FRSA_VIBVU
ID FRSA_VIBVU Reviewed; 415 AA.
AC Q8DF91;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Esterase FrsA {ECO:0000255|HAMAP-Rule:MF_01063, ECO:0000305};
DE EC=3.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01063, ECO:0000269|PubMed:30951551};
GN Name=frsA {ECO:0000255|HAMAP-Rule:MF_01063, ECO:0000303|PubMed:21623357};
GN OrderedLocusNames=VV1_0328;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SHOWS THAT IS DOES NOT HAVE PYRUVATE DECARBOXYLASE ACTIVITY.
RX PubMed=23452154; DOI=10.1021/bi400093y;
RA Kellett W.F., Brunk E., Desai B.J., Fedorov A.A., Almo S.C., Gerlt J.A.,
RA Rothlisberger U., Richards N.G.;
RT "Computational, structural, and kinetic evidence that Vibrio vulnificus
RT FrsA is not a cofactor-independent pyruvate decarboxylase.";
RL Biochemistry 52:1842-1844(2013).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=30951551; DOI=10.1371/journal.pone.0215084;
RA Wang X., Li Z.M., Li Q., Shi M., Bao L., Xu D., Li Z.;
RT "Purification and biochemical characterization of FrsA protein from Vibrio
RT vulnificus as an esterase.";
RL PLoS ONE 14:E0215084-E0215084(2019).
RN [4] {ECO:0007744|PDB:3MVE, ECO:0007744|PDB:3OUR}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH
RP IIAGLC, PRELIMINARY FUNCTION, SUBUNIT, AND INTERACTION WITH IIAGLC.
RC STRAIN=MO6-24;
RX PubMed=21623357; DOI=10.1038/nchembio.589;
RA Lee K.J., Jeong C.S., An Y.J., Lee H.J., Park S.J., Seok Y.J., Kim P.,
RA Lee J.H., Lee K.H., Cha S.S.;
RT "FrsA functions as a cofactor-independent decarboxylase to control
RT metabolic flux.";
RL Nat. Chem. Biol. 7:434-436(2011).
CC -!- FUNCTION: Catalyzes the hydrolysis of esters (PubMed:30951551). In
CC vitro, prefers short chain alkanoate ester as substrate. Displays
CC highest activity towards p-nitrophenyl acetate (pNPA). Has weaker
CC activity towards p-nitrophenyl butyrate (pNPB) (PubMed:30951551).
CC {ECO:0000269|PubMed:30951551}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01063,
CC ECO:0000269|PubMed:30951551};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18.6 mM for pNPA {ECO:0000269|PubMed:30951551};
CC Note=kcat is 0.67 sec(-1) with pNPA as substrate.
CC {ECO:0000269|PubMed:30951551};
CC pH dependence:
CC Optimum pH is 9.0-9.5. {ECO:0000269|PubMed:30951551};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:30951551};
CC -!- SUBUNIT: Monomer in solution (PubMed:21623357). Homodimer
CC (PubMed:30951551). Forms a 1:1 complex with the unphosphorylated form
CC of the EIIA component of the glucose-specific PTS system (IIAGlc)
CC (PubMed:21623357). {ECO:0000269|PubMed:21623357,
CC ECO:0000269|PubMed:30951551}.
CC -!- SIMILARITY: Belongs to the FrsA family. {ECO:0000255|HAMAP-
CC Rule:MF_01063, ECO:0000305}.
CC -!- CAUTION: Was originally reported to catalyze the cofactor-independent
CC decarboxylation of pyruvate (PubMed:21623357). In contrast, Kellett et
CC al. demonstrated with computational, structural, and kinetic evidence
CC that this enzyme does not exhibit pyruvate decarboxylase activity
CC (PubMed:23452154). {ECO:0000269|PubMed:21623357,
CC ECO:0000269|PubMed:23452154}.
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DR EMBL; AE016795; AAO08857.1; -; Genomic_DNA.
DR RefSeq; WP_011078432.1; NC_004459.3.
DR PDB; 3MVE; X-ray; 2.20 A; A/B=1-415.
DR PDB; 3OUR; X-ray; 2.20 A; A/C/E/G=1-415.
DR PDBsum; 3MVE; -.
DR PDBsum; 3OUR; -.
DR AlphaFoldDB; Q8DF91; -.
DR SMR; Q8DF91; -.
DR ESTHER; vibvy-y856; Duf_1100-R.
DR EnsemblBacteria; AAO08857; AAO08857; VV1_0328.
DR KEGG; vvu:VV1_0328; -.
DR HOGENOM; CLU_036819_0_0_6; -.
DR OMA; NIPWVDH; -.
DR EvolutionaryTrace; Q8DF91; -.
DR Proteomes; UP000002275; Chromosome 1.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_01063; FrsA; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR043423; FrsA.
DR InterPro; IPR010520; FrsA-like.
DR Pfam; PF06500; FrsA-like; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Serine esterase.
FT CHAIN 1..415
FT /note="Esterase FrsA"
FT /id="PRO_0000197161"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:3MVE"
FT HELIX 31..44
FT /evidence="ECO:0007829|PDB:3MVE"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:3MVE"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:3MVE"
FT HELIX 64..76
FT /evidence="ECO:0007829|PDB:3MVE"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:3OUR"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:3MVE"
FT HELIX 98..113
FT /evidence="ECO:0007829|PDB:3MVE"
FT HELIX 118..136
FT /evidence="ECO:0007829|PDB:3MVE"
FT HELIX 144..163
FT /evidence="ECO:0007829|PDB:3MVE"
FT STRAND 165..174
FT /evidence="ECO:0007829|PDB:3MVE"
FT STRAND 176..187
FT /evidence="ECO:0007829|PDB:3MVE"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:3MVE"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:3MVE"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:3MVE"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:3MVE"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:3MVE"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:3MVE"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:3MVE"
FT HELIX 246..254
FT /evidence="ECO:0007829|PDB:3MVE"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:3MVE"
FT STRAND 261..271
FT /evidence="ECO:0007829|PDB:3MVE"
FT HELIX 273..284
FT /evidence="ECO:0007829|PDB:3MVE"
FT TURN 285..288
FT /evidence="ECO:0007829|PDB:3MVE"
FT STRAND 291..296
FT /evidence="ECO:0007829|PDB:3MVE"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:3MVE"
FT HELIX 306..309
FT /evidence="ECO:0007829|PDB:3MVE"
FT HELIX 314..323
FT /evidence="ECO:0007829|PDB:3MVE"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:3MVE"
FT HELIX 331..337
FT /evidence="ECO:0007829|PDB:3MVE"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:3MVE"
FT TURN 343..350
FT /evidence="ECO:0007829|PDB:3MVE"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:3MVE"
FT STRAND 358..363
FT /evidence="ECO:0007829|PDB:3MVE"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:3MVE"
FT HELIX 371..379
FT /evidence="ECO:0007829|PDB:3MVE"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:3MVE"
FT HELIX 394..413
FT /evidence="ECO:0007829|PDB:3MVE"
SQ SEQUENCE 415 AA; 47013 MW; DD57542CB1483B38 CRC64;
MSEEVSKNLS ETLFVKHKQA KETSALTQYM PTSQSLLDEI KEKNGFSWYR NLRRLQWVWQ
GVDPIEQEQV LARIASSKHS RTDEQWLDTV MGYHSGNWAY EWTRLGMEHQ KRAGEMTNEA
ASEALFSASL CYSIAGYPHL KSDNLAIQAQ VLANSAYLEA AKKSKYIIKQ LEIPFEKGKI
TAHLHLTNTD KPHPVVIVSA GLDSLQTDMW RLFRDHLAKH DIAMLTVDMP SVGYSSKYPL
TEDYSRLHQA VLNELFSIPY VDHHRVGLIG FRFGGNAMVR LSFLEQEKIK ACVILGAPIH
DIFASPQKLQ QMPKMYLDVL ASRLGKSVVD IYSLSGQMAA WSLKVQGFLS SRKTKVPILA
MSLEGDPVSP YSDNQMVAFF STYGKAKKIS SKTITQGYEQ SLDLAIKWLE DELLR
