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Database: UniProt
Entry: R5V8F5_9BACT
LinkDB: R5V8F5_9BACT
Original site: R5V8F5_9BACT 
ID   R5V8F5_9BACT            Unreviewed;       409 AA.
AC   R5V8F5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=4-alpha-glucanotransferase {ECO:0000256|ARBA:ARBA00020295};
DE            EC=2.4.1.25 {ECO:0000256|ARBA:ARBA00012560};
DE   AltName: Full=Amylomaltase {ECO:0000256|ARBA:ARBA00031423};
DE   AltName: Full=Disproportionating enzyme {ECO:0000256|ARBA:ARBA00031501};
GN   ORFNames=BN754_00229 {ECO:0000313|EMBL:CCZ76962.1};
OS   Alistipes finegoldii CAG:68.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Alistipes.
OX   NCBI_TaxID=1263035 {ECO:0000313|EMBL:CCZ76962.1, ECO:0000313|Proteomes:UP000018154};
RN   [1] {ECO:0000313|EMBL:CCZ76962.1, ECO:0000313|Proteomes:UP000018154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:68 {ECO:0000313|Proteomes:UP000018154};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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   -!- SIMILARITY: Belongs to the disproportionating enzyme family.
CC       {ECO:0000256|ARBA:ARBA00005684}.
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:CCZ76962.1}.
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DR   EMBL; CBAO010000227; CCZ76962.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5V8F5; -.
DR   Proteomes; UP000018154; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   InterPro; IPR003385; Glyco_hydro_77.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR32518; -; 1.
DR   PANTHER; PTHR32518:SF3; 4-ALPHA-GLUCANOTRANSFERASE; 1.
DR   Pfam; PF02446; Glyco_hydro_77; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Transferase {ECO:0000313|EMBL:CCZ76962.1}.
SQ   SEQUENCE   409 AA;  47694 MW;  43C0576777C601F7 CRC64;
     MDSQAGAPPD AFSASGQNWG FPTYDWEHMA QDGYAWWQAR MAKMAEYFDA FRIDHILGFF
     RIWEIPVHAV HGLLGYFNPA LPYSADELRG MGFDTAGGRF TVPAPDDRML GELFGELADE
     VRTTCMKEGR LLPAYATQRK VAERFPGDDP RRSRLREGLM TLLDDVLFIE DPRRKGFFHP
     RIAAQSTYMY RTLDPQRRDT FDRLHDDFFY RRHNRFWQES ALRKLPVLLS ATRMLACGED
     LGMIPDSVPE TMRALQILSL EIQRMPKSLG EVFADPARYP YFSVCTTSTH DMNPLRAWWE
     ENRELSERFY REVLGMEGDA PRTCEPWICR RIVDMHLRSP AMLAILPLQD WLATDAALRS
     PHADRERINI PAAPRYYWRY RMHLTLEELL RQEPFNATLR EMIIAGGRR
//
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