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Database: UniProt
Entry: E6VKT8_RHOPX
LinkDB: E6VKT8_RHOPX
Original site: E6VKT8_RHOPX 
ID   E6VKT8_RHOPX            Unreviewed;       652 AA.
AC   E6VKT8;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
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   OrderedLocusNames=Rpdx1_1710 {ECO:0000313|EMBL:ADU43327.1};
OS   Rhodopseudomonas palustris (strain DX-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=652103 {ECO:0000313|EMBL:ADU43327.1, ECO:0000313|Proteomes:UP000001402};
RN   [1] {ECO:0000313|Proteomes:UP000001402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DX-1 {ECO:0000313|Proteomes:UP000001402};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Misra M., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Logan B., Oda Y., Harwood C.,
RA   Woyke T.;
RT   "Complete sequence of Rhodopseudomonas palustris DX-1.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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; CP002418; ADU43327.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6VKT8; -.
DR   STRING; 652103.Rpdx1_1710; -.
DR   KEGG; rpx:Rpdx1_1710; -.
DR   eggNOG; COG1640; Bacteria.
DR   HOGENOM; CLU_022072_1_1_5; -.
DR   OrthoDB; 9763489at2; -.
DR   BioCyc; RPAL652103:RPDX1_RS08390-MONOMER; -.
DR   Proteomes; UP000001402; 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:ADU43327.1};
KW   Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:ADU43327.1}.
SQ   SEQUENCE   652 AA;  72604 MW;  2FABD9C68CADCBC9 CRC64;
     MDLFTRASEL GIQTEFYDGQ GRRHVTPPEA LALITEAMPQ PAERRLLDRI VVIREGEPCR
     SELGAQAVLP VRWRIVTDGG ALVEGVADQR TLSWPQDLPL GIHRVRLSDA SGRTEELPLL
     MAPRRAFGGA FDRSWLIAVQ LYSLRSVRNW GIGDFTDLAN LIELAAALGA GGIGLNPLHA
     LFDDRPGDCS PYSPNSRLFL NPLYVDVERL PEFSAADRPV DAQTLAALRD GELIDYAAVA
     AVKWRGLRAA YEAFRTSASD SRREAFEAFR RERAPLLTRF ACFEVLRHRF GHPWWEWPEE
     WRQPDDARCD LLRQGPDAAE VEFVAFTQWC ADDQLRGCRD LAAARGMSVG LYLDVAVGVQ
     SDGFDAWNEQ TAISRLLSVG APPDSLNTAG QNWGLAGFNA PGLELTGFAP FRDMLRASMR
     YAGAIRLDHV LGLNRLYLVP HGFAAHEGVY VQMPFEALLA VTAQESVGHR CVVIGEDLGT
     VPDGFRDRLA AWGIWSYRVM MFERDFHQGW FFGLEHYLPN ALVTFNTHDL ATYSGWRALT
     DLHLKRSIGV DPGESDDSRH HALAMLGDAL RHQGIEHEDI YAVLTFLART PSRLLAIALE
     DLLGVLDQPN VPGTVSEHPN WRRRLPKPLE DVAAIINRSA LFAATIDRRN PG
//
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