ID A0A0X3WNZ2_9ACTN Unreviewed; 695 AA.
AC A0A0X3WNZ2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=ADL30_10275 {ECO:0000313|EMBL:KUL58555.1};
OS Streptomyces sp. NRRL S-1521.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609100 {ECO:0000313|EMBL:KUL58555.1, ECO:0000313|Proteomes:UP000053420};
RN [1] {ECO:0000313|EMBL:KUL58555.1, ECO:0000313|Proteomes:UP000053420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL S-1521 {ECO:0000313|EMBL:KUL58555.1,
RC ECO:0000313|Proteomes:UP000053420};
RA Gilbert D.G.;
RL Submitted (OCT-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:KUL58555.1}.
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DR EMBL; LLZK01000121; KUL58555.1; -; Genomic_DNA.
DR RefSeq; WP_062772667.1; NZ_LLZK01000121.1.
DR AlphaFoldDB; A0A0X3WNZ2; -.
DR Proteomes; UP000053420; 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|RuleBase:RU361207};
KW Reference proteome {ECO:0000313|Proteomes:UP000053420};
KW Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:KUL58555.1}.
FT REGION 625..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..687
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 695 AA; 74261 MW; EE09F59C68851B5D CRC64;
MTEAILGLAR AHGVATEYTT DRGRRVAVPA DTLVAVLGAC GVDATTPAAA REALDRHRAE
QAARLLPPCV VTRAGEGVTL PRTSVGEVAV EGGGTLPADA PLPPGHHTLR VRAGEREARA
PLLAVPDRLA VPDRRAWGLI VQLYSVLSRR SWGMGDLADL AELATWSGRD LGAGFVQLGP
LHAVPPGPLP DPSPYRPSSR RFPDPMHVRV EAVPEYAYLD RAGRDAAHAL VDQARAVNAR
VLDGSSLIDR ETVRSLKHRA LRAVHAVPLS PGRAAAFAAF TAREGQGLTD FATWCALADA
HGADWRCWPV ELRDPRSPAV ARARDDLAES VAFHRWLAWI TDEQLAVAQR AAKDAGMAIG
LVHDLAVGVA PDGADAWALQ HCLAAGMSVG APPDDFNPLG QDWGQPPWRP DALAAAGYLP
FAELLRSNLR HAGALRVDHV MGLFRLWWVP EGRPPSEGTY VRYDAHAMLG ALTLEAHRAG
ASVIGEDLGT VEKGVREELA GRGILGTSVQ RFEYVGGSEG RHGPLPPDQW RANCLATLTT
HDLPTTAAWL SGEHVELRER LGLLTRPAEA EKAEAASERD GWLAELTRLG LLPSPDGEVA
ALHRFLPLTP ALLLGVWLPD ATGDRRPQNL PGTSTVHPNW RLPVSDAEGR PVPLEELPAS
PLVRTVAGVF ADPGPRPAPP SPHHPDPRST TPSTT
//
