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Database: UniProt
Entry: F8CK62_MYXFH
LinkDB: F8CK62_MYXFH
Original site: F8CK62_MYXFH 
ID   F8CK62_MYXFH            Unreviewed;       529 AA.
AC   F8CK62;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Glucosyl hydrolase family protein {ECO:0000313|EMBL:AEI66438.1};
GN   OrderedLocusNames=LILAB_22715 {ECO:0000313|EMBL:AEI66438.1};
OS   Myxococcus fulvus (strain ATCC BAA-855 / HW-1).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=483219 {ECO:0000313|EMBL:AEI66438.1, ECO:0000313|Proteomes:UP000000488};
RN   [1] {ECO:0000313|EMBL:AEI66438.1, ECO:0000313|Proteomes:UP000000488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-855 / HW-1 {ECO:0000313|Proteomes:UP000000488};
RX   PubMed=21868801; DOI=10.1128/JB.05516-11;
RA   Li Z.F., Li X., Liu H., Liu X., Han K., Wu Z.H., Hu W., Li F.F., Li Y.Z.;
RT   "Genome sequence of the halotolerant marine bacterium Myxococcus fulvus HW-
RT   1.";
RL   J. Bacteriol. 193:5015-5016(2011).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 57 family.
CC       {ECO:0000256|ARBA:ARBA00006821, ECO:0000256|RuleBase:RU361196}.
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DR   EMBL; CP002830; AEI66438.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8CK62; -.
DR   STRING; 483219.LILAB_22715; -.
DR   KEGG; mfu:LILAB_22715; -.
DR   eggNOG; COG1543; Bacteria.
DR   HOGENOM; CLU_008192_1_0_7; -.
DR   Proteomes; UP000000488; Chromosome.
DR   GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030979; P:alpha-glucan biosynthetic process; IEA:InterPro.
DR   CDD; cd10792; GH57N_AmyC_like; 1.
DR   Gene3D; 1.20.1430.10; Families 57/38 glycoside transferase, middle domain; 1.
DR   Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR   InterPro; IPR037090; 57_glycoside_trans_central.
DR   InterPro; IPR015293; BE_C.
DR   InterPro; IPR040042; Branching_enz_MT3115-like.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR   InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR   InterPro; IPR004300; Glyco_hydro_57_N.
DR   PANTHER; PTHR41695; 1,4-ALPHA-GLUCAN BRANCHING ENZYME RV3031-RELATED; 1.
DR   PANTHER; PTHR41695:SF1; 1,4-ALPHA-GLUCAN BRANCHING ENZYME RV3031-RELATED; 1.
DR   Pfam; PF09210; BE_C; 1.
DR   Pfam; PF03065; Glyco_hydro_57; 1.
DR   SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361196};
KW   Hydrolase {ECO:0000313|EMBL:AEI66438.1}.
FT   DOMAIN          7..398
FT                   /note="Glycoside hydrolase family 57 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03065"
FT   DOMAIN          426..526
FT                   /note="1,4-alpha-glucan branching enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09210"
FT   ACT_SITE        190
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-1"
FT   ACT_SITE        352
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-1"
FT   BINDING         242
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT   BINDING         406
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT   BINDING         466
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
SQ   SEQUENCE   529 AA;  61410 MW;  0662F79ED076678B CRC64;
     MSLGSLALVL HAHLPFVRHP EHEDFLEEDW LYEAISETYL PLLQVFDALA EDGVPFRLAM
     TLSPTLVSML RDELLMSRYA RRLDLLCELG AREVHRTRDD ATFGPLAHFY RDHFESLRRA
     FHDRYRRDLV SAFRRLQDAG HLDILTCNAT HGFLPLMQQV PEAVRAQVTV AANHYRQHFG
     RDPAGIWLAE CGYYPGLERL LANERIRYFF VDTHGLTDAV PRPLHGPYAP VFTEAGVAAY
     ARDPESSQQV WSTEHGYPGD PDYREFYRDI GWDLDLDYIR PFIQPTGERK NTGFKYYRIT
     GKTNEKRPYD PRAARERAAV HAGNFLFNRQ RQIEDLASRL GGRAPVVVAP YDAELFGHWW
     FEGPQFLDFL IRKAAREQQT FRLVTPSDDL REHPENQVAT PPLSSWGAGG YATMWLDGSN
     DWIYRHLNQC AKQMVELARD FPDASELQRR ALNQAARELL LAQSSDWAFI MKTGTMVEYA
     QRRTREHILR FQRLHEQLRG GSLDERWLSQ VEGRDNLYPE LDYRLYLPA
//
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