ID   E3B937_9MICO            Unreviewed;       747 AA.
AC   E3B937;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
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   Name=malQ {ECO:0000313|EMBL:EFP58434.1};
GN   ORFNames=HMPREF0321_2287 {ECO:0000313|EMBL:EFP58434.1};
OS   Dermacoccus sp. Ellin185.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC   Dermacoccus.
OX   NCBI_TaxID=188626 {ECO:0000313|EMBL:EFP58434.1, ECO:0000313|Proteomes:UP000003057};
RN   [1] {ECO:0000313|EMBL:EFP58434.1, ECO:0000313|Proteomes:UP000003057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin185 {ECO:0000313|EMBL:EFP58434.1,
RC   ECO:0000313|Proteomes:UP000003057};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (OCT-2010) 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:EFP58434.1}.
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DR   EMBL; AEIQ01000057; EFP58434.1; -; Genomic_DNA.
DR   RefSeq; WP_006944828.1; NZ_AEIQ01000057.1.
DR   AlphaFoldDB; E3B937; -.
DR   eggNOG; COG1640; Bacteria.
DR   Proteomes; UP000003057; 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   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   ECO:0000313|EMBL:EFP58434.1};
KW   Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:EFP58434.1}.
FT   DOMAIN          71..147
FT                   /note="MalQ N-terminal beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF21226"
FT   REGION          152..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..179
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   747 AA;  81920 MW;  C17B4604864E4765 CRC64;
     MTDSAATPDL VELAEAYGIT TEYEDWKKAR VSVAADTLVA VLAALDVDAS TPDAVRSALQ
     TRRDAPWRRV VPPCVVVREG DDVEFPVHVV ECDQVAVHVV TEVGTHVSVT VSSRAQETRE
     VDGRVVERHV ARVDGDLPLG YHTVIVSPVG LAAGDGDSDD TRVDGEDRPS TEAGDGHDTR
     AAGARASLIV TPRVLEVPAT MRDKRVWGLA TQLYSVRSQG SWGVGDLVDL RDLAVWSAAE
     HGADYVLVNP LHAAQPSAPM EPSPYLPTSR RFVNPLYLRV EHVEEYASAS ADIRGVIDDL
     ARDVHARLDD VDRIDLDAAW GAKEQALRVL WQIGRTPGRQ AAFDAYCRAG GEQLTRFATW
     CVLFRTFGPD WRTWPHDYQD ATAPAVSRFG SEHADEVDFH RWLQWCLDEQ LRGVQSDAVA
     AGMALGVVHD LAVGVNPAGA DAWALQDAFA AGIHVGAPPD QFTQLGQDWG QPPLRPDRLA
     ETAYAPFREI VGTVLRHAGG VRIDHILGLF RLWWVPESMT PKDGTYVTYD HEAMIGILVL
     EAQRAGALVV GEDLGTLEAW VQTFLAERGV YGTSILWFEQ DWDAQRPLPP EDWREKCLAS
     VTTHDLPPTA GYLDAAHVRL RHELGLLDGS LEDELARDEA DRRRWREFLV AQGLLDDADA
     PNEQVVEALH AFLVTTPSRM LNVALVDAVG DVRVQNQPGT ADEYPNWRVP LSGPDGEPIR
     LEDVFTSERA ARLCGIFAGL NEHAAQG
//