ID A0A0B0EIC6_9BACT Unreviewed; 499 AA.
AC A0A0B0EIC6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SCABRO_01420 {ECO:0000313|EMBL:KHE92812.1};
OS Candidatus Scalindua brodae.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Scalinduaceae; Scalindua.
OX NCBI_TaxID=237368 {ECO:0000313|EMBL:KHE92812.1, ECO:0000313|Proteomes:UP000030652};
RN [1] {ECO:0000313|EMBL:KHE92812.1, ECO:0000313|Proteomes:UP000030652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU1 {ECO:0000313|EMBL:KHE92812.1};
RA Speth D.R., Russ L., Kartal B., Op den Camp H.J., Dutilh B.E., Jetten M.S.;
RT "Draft genome of anammox bacterium scalindua brodae, obtained using
RT differential coverage binning of sequence data from two enrichment
RT reactors.";
RL Submitted (OCT-2014) 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:KHE92812.1}.
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DR EMBL; JRYO01000089; KHE92812.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B0EIC6; -.
DR PATRIC; fig|237368.3.peg.1554; -.
DR eggNOG; COG1640; Bacteria.
DR Proteomes; UP000030652; 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:KHE92812.1}.
SQ SEQUENCE 499 AA; 58257 MW; 2683C3BD7B78C99A CRC64;
MDKRGNGLLL HITSLPSSYG IGDIGSEAYK FVNFLAETSQ SFWQILPLNQ TCAAYGNSPY
SSFSAYAGNT LLISPDLMVE DGILLKSDIE DHPSFSRESV DYEAVTKYKK EIFRIAFEKN
KGNLAEHHEF NKFCDENSYW LDDYSLFVSI KNHFNNVEWN NWPEHIRDRR DEDLKEWKER
LRENILRENF LQYLFFKQWY SLKDYCESKG ILIIGDLPIY VNCDSADVWA NPEIFKLNDE
KKPVFVAGVP PDYFSSTGQL WGHPVYDWTV LKETGYIWWI KRIEHNLKFF HMFRLDHFRG
FIDYWEIHAD EKFATNGRWV KAPARDFFNT LANYFDRLPI IAEDLGIITP DVRAVMDQFG
FPGMRVLLFA FGEDLPSNPY APHNYIKNCV AYTGTHDNNT ARGWFNNETS AEDRKRIFDY
IGHEVSEDQI HWELIKLVMS SVADMVIIPM QDVLGLEENS RTNIPASSEG NWGWRLLTEK
LTPLITKKLS EMTRIYGRG
//