ID A0A140L4G3_9CLOT Unreviewed; 782 AA.
AC A0A140L4G3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Alpha,alpha-trehalose phosphorylase {ECO:0000313|EMBL:KXG75438.1};
DE EC=2.4.1.64 {ECO:0000313|EMBL:KXG75438.1};
GN Name=treP {ECO:0000313|EMBL:KXG75438.1};
GN ORFNames=AN619_17020 {ECO:0000313|EMBL:KXG75438.1};
OS Thermotalea metallivorans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Thermotalea.
OX NCBI_TaxID=520762 {ECO:0000313|EMBL:KXG75438.1, ECO:0000313|Proteomes:UP000070456};
RN [1] {ECO:0000313|EMBL:KXG75438.1, ECO:0000313|Proteomes:UP000070456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B2-1 {ECO:0000313|EMBL:KXG75438.1,
RC ECO:0000313|Proteomes:UP000070456};
RA Patel B.K.;
RT "Draft genome sequence of the thermoanaerobe Thermotalea metallivorans, an
RT isolate from the runoff channel of the Great Artesian Basin, Australia.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family.
CC {ECO:0000256|ARBA:ARBA00006768}.
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:KXG75438.1}.
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DR EMBL; LOEE01000034; KXG75438.1; -; Genomic_DNA.
DR RefSeq; WP_068556295.1; NZ_LOEE01000034.1.
DR AlphaFoldDB; A0A140L4G3; -.
DR STRING; 520762.AN619_17020; -.
DR PATRIC; fig|520762.4.peg.1889; -.
DR OrthoDB; 9758855at2; -.
DR Proteomes; UP000070456; Unassembled WGS sequence.
DR GO; GO:0047656; F:alpha,alpha-trehalose phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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 Glycosyltransferase {ECO:0000313|EMBL:KXG75438.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070456};
KW Transferase {ECO:0000313|EMBL:KXG75438.1}.
FT DOMAIN 21..282
FT /note="Glycoside hydrolase family 65 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03636"
FT DOMAIN 338..702
FT /note="Glycoside hydrolase family 65 central catalytic"
FT /evidence="ECO:0000259|Pfam:PF03632"
FT DOMAIN 711..771
FT /note="Glycoside hydrolase family 65 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03633"
FT ACT_SITE 502
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-50"
FT BINDING 372..373
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
FT BINDING 614..615
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
SQ SEQUENCE 782 AA; 91512 MW; 91754C46604B5B51 CRC64;
MKFHAERNTP IYAVREWEVV EEFFDIVNNY RSETIFSVGN GYIGMRGNFE EGYSGPPGTS
AEGTYINGFY ESWPISYGEI AYGYPEQGQT MMNVVNGKRI KLILEDEPLD MCRGEILSHR
RSLHLKEGIF KRFLIWRSPK GREVKVEVER LVSLTNKHLA AIDYRVTPLN FEGEIKIISL
LDSGYAEAFP REKDPRIGGE WKRYGLPVEE KKVEKDFAFL LQRTKNSGFS LVCAMENDLK
TDCSYTTEEI HGVLEVGMAY VIRGKAGREI RLNKYIAYGT SRDYEQEKLA TTAENIVRKG
KEEGFERLKQ GQQRYLEKFW ERADIEIKGD PLLQQGIRFN IFHLLQSVGK DGKTNIAAKG
LTGEGYEGHY FWDTEMYVIP FFLYCEPKIS RKLLEYRYNT LDKARERARE MSHQKGALFP
WRTINGEECS AYYPAGTAQY HINADIAFAI KRYMEATKDE DFLIEQGAEI LFETARIWAD
LGAFLEEKGN KFCINGVTGP DEYTAIVNNN CYTNLMAREN LYYAYHTAVE MQEKYKDAFE
TIAGKIDLTE EEILFWKQAA DHMYIPYHEK RKIHPQDDSF LEKKVWDFEN TPKEKYPLLL
YYHPLVIYRH QVCKQADLIL AQFLLSHKFS HDQKKRDYDY YEKITTHDSS LSTCIFSIMA
CDIGYYEKAY AYFLETARMD LDDYKGNTKH GIHTANMAGS WMCIVNGFAG MRVHDDVIRF
HPYIHPSWEA YSFKIAYRGR RVKVTISRKE TIYELLEGEE LWIWHKENRF LLRDRAVFYE
CL
//
