ID G0JKR6_9PROT Unreviewed; 1712 AA.
AC G0JKR6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=Acife_0609 {ECO:0000313|EMBL:AEM46812.1};
OS Acidithiobacillus ferrivorans SS3.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=743299 {ECO:0000313|EMBL:AEM46812.1, ECO:0000313|Proteomes:UP000009220};
RN [1] {ECO:0000313|EMBL:AEM46812.1, ECO:0000313|Proteomes:UP000009220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS3 {ECO:0000313|EMBL:AEM46812.1,
RC ECO:0000313|Proteomes:UP000009220};
RX PubMed=21705598; DOI=10.1128/JB.05373-11;
RA Liljeqvist M., Valdes J., Holmes D.S., Dopson M.;
RT "Draft genome of the psychrotolerant acidophile Acidithiobacillus
RT ferrivorans SS3.";
RL J. Bacteriol. 193:4304-4305(2011).
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; CP002985; AEM46812.1; -; Genomic_DNA.
DR RefSeq; WP_014028081.1; NC_015942.1.
DR STRING; 743299.Acife_0609; -.
DR KEGG; afi:Acife_0609; -.
DR eggNOG; COG1640; Bacteria.
DR eggNOG; COG3280; Bacteria.
DR HOGENOM; CLU_002501_0_1_6; -.
DR Proteomes; UP000009220; 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:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11336; AmyAc_MTSase; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 4.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR003385; Glyco_hydro_77.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013797; Maltooligo_trehalose_synth_4.
DR InterPro; IPR012767; Trehalose_TreY.
DR NCBIfam; TIGR00217; malQ; 1.
DR NCBIfam; TIGR02401; trehalose_TreY; 1.
DR PANTHER; PTHR32438; 4-ALPHA-GLUCANOTRANSFERASE DPE1, CHLOROPLASTIC/AMYLOPLASTIC; 1.
DR PANTHER; PTHR32438:SF5; 4-ALPHA-GLUCANOTRANSFERASE DPE1, CHLOROPLASTIC_AMYLOPLASTIC; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02446; Glyco_hydro_77; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361207};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU361207,
KW ECO:0000313|EMBL:AEM46812.1}; Isomerase {ECO:0000313|EMBL:AEM46812.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009220};
KW Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:AEM46812.1}.
FT DOMAIN 759..1327
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1712 AA; 193248 MW; A6207B1E0C7D40E0 CRC64;
MKASFDKDLI RELCQSYGVL EHYHNAFGRK HVVPQGTLLA LLNALGVPTE NAQAAREALR
QKEAASWQSP LPPLLVQRIT TEPPRVALSL PADVAQEIWH WRFCPEEGEA QEGTFQPADL
ELLGEGCIGT RVYRRYRLEL PFAPRLGYHH LILQGPDGCW AEMPWITVPE ACYTPEAIQA
SRKVWGPALQ LYALRSGRNW GMGDFSDLLQ VLDFAAQSGA ELVGLNPLHA LFPDNPHHAS
PYSPSSRKFL NILYVDVEAV PEFAHCEAAH DRVYDAHFQA DLRALRGADL VDYGGVAAAK
REILELLYRA FRETELPGNG ERARAFRQFQ IEGGAALFRL GVFEALREHL QTQDPPPWGW
PIWPEKYRRP EAPAVAEFAT QQPDRVEFFQ YLQWVVAEQL DAVGQRSYAL DLGIGLYQDI
AVGVDPGGFD AWNDQDLYVS NIHVGAPPDA FNRKGQDWGL QPWHPLRLRE AAYAPFVALL
RANMRVAGAI RLDHILGLMR LYWIPAGESP ARGGYVRYPL DELLGILTLE SQRHHCLVVG
EDLGMVTEEI RDALQSWGIL SYRVLLLEAD PQHGYRPPED YPAWSVAALT THDLPTLAGF
WQGLDLDTRA ALDLIPDTAT RDSLIVERAR DRSFLLLALE REGLLPRGVG VQPVDLSKLT
DDMIRAIHHL LARAASAVLL VQMDDVLAVT DQSNLPGTAD QYPNWRRKLP LTLEQWAEDP
HVNGLFATLR EVRPVPPRGQ IAEATIPIPR ATYRLQFNQN FTFNDAAALV PYLTRLGISH
CYASPILKAR KGSPHGYDIV DHNALNQEIG SSEDFLRFSD TLAAHGMGLM LDIVPNHMGA
LGSDNAWWLN VLEHGPASPY ADYFDIDWYP LNPQLRGKVL LPVLGDHYGQ VLEDGELKLC
FAAEQGEIYI QYLENSFPVD PREYPRILDL RADILRTELG MEHPDTQELA TLSDALRRLP
ERYSAEAESR AARVRDGTVY RRLLAELCAR SPEVTAFLQE NIVLFNGHPG DAESFDSLHR
LIEAQAYRLA FWRVAADDIN YRRFFDINDL AGLRMEDPAV FGDAHRLIFR LLSEGRVNAL
RIDHPDGLYD PQMYFRRIQA WRAWRQARRD KGGRSLYLVV EKILADGEAM PPDWPVHGST
GYDFANDVTS LFVNDRARAA FERLYSAFIG HPCDFDTLLY DCKKLIMKSS MASELNVLAD
HLSHIAQTDR RTRDYTLNGL RWALQEVIAY FPVYRTYSAD GILLDADRQR VQTAINQARR
NSQAEDVSVF QFLEEVLTLS ALPGNPPAYT RERIAFVGKF QQYTGPVMAK GGEDTALYRY
QRLTCLNDVG GDPRHFGISV AAFHKSCRDR AAYRPHDMLT SSTHDSKRSE DVRARIAVLS
EMPKRWQQAL QRWQHLNNGK KGRIDGNSAP DANDEYLIYQ TLLGTWPAQE TPDADYVERI
VAYMRKVVRE AKVHSSWINP DSAYEEALER FIRAILDKDS HNPFPSACTD LCRIIRHFGT
LNSLGMTLLK LTAPGVPDIY QGCEDLVLHL VDPDNRRPVD FAAYSDALSE LESRFSVHVR
TEDLQDLLIE PDRGRLKLYL TWRSLEARRQ RPELFQSGSY ISLRACGKHA KHLCAFARKG
PDGVALTVVP RLCFRLLGAD ESHPLPLGLE VWEDTALILP KNWKALRFRN QFTGEDLDLQ
GGAEALSVGR LLSRFPLALL LADPESSVQA KS
//
