MALQ_AQUAE
ID MALQ_AQUAE Reviewed; 485 AA.
AC O66937;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=4-alpha-glucanotransferase;
DE EC=2.4.1.25;
DE AltName: Full=Amylomaltase;
DE AltName: Full=Disproportionating enzyme;
DE Short=D-enzyme;
GN Name=malQ; Synonyms=malM; OrderedLocusNames=aq_723;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the disproportionating enzyme family.
CC {ECO:0000305}.
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DR EMBL; AE000657; AAC06897.1; -; Genomic_DNA.
DR PIR; E70363; E70363.
DR RefSeq; NP_213497.1; NC_000918.1.
DR RefSeq; WP_010880435.1; NC_000918.1.
DR PDB; 1TZ7; X-ray; 2.15 A; A/B=1-485.
DR PDBsum; 1TZ7; -.
DR AlphaFoldDB; O66937; -.
DR SMR; O66937; -.
DR STRING; 224324.aq_723; -.
DR CAZy; GH77; Glycoside Hydrolase Family 77.
DR EnsemblBacteria; AAC06897; AAC06897; aq_723.
DR KEGG; aae:aq_723; -.
DR PATRIC; fig|224324.8.peg.580; -.
DR eggNOG; COG1640; Bacteria.
DR HOGENOM; CLU_014132_1_0_0; -.
DR InParanoid; O66937; -.
DR OMA; TGQLWGT; -.
DR OrthoDB; 814704at2; -.
DR BRENDA; 2.4.1.25; 396.
DR EvolutionaryTrace; O66937; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 InterPro; IPR003385; Glyco_hydro_77.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR32438; PTHR32438; 1.
DR Pfam; PF02446; Glyco_hydro_77; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR TIGRFAMs; TIGR00217; malQ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Glycosyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..485
FT /note="4-alpha-glucanotransferase"
FT /id="PRO_0000170119"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:1TZ7"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 24..36
FT /evidence="ECO:0007829|PDB:1TZ7"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:1TZ7"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 97..113
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 118..127
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 129..145
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 161..170
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 172..198
FT /evidence="ECO:0007829|PDB:1TZ7"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:1TZ7"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 216..220
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:1TZ7"
FT STRAND 233..239
FT /evidence="ECO:0007829|PDB:1TZ7"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:1TZ7"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 258..263
FT /evidence="ECO:0007829|PDB:1TZ7"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 267..277
FT /evidence="ECO:0007829|PDB:1TZ7"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:1TZ7"
FT STRAND 293..298
FT /evidence="ECO:0007829|PDB:1TZ7"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:1TZ7"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 314..324
FT /evidence="ECO:0007829|PDB:1TZ7"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 340..348
FT /evidence="ECO:0007829|PDB:1TZ7"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:1TZ7"
FT STRAND 375..381
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 389..394
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 398..408
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 417..427
FT /evidence="ECO:0007829|PDB:1TZ7"
FT STRAND 431..436
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 437..440
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 445..447
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 467..470
FT /evidence="ECO:0007829|PDB:1TZ7"
FT HELIX 471..480
FT /evidence="ECO:0007829|PDB:1TZ7"
SQ SEQUENCE 485 AA; 58086 MW; D6D9B98BB90A0E22 CRC64;
MRLAGILLHV TSLPSPYGIG DLGKEAYRFL DFLKECGFSL WQVLPLNPTS LEAGNSPYSS
NSLFAGNYVL IDPEELLEED LIKERDLKRF PLGEALYEVV YEYKKELLEK AFKNFRRFEL
LEDFLKEHSY WLRDYALYMA IKEEEGKEWY EWDEELKRRE KEALKRVLNK LKGRFYFHVF
VQFVFFKQWE KLRRYARERG ISIVGDLPMY PSYSSADVWT NPELFKLDGD LKPLFVAGVP
PDFFSKTGQL WGNPVYNWEE HEKEGFRWWI RRVHHNLKLF DFLRLDHFRG FEAYWEVPYG
EETAVNGRWV KAPGKTLFKK LLSYFPKNPF IAEDLGFITD EVRYLRETFK IPGSRVIEFA
FYDKESEHLP HNVEENNVYY TSTHDLPPIR GWFENLGEES RKRLFEYLGR EIKEEKVNEE
LIRLVLISRA KFAIIQMQDL LNLGNEARMN YPGRPFGNWR WRIKEDYTQK KEFIKKLLGI
YGREV
