ID L7CNG2_RHOBT Unreviewed; 505 AA.
AC L7CNG2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=RBSWK_00850 {ECO:0000313|EMBL:ELP35182.1};
OS Rhodopirellula baltica SWK14.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=993516 {ECO:0000313|EMBL:ELP35182.1, ECO:0000313|Proteomes:UP000010959};
RN [1] {ECO:0000313|EMBL:ELP35182.1, ECO:0000313|Proteomes:UP000010959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SWK14 {ECO:0000313|EMBL:ELP35182.1,
RC ECO:0000313|Proteomes:UP000010959};
RX PubMed=23273849;
RA Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C., Richter M.,
RA Achstetter T., Glockner F.O., Harder J.;
RT "Expression of sulfatases in Rhodopirellula baltica and the diversity of
RT sulfatases in the genus Rhodopirellula.";
RL Mar. Genomics 0:0-0(2012).
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:ELP35182.1}.
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DR EMBL; AMWG01000020; ELP35182.1; -; Genomic_DNA.
DR RefSeq; WP_007336156.1; NZ_AMWG01000020.1.
DR AlphaFoldDB; L7CNG2; -.
DR PATRIC; fig|993516.3.peg.902; -.
DR Proteomes; UP000010959; 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 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 Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:ELP35182.1}.
SQ SEQUENCE 505 AA; 57209 MW; E4F773633C139666 CRC64;
MRFPRSSGIL CHITSLPSEL GIGDLGSAAY EMVDFLHAAG QSIWQILPLS PPAYGNSPYS
AYSAFGGNAL LISLEALVDE GLLEASDLDG FTQTDPARVD FGTVSEFKHA RLKLAYERYL
TKPPRELKIA FELFLDANDW WLDEFSLFEV FLNKFEQSNW SKWPDPISHR EPDALGQARQ
EMSREIDYSR FQQFLFDRQW NRLKAYANER QVQLCGDMPI FVAYESADVW GNQDMFALND
DGTPKLVAGV PPDYFSETGQ LWGNPQYDWD ALEKADYAWW TARFRRSLEQ FDLLRVDHFR
GFEAYWEVPY GAETAIGGQW RTGPGAKPFR AAEKELGELP FIAEDLGMIT DAVHELREEL
GFPGMRVLQF GFATMEDDFH RPSTYPESCV AYTGTHDNDT VMGWYHLRTP PEEGDDPLDE
VVTSEHEVHW QLIDAVMSSA AEIAIVPIQD VLGLGNEARM NLPGIADGNW AWRLSPQALT
QEHADRLASL CQQRGRLTHE VPSVG
//
