11051:SF13; GLYCOSYL TRANSFERASE-RELATED; 1.
DR   Pfam; PF03633; Glyco_hydro_65C; 1.
DR   Pfam; PF03632; Glyco_hydro_65m; 1.
DR   Pfam; PF03636; Glyco_hydro_65N; 1.
DR   PIRSF; PIRSF036289; Glycosyl_hydrolase_malt_phosph; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199651}.
FT   DOMAIN          15..266
FT                   /note="Glycoside hydrolase family 65 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03636"
FT   DOMAIN          323..675
FT                   /note="Glycoside hydrolase family 65 central catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03632"
FT   DOMAIN          685..745
FT                   /note="Glycoside hydrolase family 65 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03633"
FT   REGION          750..778
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        754..768
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        484
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036289-50"
FT   BINDING         357..358
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
FT   BINDING         588..589
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
SQ   SEQUENCE   778 AA;  85500 MW;  A281A936E6527F3A CRC64;
     MNGYEVSPWE LRWRGLAIDQ LHRTESTFAL ANGHIGMRGA LEEGEPVGLP GTYLNGFYES
     HALPYAEIGY GYPEDGQTIV NVTDGKIIRL LVEDEPLDLR YGRTLAHQRW IDFRSGILSR
     DTVWESPTGR RVRIRSRRMV SFTQRAVAAI HYEIEPADDL QLVVQSDLLA NEPIESRGKD
     PRVAAALRSP LVADFAAAEG YNAVLVHHTR ESGLRVAAGM DHEIDTSDGM QTDIRAEGDL
     ARLTAAVDVP AGGKLRLVKY LGYGWSAKRS VPALRAQVEA ALAGARQTGW EGLLREQRAF
     LDDFWTAADI EIDGDERLQQ AVRFALFHIL QAGARGESRA IAGKGLTGPG YDGHAFWDTE
     TFVLPVLTYT MPDAARDALR WRHSTLPQAR ERAKVLGKRG AAFPWRSITG AECSAYWPAG
     TAAFHVSAAV ADAAARYTAA CADDTFDREY GTELLVETAR LWVSLGHHDQ HGGFRIDGVT
     GPDEYTAVVD NNVYTNLMAQ RNLTEAGTAC GRNPEVADRL GVSPDEVEAW RRAAEEMVIP
     FDDLLGVHPQ SEGFTQHEEW DFAATPKDKY PLLLHYPYFD LYRKQVVKQA DLVLAMHLRG
     DAFTPEQKAA NFAYYEARTV RDSSLSAGTQ AVLAAEVGHL GLAYDYIVEA AMTDLADLHD
     NVRNGLHMAS LAGAWAGVVA GLGGFRDHGG VPTFAPRLPK ELDRVSFRMC VHRSRIQVEI
     NRDAARYRHI SGGALSTSHH GEPIVIEAGP GLSLPIPDCP PQPRPKQPAG REPGSRRA
//
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