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Database: UniProt/TrEMBL
Entry: D4H3E7_DENA2
LinkDB: D4H3E7_DENA2
Original site: D4H3E7_DENA2 
ID   D4H3E7_DENA2            Unreviewed;       525 AA.
AC   D4H3E7;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Glycoside hydrolase family 57 {ECO:0000313|EMBL:ADD67231.1};
GN   OrderedLocusNames=Dacet_0432 {ECO:0000313|EMBL:ADD67231.1};
OS   Denitrovibrio acetiphilus (strain DSM 12809 / NBRC 114555 / N2460).
OC   Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC   Geovibrionaceae; Denitrovibrio.
OX   NCBI_TaxID=522772 {ECO:0000313|EMBL:ADD67231.1, ECO:0000313|Proteomes:UP000002012};
RN   [1] {ECO:0000313|EMBL:ADD67231.1, ECO:0000313|Proteomes:UP000002012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12809 / NBRC 114555 / N2460
RC   {ECO:0000313|Proteomes:UP000002012};
RX   PubMed=21304711; DOI=10.4056/sigs.892105;
RA   Kiss H., Lang E., Lapidus A., Copeland A., Nolan M., Glavina Del Rio T.,
RA   Chen F., Lucas S., Tice H., Cheng J.F., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Brettin T.,
RA   Spring S., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Denitrovibrio acetiphilus type strain
RT   (N2460).";
RL   Stand. Genomic Sci. 2:270-279(2010).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 57 family.
CC       {ECO:0000256|ARBA:ARBA00006821, ECO:0000256|RuleBase:RU361196}.
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DR   EMBL; CP001968; ADD67231.1; -; Genomic_DNA.
DR   RefSeq; WP_013009775.1; NC_013943.1.
DR   AlphaFoldDB; D4H3E7; -.
DR   STRING; 522772.Dacet_0432; -.
DR   CAZy; GH57; Glycoside Hydrolase Family 57.
DR   PaxDb; 522772-Dacet_0432; -.
DR   KEGG; dap:Dacet_0432; -.
DR   eggNOG; COG1543; Bacteria.
DR   HOGENOM; CLU_008192_1_0_0; -.
DR   InParanoid; D4H3E7; -.
DR   OrthoDB; 9803279at2; -.
DR   Proteomes; UP000002012; 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:ADD67231.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002012}.
FT   DOMAIN          8..309
FT                   /note="Glycoside hydrolase family 57 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03065"
FT   DOMAIN          423..524
FT                   /note="1,4-alpha-glucan branching enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09210"
FT   ACT_SITE        189
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-1"
FT   ACT_SITE        350
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-1"
FT   BINDING         241
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT   BINDING         258
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT   BINDING         403
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   525 AA;  62040 MW;  87028D529F8BCDB3 CRC64;
     MSNGYWMLVL HSHLPFVKHP EYEYFLEEHW FYEAISETYI PILQYMKKME DEGINFRFAV
     SVTPPLAEMM SDGLLMERYE KHMDKMLALA DKEVERTKGT CFEHLAHMYK ERFQGIKDFY
     YGYLNRSLIS GYRHFLEKGY IDVITCGFTH GFLPLLNNTE NAVRAQVEMA VKSHEQKFGQ
     APKGIWLPEC AYFEGLDEIL AEYGIRYFFV DTHGVLYAKP RPKYGVYAPV YTQSGVAAFG
     RDYYSSKQVW SSKEGYPGDV SYRDFYRDIG YDLDHDYIKP YISPDGERVF TGFKYHRITG
     DSEYKEFYDN KVASAKTVDH AKHFVAEREK QLAEIAELID RKPVVVSPYD AELYGHWWFE
     GPEFLYNVFK EMDKSETIKS ITPLEYLNEY PTNQVVSVNP SSWGDKGYYD VWLNKGNDWI
     YRHLHFMSEK MVDMAKFHLS TKDDFKVRCL NQMARELFLA QSSDWAFLVT TGTAIDYAMQ
     RTKEHIHNFM RLRDMIDDGF KDWHFLEKLE NKNSIFPAMD FRIYC
//
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