ID A7HLD6_FERNB Unreviewed; 533 AA.
AC A7HLD6;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=DUF1957 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=Fnod_0867 {ECO:0000313|EMBL:ABS60719.1};
OS Fervidobacterium nodosum (strain ATCC 35602 / DSM 5306 / Rt17-B1).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=381764 {ECO:0000313|EMBL:ABS60719.1, ECO:0000313|Proteomes:UP000002415};
RN [1] {ECO:0000313|EMBL:ABS60719.1, ECO:0000313|Proteomes:UP000002415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1
RC {ECO:0000313|Proteomes:UP000002415};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Fervidobacterium nodosum Rt17-B1.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABS60719.1, ECO:0000313|Proteomes:UP000002415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1
RC {ECO:0000313|Proteomes:UP000002415};
RX PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA Noll K.M.;
RT "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT the Thermotogales.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 57 family.
CC {ECO:0000256|ARBA:ARBA00006821, ECO:0000256|RuleBase:RU361196}.
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DR EMBL; CP000771; ABS60719.1; -; Genomic_DNA.
DR RefSeq; WP_011994035.1; NC_009718.1.
DR AlphaFoldDB; A7HLD6; -.
DR STRING; 381764.Fnod_0867; -.
DR CAZy; GH57; Glycoside Hydrolase Family 57.
DR KEGG; fno:Fnod_0867; -.
DR eggNOG; COG1543; Bacteria.
DR HOGENOM; CLU_008192_1_0_0; -.
DR OrthoDB; 9803279at2; -.
DR Proteomes; UP000002415; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002415}.
FT DOMAIN 7..301
FT /note="Glycoside hydrolase family 57 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03065"
FT DOMAIN 429..530
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 356
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 409
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT BINDING 470
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
SQ SEQUENCE 533 AA; 63298 MW; 49B035F73A6D4988 CRC64;
MPRGQIAFVL HAHLPYVHHP DYPFFLEEHW FFEAITETYI PLLRMFRELE KEKVPVKLTM
SITPPLMEMF ANPNLQNKYE KHIEKLIELA RKEVVRTEAE HPTKNKMAKF YLNFFEETLF
LFRDVYQRNI LNGFREYFSK GNLDIITCNA THGYLPFMEQ YPQAIRAQLE QAVKTYERHI
GVKPRGIWLA ECAYFPGLDK YLAEYGIEYF FVDSHALWYA DERPRYGVYR PVVTPNNVFA
FARDPESSEQ VWSAQIGYPG DSRYREFYRD IGFDREYEYI KPYIDPSGVR MNVGIKYHKI
TSKDTPLEKK DFYDIDEAKK VAYEHAKDFL RKKEAQVDYL LNLFEGLEPI IVAPFDAELF
GHWWFEGPYF IEYFMREAAK SQKLRAVRVC DVVDWIEKVQ IVTPAASSWG ANGYNEVWLN
GTNDWIYPHL HEMVEKMTEM AKLHTNETDP IKIRVLNQMV RELLLAQSSD WAFIMTTRTS
VEYAVNRTKT HIKRFLTLYE MLKSGNIDTG ELQRLEYLDD IFPDADYRMY LKI
//
