ID A0A0M2XTN4_9SPHI Unreviewed; 1401 AA.
AC A0A0M2XTN4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-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=AAW12_24895 {ECO:0000313|EMBL:KKO89466.1};
OS Sphingobacterium sp. Ag1.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1643451 {ECO:0000313|EMBL:KKO89466.1, ECO:0000313|Proteomes:UP000034524};
RN [1] {ECO:0000313|EMBL:KKO89466.1, ECO:0000313|Proteomes:UP000034524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKO89466.1,
RC ECO:0000313|Proteomes:UP000034524};
RA Pei D., Yu W., Kukutla P., Xu J.;
RT "Draft Genome Sequences of Sphingobacterium sp. Ag1 from Mosquito Anopheles
RT gambiae.";
RL Submitted (APR-2015) 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:KKO89466.1}.
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DR EMBL; LBGU01000044; KKO89466.1; -; Genomic_DNA.
DR PATRIC; fig|1643451.3.peg.997; -.
DR Proteomes; UP000034524; 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 CDD; cd11336; AmyAc_MTSase; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 3.30.1590.10; Maltooligosyl trehalose synthase, domain 2; 1.
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 Transferase {ECO:0000256|RuleBase:RU361207}.
FT DOMAIN 26..489
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1401 AA; 162238 MW; B4C078CAB6FE8E66 CRC64;
MQTNRNVSIN KPNTTYRIQF HKAFNFADFK AIIPYLLNLG IDTIYAAPIL QSTPGSVHGY
DGVNMHQINP ELGTLDELRA IKKQLRESNI KWIQDIVPNH MAFHPANEWL MDLLEFGQSS
TFSRFFDTCY SSNLFEQGKL MVPVLAKTLD EAISDNEITV VSSDDSLRLS YLGNVYPISP
ESYGFILGDY LRDTQADFSG LLVQINTAQA NGDNEEWKQL RVHLFKDLSD DILTSMLQRF
NADPDRILAL VTSQNYELCP WWHTHQRINY RRFFTVNELI CLNVQDEEVF KQSHELIKTL
VDEGLIDGLR IDHIDGLYNP TAYLYNLRKY IGPKTYIVAE KILEKGEKLP LEWPIQGTTG
YDFLSVCNNV CSCQSGKKIL NNYYRKVTGE NLSIKKDQYA KKCKILTDQM QGEVDNLAKS
LASLLGVADQ EKRDALKDIL KSFIALFPVY RLYDDCFPLS ITNFELVSSL FDKLMKNPEL
DQELVDQFRN LFQQAQVAYQ SPNQTALVDF FLRCMQLTGP VMAKGVEDTL MYTYNRFIGH
NEVGDHPQNL GLSIKQFHRF MQDRQKDWRL SINASSTHDT KRGEDSRSRL LVLTAMAQKW
VKQLRIWQDV VWNEYRKDLP HPNDEYFIYQ SLVSSYPMEK QDAKANTASF EERFLDYLVK
YLREGKERSS WENPNLVYEA SVRDFASFLL DKDRPFFTSF YQFIEAVADY GILNSLIQQI
LKFTCPGIPD IYQGSELWNY SFVDPDNRRP IAYELSKSLL DTIEETAKEE RIPFLWRNRY
DGRIKLWLVK ELVKLRKDDH TLAPDSSYIP LKVTGRYRKH ILAFARRSGD EWLVVILPLH
LAAIGKISKF VPCSFDWSDT KVQLLTHRSV TWQHILMDSS GEGTEVSINA IFKDLPMAIL
KYKDSTQKRS SGVLLHISSL PSSYGIGDLG NEARRFVKQL QRGGQSWWQI LPLGPTDLAQ
CYSPYSTLSS RAGNPLLIDL KELLKFGLLN KDELKILKKK SLQTIDFAEI NSSKYRLLEK
AFHRLPAQPT HEFSEFIDRE SSWLDDYALF KVLKNRHDDL PWYQWPALYK LRDSAALEDF
ATRFADELQQ EKWFQFLFFR QWSALRNFAR DYGIRFIGDI PFYVAYDSAD VWVNPQYFSL
KADGTINHVA GVPPDYFNAD GQLWGMPTYN WSSLQKDGYQ WWVERLSHNC TLFDTLRLDH
FRAFSSYWEV PHEETSAKNG SWVVGPGSDF FDHVKTTLDH MPFIAEDLGD IDAKVYQLRN
EYNFPGMAVL QFAFGNDMPH SPHIPHQYNR NTVAYTGTHD NNTSLSWFNQ DLDGAGKERI
NNYYGQIVEN TNLNDVLIRS LYASVADSVI IAMQDILNLD GSCRMNRPAS TAGNWVWRMQ
KGAFAANHQE KLAYYTKLYN R
//
