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Database: UniProt
Entry: A0A164B654_9SYNE
LinkDB: A0A164B654_9SYNE
Original site: A0A164B654_9SYNE 
ID   A0A164B654_9SYNE        Unreviewed;       504 AA.
AC   A0A164B654;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
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   Name=malQ {ECO:0000313|EMBL:KZR88241.1};
GN   ORFNames=MITS9508_02385 {ECO:0000313|EMBL:KZR88241.1};
OS   Synechococcus sp. MIT S9508.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1801629 {ECO:0000313|EMBL:KZR88241.1, ECO:0000313|Proteomes:UP000076799};
RN   [1] {ECO:0000313|EMBL:KZR88241.1, ECO:0000313|Proteomes:UP000076799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT S9508 {ECO:0000313|EMBL:KZR88241.1,
RC   ECO:0000313|Proteomes:UP000076799};
RA   Cubillos-Ruiz A., Berta-Thompson J.W., Becker J.W., Chisholm S.W.;
RT   "Evolutionary Radiation of Lanthipeptides in Marine Picocyanobacteria.";
RL   Submitted (FEB-2016) 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:KZR88241.1}.
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DR   EMBL; LVHU01000012; KZR88241.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A164B654; -.
DR   STRING; 1801629.MITS9508_02385; -.
DR   PATRIC; fig|1801629.3.peg.2554; -.
DR   Proteomes; UP000076799; 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|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU361207};
KW   Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:KZR88241.1}.
SQ   SEQUENCE   504 AA;  57298 MW;  BAEFC2CB1778E606 CRC64;
     MTSISLPRRR VGVLLHPTAL PGSPVCGGLG APARDWLKAL AQQGIGVWQI LPLSPPDGTG
     SPYSSPSSFA INPWLLDAKD LSDQGFLQPG DLEALPGVEA AEALLDFPLA DRRAAALARQ
     LRHCWDQLPH SNHADFDRWR RDQSRWLQDH AAFMVLREQN EGRPWWEWPQ QLAVHDQTAL
     WEWRDAHEDR LLEQELLQWH LSRQWTRLRE LARELDVEIL GDLPFYVARD SSDVWSHRSL
     FSIAADGRLR EQSGVPPDYF SETGQLWGTP VYSWPRHRCT GFRWWRDRLR RQWQLADRLR
     LDHFRALASY WSVPGGDSTA MNGAWRRSPG RELLSCLRRD AGGRLPLVAE DLGVITTDVE
     QLRDRFHLPG MKVLQFAFDG NPQNPYLPSN IHGTGWVVYP GTHDNPTSLG WWQRLDGDSR
     ARFASCLECP IEAPGWQLLE LGLATSAQLV IASLQDLLHL DDVARFNTPG TVGGNWNWRL
     AAFDDSVEGA LQGYGLRADV WSRR
//
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