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Database: UniProt
Entry: Q73JN0_TREDE
LinkDB: Q73JN0_TREDE
Original site: Q73JN0_TREDE 
ID   Q73JN0_TREDE            Unreviewed;       540 AA.
AC   Q73JN0;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=4-alpha-glucanotransferase {ECO:0000256|ARBA:ARBA00020295, ECO:0000256|RuleBase:RU361207};
DE            EC=2.4.1.25 {ECO:0000256|ARBA:ARBA00012560, ECO:0000256|RuleBase:RU361207};
DE   AltName: Full=Amylomaltase {ECO:0000256|ARBA:ARBA00031423, ECO:0000256|RuleBase:RU361207};
DE   AltName: Full=Disproportionating enzyme {ECO:0000256|ARBA:ARBA00031501, ECO:0000256|RuleBase:RU361207};
GN   Name=malQ {ECO:0000313|EMBL:AAS12905.1};
GN   OrderedLocusNames=TDE_2387 {ECO:0000313|EMBL:AAS12905.1};
OS   Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS   / KCTC 15104).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC   Treponema.
OX   NCBI_TaxID=243275 {ECO:0000313|EMBL:AAS12905.1, ECO:0000313|Proteomes:UP000008212};
RN   [1] {ECO:0000313|EMBL:AAS12905.1, ECO:0000313|Proteomes:UP000008212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104
RC   {ECO:0000313|Proteomes:UP000008212};
RX   PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA   Seshadri R., Myers G.S., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA   Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA   Ren Q., Brinkac L.M., Madupu R., Kolonay J., Durkin S.A., Daugherty S.C.,
RA   Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G., Malek J.,
RA   Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K., Pal S.,
RA   Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E., Baca E.,
RA   Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT   "Comparison of the genome of the oral pathogen Treponema denticola with
RT   other spirochete genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Transfers a segment of a (1->4)-alpha-D-glucan to a new
CC         position in an acceptor, which may be glucose or a (1->4)-alpha-D-
CC         glucan.; EC=2.4.1.25; Evidence={ECO:0000256|ARBA:ARBA00000439,
CC         ECO:0000256|RuleBase:RU361207};
CC   -!- SIMILARITY: Belongs to the disproportionating enzyme family.
CC       {ECO:0000256|ARBA:ARBA00005684, ECO:0000256|RuleBase:RU361207}.
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DR   EMBL; AE017226; AAS12905.1; -; Genomic_DNA.
DR   RefSeq; NP_972986.1; NC_002967.9.
DR   RefSeq; WP_002680318.1; NC_002967.9.
DR   AlphaFoldDB; Q73JN0; -.
DR   STRING; 243275.TDE_2387; -.
DR   CAZy; GH77; Glycoside Hydrolase Family 77.
DR   PaxDb; 243275-TDE_2387; -.
DR   GeneID; 2740689; -.
DR   KEGG; tde:TDE_2387; -.
DR   PATRIC; fig|243275.7.peg.2255; -.
DR   eggNOG; COG1640; Bacteria.
DR   HOGENOM; CLU_014132_1_0_12; -.
DR   OrthoDB; 9811841at2; -.
DR   Proteomes; UP000008212; Chromosome.
DR   GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102500; F:beta-maltose 4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR003385; Glyco_hydro_77.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   NCBIfam; TIGR00217; malQ; 1.
DR   PANTHER; PTHR32438; 4-ALPHA-GLUCANOTRANSFERASE DPE1, CHLOROPLASTIC/AMYLOPLASTIC; 1.
DR   PANTHER; PTHR32438:SF5; 4-ALPHA-GLUCANOTRANSFERASE DPE1, CHLOROPLASTIC_AMYLOPLASTIC; 1.
DR   Pfam; PF02446; Glyco_hydro_77; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361207};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU361207,
KW   ECO:0000313|EMBL:AAS12905.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008212};
KW   Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:AAS12905.1}.
SQ   SEQUENCE   540 AA;  62847 MW;  CEBB41BC644575A1 CRC64;
     MKRSSGIILH PTSLPNDEGI GTIGKEAFAF IDWLKKTRTG VWQMLPIGPT GYGDSPYASF
     SAFAGNPYLI SLQDLYEKGF LEKRDFTEYK KIVQENTDPK RADFGLIHYH KTKMLKKAAA
     SLLHKMERDS SSKEELENFY QEESFWLDGY AAFMTIKEDY EERLDKENLV QGIWNEVWPK
     ELALNKKDKI KEFLGKHSEE YETQKIIQFF FFSQWKKLKE YAEKNGIQLI GDIPIFAAMD
     SADVWQNQSL FLLDKEATPK AVAGVPPDFF SPTGQLWGNP LYDWAKMKKD SYLWWKARIR
     HTLKLFDIIR LDHFRGFEAF WAIPQGAKTA QEGKWVKGPD HHFFEEIQKD LISLDEKYRG
     ELPILTEDLG VITPEVARLR DDFNFPTMKI LQFAFDLNEL KSENLTNPYL PHNHKKNCAV
     YTGSHDNDTI MGWLEGSSDE MLKFIYTYLY GKKADKRICS ILNTYEFKKE LASEIIRKAF
     SSVADFAAVQ MQDLLFLNSE ARMNAPSTVG KNWQWRVTGS YENCEMTEKL ELWNVLYNRV
//
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