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Database: UniProt
Entry: A0KP86_AERHH
LinkDB: A0KP86_AERHH
Original site: A0KP86_AERHH 
ID   A0KP86_AERHH            Unreviewed;       758 AA.
AC   A0KP86;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 83.
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:ABK39407.1};
GN   OrderedLocusNames=AHA_3617 {ECO:0000313|EMBL:ABK39407.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS   13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK39407.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK39407.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 /
RC   KCTC 2358 / NCIMB 9240 / NCTC 8049
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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}.
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DR   EMBL; CP000462; ABK39407.1; -; Genomic_DNA.
DR   RefSeq; YP_858087.1; NC_008570.1.
DR   AlphaFoldDB; A0KP86; -.
DR   STRING; 380703.AHA_3617; -.
DR   CAZy; GH77; Glycoside Hydrolase Family 77.
DR   EnsemblBacteria; ABK39407; ABK39407; AHA_3617.
DR   KEGG; aha:AHA_3617; -.
DR   PATRIC; fig|380703.7.peg.3606; -.
DR   eggNOG; COG1640; Bacteria.
DR   HOGENOM; CLU_022072_1_1_6; -.
DR   OrthoDB; 9763489at2; -.
DR   Proteomes; UP000000756; Chromosome.
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   ECO:0000313|EMBL:ABK39407.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756};
KW   Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:ABK39407.1}.
SQ   SEQUENCE   758 AA;  84174 MW;  11C389FDDFB7C389 CRC64;
     MAHRATVQVP PIKINQNSID RIHSGNSQTM TTLIEQLAAA KGIASEYVDA WGHPAQVSEE
     SKAAMLGAMG YRVDDEAALT EQLEQEHRQH WLRALDPVMV VRSGEPITLE VRLPIEFVND
     ALSWQLKLEQ GGLLSGQLTP IDGELVGVAE FEEMECQAYR VALAVQPELG YHDLILLEEG
     NDEPLASMRL IVAPKACYKQ PPIANGRKVW GPSVQLYCLR SRHNWGIGDF SDLGQLVEKM
     AAWGAHFVGL NPIHALYPAN PESASPYSPS SRRWLNVAYI DVEAVPEFLA NARLKAEVAN
     PAFQQHLSEL RAKGNVDYTG VVETKLGMLR QVFDQASLSA ERQAAFDAFV AAGGDSLQQQ
     AAFDALQAHF YAKGENAWGW PVWPEPFRDY HNPEVAAWMA EHRQDVNFYL YLQFLADEQL
     ARADARAKAA GMVMGIYRDL AVGVSEGSTE IWANRDLYCP KASVGAPPDI LGPLGQNWGL
     PPMNPNQLFE AAYQPMVDLF RANMRSCGAL RIDHVMALLR LWWVPPGESA AKGAYIYYPV
     NDLLGILALE SHRNQCLLIG EDLGTVPEGI DVTLKENGVH SYKVFFFERS KADGGFISPA
     HYAEQAMSAL TTHDMPTLKG FWHCDDLALG RELGLYPDED VLKTLYADRH QAKQRILDSL
     HGHGVISGNI SHDVNWVGMN TELNHGLQLH MSRGSCALFS TQLEDWLEMD KPVNVPGTSY
     EYPNWRRKLS TDLEDIFANE ALKALAGKMS QARDEASR
//
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