ID L1N5E4_9BACT Unreviewed; 913 AA.
AC L1N5E4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=4-alpha-glucanotransferase {ECO:0000256|ARBA:ARBA00020295};
DE EC=2.4.1.25 {ECO:0000256|ARBA:ARBA00012560};
DE AltName: Full=Amylomaltase {ECO:0000256|ARBA:ARBA00031423};
DE AltName: Full=Disproportionating enzyme {ECO:0000256|ARBA:ARBA00031501};
GN ORFNames=HMPREF9151_01999 {ECO:0000313|EMBL:EKX98401.1};
OS Hoylesella saccharolytica F0055.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=1127699 {ECO:0000313|EMBL:EKX98401.1, ECO:0000313|Proteomes:UP000010433};
RN [1] {ECO:0000313|EMBL:EKX98401.1, ECO:0000313|Proteomes:UP000010433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0055 {ECO:0000313|EMBL:EKX98401.1,
RC ECO:0000313|Proteomes:UP000010433};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-2012) 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 -!- SIMILARITY: Belongs to the disproportionating enzyme family.
CC {ECO:0000256|ARBA:ARBA00005684}.
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:EKX98401.1}.
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DR EMBL; AMEP01000114; EKX98401.1; -; Genomic_DNA.
DR RefSeq; WP_009163304.1; NZ_KB291010.1.
DR AlphaFoldDB; L1N5E4; -.
DR STRING; 1127699.HMPREF9151_01999; -.
DR PATRIC; fig|1127699.3.peg.1834; -.
DR HOGENOM; CLU_014132_0_0_10; -.
DR OrthoDB; 9811841at2; -.
DR Proteomes; UP000010433; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR003385; Glyco_hydro_77.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR32518; -; 1.
DR PANTHER; PTHR32518:SF3; 4-ALPHA-GLUCANOTRANSFERASE; 1.
DR Pfam; PF00686; CBM_20; 1.
DR Pfam; PF02446; Glyco_hydro_77; 1.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000010433};
KW Transferase {ECO:0000313|EMBL:EKX98401.1}.
FT DOMAIN 142..249
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
SQ SEQUENCE 913 AA; 106945 MW; D0138337B3FB2735 CRC64;
MNLYFNIEYQ TIFGEEVVLN VFTDDECTPA AVTKYRMNTV DGQHWTCCIT QLPAACKKVI
HYYYGVDCAG TEKRKEWTLK PHRLELTSDK AKVYYIYDRW SDMPEDAYLY SSAFTDCIRR
KHGERKETPR KTEHAHTGSK HNTAAYEKTL RLIVSAPQLR SEQRLVVVGN DLALGAWTLS
RAIDMTEVSL NEWAVDLDID RFSGHRIELK FVAVSADKHT APLWETGYNR ILELPELKKG
EVVVYSLNQA FFELCNERFA GTLVPVFSLR SKESFGVGDF GDLQRMINFV SATRQRVLQV
LPINDTTTTH TWTDSYPYSC ISIFAIHPQY VDLTQLPPLK DTKVRARFKR LQEELNALPQ
IDYERVNATK NEYLRLIFEQ EGSLMMKSDA FSRFFNEEAH WLVPYAQYCY LRDQYGTADF
SQWKDHHTWD ETQRKALSTP TTKAYKQVSF FYFVQFILSQ QMQAAHEYAK SKGVILKGDI
PIGVSRYGCD VWMEPKYFHM NGQAGAPPDD FSVNGQNWGF PTYNWDEMLK DNCAWWVHRF
QYMAKFFDAY RIDHVLGFFR IWEIPITSVH GLLGQFSPAL GLSREEIEAY GLPFNEDAFT
RPFIADWVLA RMFGEHADEV KATYLQHDHD DIWQMRPEYD TQRKVEAAFE GREDDKNLWI
RDALYALISD VLFVRDRKDP LRFHPRISVQ HSFVYEALWD KDKVAFNNLY NDYYYRRNNQ
FWYNEAMKKL PMLTEATRML VCAEDLGMVP ACVDWVMNQL RILSLEVQSM PKDANVRFGN
LNTYPYRSVC TFSSHDMPTL RQWWDEDPSR TQVYYNSMLY KQGDAPHPLP GWLARDIILQ
QLRSPSMLCI LSIQDWLSTD EALRLPDADA ERINIPANPR HYWRYRMHIT IEELMNNVPF
CTAVTDLVQQ SGR
//
