FUMB_ECOLI
ID FUMB_ECOLI Reviewed; 548 AA.
AC P14407; P78139; Q2M6I2;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Fumarate hydratase class I, anaerobic {ECO:0000303|PubMed:3282546};
DE EC=4.2.1.2 {ECO:0000269|PubMed:23405168};
DE AltName: Full=D-tartrate dehydratase {ECO:0000303|PubMed:23405168};
DE EC=4.2.1.81 {ECO:0000269|PubMed:23405168};
DE AltName: Full=Fumarase B {ECO:0000303|PubMed:23405168};
GN Name=fumB {ECO:0000303|PubMed:2656658}; OrderedLocusNames=b4122, JW4083;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2656658; DOI=10.1128/jb.171.6.3494-3503.1989;
RA Bell P.J., Andrews S.C., Sivak M.N., Guest J.R.;
RT "Nucleotide sequence of the FNR-regulated fumarase gene (fumB) of
RT Escherichia coli K-12.";
RL J. Bacteriol. 171:3494-3503(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO 50.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP IDENTIFICATION OF THE STRUCTURAL GENE.
RX PubMed=3005475; DOI=10.1099/00221287-131-11-2971;
RA Guest J.R., Miles J.S., Roberts R.E., Woods S.A.;
RT "The fumarase genes of Escherichia coli: location of the fumB gene and
RT discovery of a new gene (fumC).";
RL J. Gen. Microbiol. 131:2971-2984(1985).
RN [6]
RP FUNCTION, AND INDUCTION.
RX DOI=10.1111/j.1574-6968.1987.tb02545.x;
RA Woods S.A., Guest J.R.;
RT "Differential roles of the Escherichia coli fumarases and fnr-dependent
RT expression of fumarase B and aspartase.";
RL FEMS Microbiol. Lett. 48:219-224(1987).
RN [7]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=3282546; DOI=10.1016/0167-4838(88)90050-7;
RA Woods S.A., Shwartzbach S.D., Guest J.R.;
RT "Two biochemically distinct classes of fumarase in Escherichia coli.";
RL Biochim. Biophys. Acta 954:14-26(1988).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-192, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17643228; DOI=10.1007/s00203-007-0279-9;
RA Kim O.B., Lux S., Unden G.;
RT "Anaerobic growth of Escherichia coli on D-tartrate depends on the fumarate
RT carrier DcuB and fumarase, rather than the L-tartrate carrier TtdT and L-
RT tartrate dehydratase.";
RL Arch. Microbiol. 188:583-589(2007).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=23405168; DOI=10.1371/journal.pone.0055549;
RA van Vugt-Lussenburg B.M., van der Weel L., Hagen W.R., Hagedoorn P.L.;
RT "Biochemical similarities and differences between the catalytic [4Fe-4S]
RT cluster containing fumarases FumA and FumB from Escherichia coli.";
RL PLoS ONE 8:E55549-E55549(2013).
CC -!- FUNCTION: Catalyzes the reversible hydration of fumarate to (S)-malate.
CC Functions in the generation of fumarate for use as an anaerobic
CC electron acceptor. To a lesser extent, also displays D-tartrate
CC dehydratase activity, but is not able to convert (R)-malate, L-tartrate
CC or meso-tartrate. Is required for anaerobic growth on D-tartrate.
CC {ECO:0000269|PubMed:17643228, ECO:0000269|PubMed:23405168,
CC ECO:0000269|PubMed:3282546, ECO:0000269|Ref.6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate = fumarate + H2O; Xref=Rhea:RHEA:12460,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15589, ChEBI:CHEBI:29806; EC=4.2.1.2;
CC Evidence={ECO:0000269|PubMed:23405168};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S,S)-tartrate = H2O + oxaloacetate; Xref=Rhea:RHEA:18289,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16452, ChEBI:CHEBI:30927; EC=4.2.1.81;
CC Evidence={ECO:0000269|PubMed:23405168};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:23405168};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:23405168};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=300 uM for (S)-malate {ECO:0000269|PubMed:23405168};
CC KM=320 uM for fumarate {ECO:0000269|PubMed:23405168};
CC KM=800 uM for D-tartrate {ECO:0000269|PubMed:23405168};
CC Vmax=490 umol/min/mg enzyme for (S)-malate dehydration
CC {ECO:0000269|PubMed:23405168};
CC Vmax=1430 umol/min/mg enzyme for fumarate hydration
CC {ECO:0000269|PubMed:23405168};
CC Vmax=9.2 umol/min/mg enzyme for D-tartrate dehydration
CC {ECO:0000269|PubMed:23405168};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23405168,
CC ECO:0000269|PubMed:3282546}.
CC -!- INDUCTION: Is mainly expressed during anaerobic growth. Is under the
CC control of the Fnr transcriptional regulator. {ECO:0000269|Ref.6}.
CC -!- DISRUPTION PHENOTYPE: Disruption of this gene seriously impairs growth
CC under anaerobic conditions on D-tartrate when glycerol is supplied as
CC an electron donor (D-tartrate fermentation). Cells lacking this gene
CC also lose most (about 79%) of D-tartrate dehydratase activity.
CC {ECO:0000269|PubMed:17643228}.
CC -!- SIMILARITY: Belongs to the class-I fumarase family. {ECO:0000305}.
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DR EMBL; M27058; AAA23827.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97022.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77083.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78124.1; -; Genomic_DNA.
DR PIR; A65222; B44511.
DR RefSeq; NP_418546.1; NC_000913.3.
DR RefSeq; WP_000066707.1; NZ_SSZK01000018.1.
DR AlphaFoldDB; P14407; -.
DR SMR; P14407; -.
DR BioGRID; 4262150; 11.
DR IntAct; P14407; 6.
DR STRING; 511145.b4122; -.
DR iPTMnet; P14407; -.
DR jPOST; P14407; -.
DR PaxDb; P14407; -.
DR PRIDE; P14407; -.
DR EnsemblBacteria; AAC77083; AAC77083; b4122.
DR EnsemblBacteria; BAE78124; BAE78124; BAE78124.
DR GeneID; 948642; -.
DR KEGG; ecj:JW4083; -.
DR KEGG; eco:b4122; -.
DR PATRIC; fig|1411691.4.peg.2578; -.
DR EchoBASE; EB0352; -.
DR eggNOG; COG1838; Bacteria.
DR eggNOG; COG1951; Bacteria.
DR HOGENOM; CLU_026758_0_0_6; -.
DR InParanoid; P14407; -.
DR OMA; SMYDEKN; -.
DR PhylomeDB; P14407; -.
DR BioCyc; EcoCyc:FUMB-MON; -.
DR BioCyc; MetaCyc:FUMB-MON; -.
DR BRENDA; 4.2.1.2; 2026.
DR BRENDA; 4.2.1.34; 2026.
DR SABIO-RK; P14407; -.
DR PRO; PR:P14407; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0047808; F:D(-)-tartrate dehydratase activity; IDA:EcoCyc.
DR GO; GO:0004333; F:fumarate hydratase activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; IEA:InterPro.
DR GO; GO:0044010; P:single-species biofilm formation; IMP:EcoCyc.
DR Gene3D; 3.20.130.10; -; 1.
DR InterPro; IPR004646; Fe-S_hydro-lyase_TtdA-typ_cat.
DR InterPro; IPR004647; Fe-S_hydro-lyase_TtdB-typ_cat.
DR InterPro; IPR036660; Fe-S_hydroAse_TtdB_cat_sf.
DR InterPro; IPR011167; Fe_dep_fumarate_hydratase.
DR InterPro; IPR020557; Fumarate_lyase_CS.
DR Pfam; PF05681; Fumerase; 1.
DR Pfam; PF05683; Fumerase_C; 1.
DR PIRSF; PIRSF001394; Fe_dep_fumar_hy; 1.
DR SUPFAM; SSF117457; SSF117457; 1.
DR TIGRFAMs; TIGR00722; ttdA_fumA_fumB; 1.
DR TIGRFAMs; TIGR00723; ttdB_fumA_fumB; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Acetylation; Iron; Iron-sulfur; Lyase; Metal-binding;
KW Reference proteome.
FT CHAIN 1..548
FT /note="Fumarate hydratase class I, anaerobic"
FT /id="PRO_0000195660"
FT BINDING 105
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:E9AE57"
FT BINDING 224
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:E9AE57"
FT BINDING 318
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:E9AE57"
FT MOD_RES 192
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT CONFLICT 50
FT /note="L -> V (in Ref. 1; AAA23827)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 60105 MW; 73685337862496B7 CRC64;
MSNKPFIYQA PFPMGKDNTE YYLLTSDYVS VADFDGETIL KVEPEALTLL AQQAFHDASF
MLRPAHQKQV AAILHDPEAS ENDKYVALQF LRNSEIAAKG VLPTCQDTGT AIIVGKKGQR
VWTGGGDEET LSKGVYNTYI EDNLRYSQNA ALDMYKEVNT GTNLPAQIDL YAVDGDEYKF
LCVAKGGGSA NKTYLYQETK ALLTPGKLKN FLVEKMRTLG TAACPPYHIA FVIGGTSAET
NLKTVKLASA HYYDELPTEG NEHGQAFRDV QLEQELLEEA QKLGLGAQFG GKYFAHDIRV
IRLPRHGASC PVGMGVSCSA DRNIKAKINR EGIWIEKLEH NPGQYIPQEL RQAGEGEAVK
VDLNRPMKEI LAQLSQYPVS TRLSLTGTII VGRDIAHAKL KELIDAGKEL PQYIKDHPIY
YAGPAKTPAG YPSGSLGPTT AGRMDSYVDL LQSHGGSMIM LAKGNRSQQV TDACHKHGGF
YLGSIGGPAA VLAQQSIKHL ECVAYPELGM EAIWKIEVED FPAFILVDDK GNDFFQQIVN
KQCANCTK
