ID V5XDA8_MYCNE Unreviewed; 702 AA.
AC V5XDA8;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=D174_15935 {ECO:0000313|EMBL:AHC25987.1};
OS Mycolicibacterium neoaurum VKM Ac-1815D.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=700508 {ECO:0000313|EMBL:AHC25987.1, ECO:0000313|Proteomes:UP000018763};
RN [1] {ECO:0000313|EMBL:AHC25987.1, ECO:0000313|Proteomes:UP000018763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-1815D {ECO:0000313|EMBL:AHC25987.1,
RC ECO:0000313|Proteomes:UP000018763};
RX PubMed=24435872;
RA Shtratnikova V.Y., Bragin E.Y., Dovbnya D.V., Pekov Y.A., Schelkunov M.I.,
RA Strizhov N., Ivashina T.V., Ashapkin V.V., Donova M.V.;
RT "Complete Genome Sequence of Sterol-Transforming Mycobacterium neoaurum
RT Strain VKM Ac-1815D.";
RL Genome Announc. 2:e01177-13(2014).
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; CP006936; AHC25987.1; -; Genomic_DNA.
DR RefSeq; WP_019509955.1; NC_023036.2.
DR AlphaFoldDB; V5XDA8; -.
DR KEGG; mne:D174_15935; -.
DR eggNOG; COG1640; Bacteria.
DR HOGENOM; CLU_022072_1_0_11; -.
DR Proteomes; UP000018763; 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:UP000018763};
KW Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:AHC25987.1}.
FT DOMAIN 65..156
FT /note="MalQ N-terminal beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF21226"
SQ SEQUENCE 702 AA; 77769 MW; 5A339E862478B90E CRC64;
MTELAELAQR YAVATEFVDW RGRSVPVPEH TLVSVLAALG VPADTPADRE HAARTHDREY
WGDALPPTVV ARSGTASSFW VHVTHGRPVD VWVELEDGSV RTELRQLENN RAPYDLDGRT
IGEATFELPA DLPPGYHRLH ARTDTGETDT TVIVAPAVLA PPRRRHWGLA TQLYSVTSEQ
SWGTGDLTDL TDLAVWSAAR HGAGFILVNP LHAAAPVAPM EPSPYLPTSR RFVNPLYLRV
EAIDEYAQLR RRGPLRKARA ELAGRARRRD GIDRDAAWKV KRAALQQVYR VPRSAGRDLA
YAAFRDREGR SLDDFATWCA LAEVHGPDWH TWPQKLTHPD NPEVAAFAAA NEAAVDFHRW
LQWQLDDQLT TAQARATQAG MGLGIMHDLA VGVDPDGADA WALQDVLARG VSAGAPPDEY
NQLGQNWSQP PWRPDQLRRT GYAPFRALVN AVLRHAGGVR IDHIIGLFRL WWIPQGAAPT
EGTYVRYDHD ALIGIVALEA YRSGAVVVGE DLGTVEPWVR DYLRDRGLFG TSILWFERTD
GGAPLPAERW REACLSAVTT HDLPPTAGYL AGEHIRLRES LGLLTRPVDE EIADDRIEQQ
AWLDELRRLG LLGEQPDIDE IVRGLHAFLG RTPSKLLALA LPDAVGDLRA QNQPGTTDEY
PNWRVPLSGP DGERMSLEDV FTDPRANALA EVMKAQVPAM DT
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