ID E0RVY7_BUTPB Unreviewed; 376 AA. AC E0RVY7; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAR-2024, entry version 64. DE SubName: Full=Acetyl-xylan esterase Est2A {ECO:0000313|EMBL:ADL35669.1}; GN Name=est2A {ECO:0000313|EMBL:ADL35669.1}; GN OrderedLocusNames=bpr_I2939 {ECO:0000313|EMBL:ADL35669.1}; OS Butyrivibrio proteoclasticus (strain ATCC 51982 / DSM 14932 / B316) OS (Clostridium proteoclasticum). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; OC Butyrivibrio. OX NCBI_TaxID=515622 {ECO:0000313|EMBL:ADL35669.1, ECO:0000313|Proteomes:UP000001299}; RN [1] {ECO:0000313|EMBL:ADL35669.1, ECO:0000313|Proteomes:UP000001299} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51982 / DSM 14932 / B316 RC {ECO:0000313|Proteomes:UP000001299}; RX PubMed=20689770; DOI=10.1371/journal.pone.0011942; RA Kelly W.J., Leahy S.C., Altermann E., Yeoman C.J., Dunne J.C., Kong Z., RA Pacheco D.M., Li D., Noel S.J., Moon C.D., Cookson A.L., Attwood G.T.; RT "The glycobiome of the rumen bacterium Butyrivibrio proteoclasticus B316(T) RT highlights adaptation to a polysaccharide-rich environment."; RL PLoS ONE 5:E11942-E11942(2010). RN [2] {ECO:0007829|PDB:3U37, ECO:0007829|PDB:4DEV} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS). RX PubMed=23345031; DOI=10.1002/prot.24254; RA Till M., Goldstone D.C., Attwood G.T., Moon C.D., Kelly W.J., Arcus V.L.; RT "Structure and function of an acetyl xylan esterase (Est2A) from the rumen RT bacterium Butyrivibrio proteoclasticus."; RL Proteins 81:911-917(2013). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001810; ADL35669.1; -; Genomic_DNA. DR PDB; 3U37; X-ray; 2.10 A; A/B/C/D/E/F/G/H=1-376. DR PDB; 4DEV; X-ray; 2.00 A; A/B/C/D/E/F/G/H=1-376. DR PDBsum; 3U37; -. DR PDBsum; 4DEV; -. DR AlphaFoldDB; E0RVY7; -. DR SMR; E0RVY7; -. DR STRING; 515622.bpr_I2939; -. DR KEGG; bpb:bpr_I2939; -. DR eggNOG; COG2755; Bacteria. DR HOGENOM; CLU_042506_0_0_9; -. DR BRENDA; 3.1.1.72; 9372. DR Proteomes; UP000001299; Chromosome 1. DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:InterPro. DR CDD; cd01831; Endoglucanase_E_like; 1. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR Gene3D; 3.40.50.1110; SGNH hydrolase; 1. DR InterPro; IPR037461; CtCE2-like_dom. DR InterPro; IPR001087; GDSL. DR InterPro; IPR036514; SGNH_hydro_sf. DR PANTHER; PTHR37834; GDSL-LIKE LIPASE/ACYLHYDROLASE DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_2G00620); 1. DR PANTHER; PTHR37834:SF2; PUTATIVE-RELATED; 1. DR Pfam; PF00657; Lipase_GDSL; 1. DR SUPFAM; SSF52266; SGNH hydrolase; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:3U37, ECO:0007829|PDB:4DEV}; KW Reference proteome {ECO:0000313|Proteomes:UP000001299}. SQ SEQUENCE 376 AA; 42446 MW; F3EEE4CF3959E189 CRC64; MSVLQYTEIS NISSDKINIL GRTGKKRQPL PVFFNGGGVE VVVTGSELWI DLETDSDVNE MWVALEINGA FIARQMLLPG EHSLCLFRSM EKTTPKRVRL YRELQAMNDD PKVKLLFKGF KHDGEFQNVP VYSRKLEFIG DSITSGEGSY GAFDDVDWIP MYMSASANYA TMTAKALNAD YHLVSQGGWG VFCGWDNDVR HNLPSVYEKV CGLAKGEMNE ELGAQEEYDF ASWQPDAIIV NLGTNDVTSF NQPEFLNPDD GKTYKMRTNT DGTRNREDEL KIVSAIIDFL TMLRKHNPNA QIIWSYGMLG SDLNLVITEG INKYKENAGD EKVSFFQLPN TTMENFGSHM HPGPKSHQNA AKELVDYLRN KLGWFE //