ID H2IQD2_RAHAC Unreviewed; 708 AA.
AC H2IQD2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 58.
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 OrderedLocusNames=Rahaq2_0245 {ECO:0000313|EMBL:AEX50192.1};
OS Rahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 /
OS NCIMB 13365 / CIP 78.65).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Rahnella.
OX NCBI_TaxID=745277 {ECO:0000313|EMBL:AEX50192.1, ECO:0000313|Proteomes:UP000009010};
RN [1] {ECO:0000313|EMBL:AEX50192.1, ECO:0000313|Proteomes:UP000009010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 /
RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010};
RX PubMed=22582378; DOI=10.1128/JB.00380-12;
RA Martinez R.J., Bruce D., Detter C., Goodwin L.A., Han J., Han C.S.,
RA Held B., Land M.L., Mikhailova N., Nolan M., Pennacchio L., Pitluck S.,
RA Tapia R., Woyke T., Sobecky P.A.;
RT "Complete Genome Sequence of Rahnella aquatilis CIP 78.65.";
RL J. Bacteriol. 194:3020-3021(2012).
RN [2] {ECO:0000313|Proteomes:UP000009010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 /
RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Held B., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sobecky P.,
RA Martinez R., Woyke T.;
RT "Complete sequence of chromosome of Rahnella aquatilis CIP 78.65.";
RL Submitted (JAN-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}.
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DR EMBL; CP003244; AEX50192.1; -; Genomic_DNA.
DR RefSeq; WP_014333500.1; NC_016818.1.
DR AlphaFoldDB; H2IQD2; -.
DR STRING; 745277.Rahaq2_0245; -.
DR GeneID; 61510397; -.
DR KEGG; raq:Rahaq2_0245; -.
DR PATRIC; fig|745277.3.peg.236; -.
DR HOGENOM; CLU_022072_1_1_6; -.
DR OMA; HEMKARA; -.
DR OrthoDB; 9763489at2; -.
DR Proteomes; UP000009010; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000009010};
KW Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:AEX50192.1}.
FT DOMAIN 53..128
FT /note="MalQ N-terminal beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF21226"
SQ SEQUENCE 708 AA; 79229 MW; C5D622EBBEB1F197 CRC64;
MEDKQLAEAA RRAGIVDSFI NMTDDVETVS DDTRVALLAA MGRDPADVPE ITPVPPVNVF
TQGKKVLLTP EVSGAFSWQL TQENGSQTQG EIPAGTVLNL GAALPTGYHQ LTLSQNGNVW
PCRIIVVPPR CYEPEALLTG EKLWGATLQL YTLRSENNWG VGDFGDLKKM VEEIGLRGGA
FVGLNPIHAL YPANPQSASP YSPSSRRWLN LTYIDVNAVE EFTASSEAQR WWHSHETREA
LLQARSTEFV DYPQVIELKL TALKLAWQLF CSLPESRPRK QDFRQFVELG GESLRQQALF
DALHVHLRDL DLGQWGWPVW PEAYRDAKSA DVREFSERYA SEVAFYQWLQ WLAQTQFSAC
YQRSVELKMP IGVYRDLAVG VAQGGAETWS DPALYCLNAT VGAPPDILGP QGQNWGLPPI
DPHEMKARAY QPFIDLLRAN MAECGALRID HVMGLLRLWW IPADQEAGSG AYVRYPLEDL
LGVLALESQR HQCMVIGEDL GTVPKEILAS LRDCGVYSYK VLYFEHDKNF LYRPPQDYVS
QAMATVTTHD LPTLRGYWEG ADLTLGASLG VYPDPLVLEK LRGERERSKQ GLLDALHRTG
CVPKSISRSA ENMPMMPLLN RGLQRYLAGS ASALLGLQPE DWLDMSTPVN VPGTNTEYPN
WRRKLTRTLE EMFADEYIDA LLSDLNQRRA CASSAKPSPR LPLRRGRS
//