ID R6Q3M1_9BIFI Unreviewed; 720 AA.
AC R6Q3M1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
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 ORFNames=BN571_00523 {ECO:0000313|EMBL:CDC16507.1};
OS Bifidobacterium pseudocatenulatum CAG:263.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1263060 {ECO:0000313|EMBL:CDC16507.1, ECO:0000313|Proteomes:UP000018036};
RN [1] {ECO:0000313|EMBL:CDC16507.1, ECO:0000313|Proteomes:UP000018036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:263 {ECO:0000313|Proteomes:UP000018036};
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 ECO:0000256|RuleBase:RU361207};
CC -!- SIMILARITY: Belongs to the disproportionating enzyme family.
CC {ECO:0000256|ARBA:ARBA00005684, ECO:0000256|RuleBase:RU361207}.
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:CDC16507.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CBEV010000150; CDC16507.1; -; Genomic_DNA.
DR AlphaFoldDB; R6Q3M1; -.
DR Proteomes; UP000018036; Unassembled WGS sequence.
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 InterPro; IPR048458; MalQ_N.
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 Pfam; PF21226; MalQ_N; 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 Transferase {ECO:0000256|RuleBase:RU361207}.
FT DOMAIN 79..161
FT /note="MalQ N-terminal beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF21226"
SQ SEQUENCE 720 AA; 79636 MW; 33C6C31783FCE6C2 CRC64;
MTATQQTESA ERIARPLIQL AKLNGISTSY IDQLGTYVEI RDEVLVSVLA ALGVDASSDE
AIAASYELTK QRIADTLVEP TIVKFIGKEA TTPIRAKGHD VTLRLLLEDG TRYEGNLCMY
LAPQTDGSLT LTLPDDIPAG YHTLRVNAGP LHGEARLICA PARVPLPPAV AEKQRWGWMA
QMYSIRSAES WGVGDYGDLK LLLTDAAEKS HADFMLINPI HATAPVEPLE PSPYLPESRR
FMNVTYIRPQ DIEEYAGLDE AALAEVERLH AEVAPANDNA DELDINSAWW HKRQALRLVF
KVPRSAERQA AFEAFKEAAG PDLRAFAAWS VAFQMWGAPW EGTWFAETNR DSPEVAELMR
DHADMVEFEC WLQWIADEQV TAAQNAARES GMALGLMQDM AVGVHSLGAD VWWNPERFAV
GSVTVGCPPD FYNQQGQDWG QPPFNPNYLA KTGYGVYREM VHNMFSHAGA VRIDHVLGLF
RLWWIPQGEG ARGGAYVTYD YEAMIAILTI EASRVNGLVV GEDLGTVPDY VRTVLAEHGL
LGCTVEWFAR VDDSPNAGDP YADPADYREY ALASVTTHDL PPTAGYLQFE HVKLREELNL
LTGPVEEFQA SATAERQAML DRLVESELIT PEIAADVDDH IQEIVEAMHK MLLRSPSVLL
QAALVDGVGE TRSQNQPGTS SEYCNWRVPL AGPDHKVVHT DEVFDLPRVK SLSAIMNGEK
//
