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Database: UniProt
Entry: Q31AG0_PROM9
LinkDB: Q31AG0_PROM9
Original site: Q31AG0_PROM9 
ID   Q31AG0_PROM9            Unreviewed;       527 AA.
AC   Q31AG0;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=(1->4)-alpha-D-glucan branching enzyme {ECO:0000313|EMBL:ABB50135.1};
GN   OrderedLocusNames=PMT9312_1076 {ECO:0000313|EMBL:ABB50135.1};
OS   Prochlorococcus marinus (strain MIT 9312).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=74546 {ECO:0000313|EMBL:ABB50135.1, ECO:0000313|Proteomes:UP000002715};
RN   [1] {ECO:0000313|Proteomes:UP000002715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9312 {ECO:0000313|Proteomes:UP000002715};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 57 family.
CC       {ECO:0000256|ARBA:ARBA00006821, ECO:0000256|RuleBase:RU361196}.
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DR   EMBL; CP000111; ABB50135.1; -; Genomic_DNA.
DR   RefSeq; WP_011376626.1; NC_007577.1.
DR   AlphaFoldDB; Q31AG0; -.
DR   STRING; 74546.PMT9312_1076; -.
DR   CAZy; GH57; Glycoside Hydrolase Family 57.
DR   KEGG; pmi:PMT9312_1076; -.
DR   eggNOG; COG1543; Bacteria.
DR   HOGENOM; CLU_008192_1_0_3; -.
DR   OrthoDB; 9803279at2; -.
DR   Proteomes; UP000002715; Chromosome.
DR   GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:InterPro.
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}.
FT   DOMAIN          15..389
FT                   /note="Glycoside hydrolase family 57 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03065"
FT   DOMAIN          426..525
FT                   /note="1,4-alpha-glucan branching enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09210"
FT   ACT_SITE        191
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-1"
FT   ACT_SITE        353
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-1"
FT   BINDING         243
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT   BINDING         260
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT   BINDING         405
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT   BINDING         464
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
SQ   SEQUENCE   527 AA;  60817 MW;  98CEB07CA7FA5E00 CRC64;
     MNGQYPKKNV LGQLAIVLHA HLPYVRKNER NSLEEDWLFQ AILECYIPLL QSIESSKNEN
     PLNTKLTISL SPTLLSLLDN KQIQETFPSW IETRNDFLNE LPQKEKNASA FLIKNLNDKY
     LYWQKCSGNL IEKFRVLSIS GNLDILTCAA THGYLPILRE NPETVKGQIN TAIRSHENIF
     GIKPLGIWLP ECAYYENLDE ILFNSGIRYA ILDGHGILNS TPRPRYGVYA PICSKKGVAF
     FGRDSESTLP VWSAKDGFPG DKVYREFHKD LGWELPIFKL QKKGISTKRP LGLKFHKITD
     ENVPLGEKEF YLENEAKKKA SEHADAYLLE RSKQLEKLTL SSSFKPLLVA PFDAELFGHW
     WYEGPFFIEN ILKNSSKYSI KLTNLKEFLL QKPNLQICDP SSSSWGQGGY HNYWINDANA
     WIVPEITKAG STFVDLCSKN FNNELSLRLF KQAARELLLS ESSDWSFILR AGTTTKLAKE
     RIERHLFRFW KLVEMIKNHS NINLKFLEDI EEEDKVFPDI NINDWRK
//
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