ID F1T5J9_9ACTN Unreviewed; 1125 AA.
AC F1T5J9;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
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 Name=malQ {ECO:0000313|EMBL:EGF23144.1};
GN ORFNames=HMPREF0091_10091 {ECO:0000313|EMBL:EGF23144.1};
OS Fannyhessea vaginae DSM 15829.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Fannyhessea.
OX NCBI_TaxID=525256 {ECO:0000313|EMBL:EGF23144.1, ECO:0000313|Proteomes:UP000005947};
RN [1] {ECO:0000313|EMBL:EGF23144.1, ECO:0000313|Proteomes:UP000005947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15829 {ECO:0000313|EMBL:EGF23144.1,
RC ECO:0000313|Proteomes:UP000005947};
RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL Submitted (FEB-2011) 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:EGF23144.1}.
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DR EMBL; ACGK02000001; EGF23144.1; -; Genomic_DNA.
DR RefSeq; WP_006302200.1; NZ_ADNA01000037.1.
DR AlphaFoldDB; F1T5J9; -.
DR GeneID; 78488847; -.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG1640; Bacteria.
DR OrthoDB; 9811841at2; -.
DR Proteomes; UP000005947; 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:InterPro.
DR CDD; cd11338; AmyAc_CMD; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 3.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR003385; Glyco_hydro_77.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR045857; O16G_dom_2.
DR PANTHER; PTHR32438; 4-ALPHA-GLUCANOTRANSFERASE DPE1, CHLOROPLASTIC/AMYLOPLASTIC; 1.
DR PANTHER; PTHR32438:SF5; 4-ALPHA-GLUCANOTRANSFERASE DPE1, CHLOROPLASTIC_AMYLOPLASTIC; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02446; Glyco_hydro_77; 2.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000313|EMBL:EGF23144.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005947};
KW Transferase {ECO:0000313|EMBL:EGF23144.1}.
FT DOMAIN 150..562
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1125 AA; 128200 MW; CFE45DA22A93E5B9 CRC64;
MRAQHNSLDT RYRSIAGAVA VGEQLRLTID IWDDVPRRVV LRTWTDEEKE KLVPMRKVGC
SERRNIVLCG ELNGGCRYGV TLTFDKPQVL WYSFQITSSK GDVWRYGAAQ EDKVGVGAFA
YGEPPSFQVT VYKKQRTVDP TWYTQGVAYQ IFPDRFARDD NWRARCERVL SIPRKGVTRR
LVGDWNTYPY YERDADGNIL AWDFYGGSLQ GIISKLDYLK NLGITIIYLN PIVEAQSNHR
YDTADYFHVD PMLGTDEDFE ELCKRASDMG ISIMLDGVFN HVGADSHYFN ACGNYAELPA
SNKKATTHSW FTFNDSGAYD CWWGIKDLPA IRKHCPEFRE LICGENGVIR TWLRRGARAW
RLDVVDELTD DFVEDIKSAA LAEKPDSVVI GEVWEDASHK RAYGNLRKYF QGAELDATMN
YPLRDALISF ITRRSSADSF ASSIESLRAN YPREAFYAEF NMMSTHDRAR ILTMLGDAPD
KSAISEGDQY WFRLNPGCRA LAVSRLWLTT LIQMCLPGVP CVYYGDEAGL EGYSDPFCRF
TFPWENPDKN CQIIYRNAIQ LRKTLDVFVT GDLHVRSFGY DVFGMWRRDK TTSVCVLVNT
HTEMSQTVDI PVENFVPLTQ NLGKDMQALR LVDLLTGNEY QAHNGTLTLT LQNLGSMILC
ASIKTPLSLP FKPGAGVLCH ITSLPGGTLG QPSYNFVNYL SQAHMRYWQM LPVHPVDEDK
SPYAGYSAFA GNMALVEQQE QCNTKDDEDE DNTPDSVEFH RFVQDNDHWL VPYACFRALK
KRYKGVCWQK WPAPYNRWDP AFTREHDLLD DIETCVKKQF IFDRQWRALK AYAHENGVSL
IGDIPMYVSA DSADVWTNPQ MFNLDVDGYP TLAAGVPPDE FSATGQLWGN PTYNWDLMEQ
DGFSWWTRRL AREFDLFDYV RLDHFLGFSS YFAIPVTKQA VRGSEQTESE EAAIQAIAHG
SWREGPGVRV MRALYKKLGP LPLIAEDLGI VTPAVRALLM DTHICGMDVM QFSHEDVRFG
YHPSYKKVAY TSTHDTQTLI GWCKDHYHMD SYTAEKQAEY LLSEAFSSDA LVSIATLQDI
LHLDDSARMN VPGTSNDNWS WQANTEDLAT SAEYVRTLVD QTGRI
//
