FUMA_ECO57
ID FUMA_ECO57 Reviewed; 548 AA.
AC Q8X4P8; Q7ADM1;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Fumarate hydratase class I, aerobic {ECO:0000250|UniProtKB:P0AC33};
DE EC=4.2.1.2 {ECO:0000250|UniProtKB:P0AC33};
DE AltName: Full=Fumarase A {ECO:0000250|UniProtKB:P0AC33};
DE AltName: Full=Oxaloacetate keto--enol-isomerase {ECO:0000250|UniProtKB:P0AC33};
DE Short=OAAKE isomerase {ECO:0000250|UniProtKB:P0AC33};
DE AltName: Full=Oxaloacetate tautomerase {ECO:0000250|UniProtKB:P0AC33};
DE EC=5.3.2.2 {ECO:0000250|UniProtKB:P0AC33};
GN Name=fumA {ECO:0000250|UniProtKB:P0AC33}; OrderedLocusNames=Z2615, ECs2318;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Catalyzes the reversible hydration of fumarate to (S)-malate.
CC Functions as an aerobic enzyme in the direction of malate formation as
CC part of the citric acid cycle. Accounts for about 80% of the fumarase
CC activity when the bacteria grow aerobically. To a lesser extent, also
CC displays D-tartrate dehydratase activity in vitro, but is not able to
CC convert (R)-malate, L-tartrate or meso-tartrate. Can also catalyze the
CC isomerization of enol- to keto-oxaloacetate.
CC {ECO:0000250|UniProtKB:P0AC33}.
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:0000250|UniProtKB:P0AC33};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=oxaloacetate = enol-oxaloacetate; Xref=Rhea:RHEA:16021,
CC ChEBI:CHEBI:16452, ChEBI:CHEBI:17479; EC=5.3.2.2;
CC Evidence={ECO:0000250|UniProtKB:P0AC33};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P0AC33};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:P0AC33};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate
CC from fumarate: step 1/1. {ECO:0000250|UniProtKB:P0AC33}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0AC33}.
CC -!- INDUCTION: Is expressed under aerobic conditions. Is repressed by
CC glucose and anaerobiosis. {ECO:0000250|UniProtKB:P0AC33}.
CC -!- SIMILARITY: Belongs to the class-I fumarase family. {ECO:0000305}.
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; AE005174; AAG56599.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB35741.1; -; Genomic_DNA.
DR PIR; C85767; C85767.
DR PIR; F90918; F90918.
DR RefSeq; NP_310345.1; NC_002695.1.
DR RefSeq; WP_000066619.1; NZ_SWKA01000004.1.
DR AlphaFoldDB; Q8X4P8; -.
DR SMR; Q8X4P8; -.
DR STRING; 155864.EDL933_2564; -.
DR EnsemblBacteria; AAG56599; AAG56599; Z2615.
DR EnsemblBacteria; BAB35741; BAB35741; ECs_2318.
DR GeneID; 916929; -.
DR KEGG; ece:Z2615; -.
DR KEGG; ecs:ECs_2318; -.
DR PATRIC; fig|386585.9.peg.2428; -.
DR eggNOG; COG1838; Bacteria.
DR eggNOG; COG1951; Bacteria.
DR HOGENOM; CLU_026758_0_0_6; -.
DR OMA; AGVLPMC; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004333; F:fumarate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050163; F:oxaloacetate tautomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Isomerase; Lyase; Metal-binding;
KW Reference proteome; Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P0AC33"
FT CHAIN 2..548
FT /note="Fumarate hydratase class I, aerobic"
FT /id="PRO_0000195657"
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"
SQ SEQUENCE 548 AA; 60298 MW; F26C7AA07630563F CRC64;
MSNKPFHYQA PFPLKKDDTE YYLLTSEHVS LSEFEGQEIL KVAPEALTLL ARQAFHDASF
MLRPAHQQQV ADILRDPEAS ENDKYVALQF LRNSDIAAKG VLPTCQDTGT AIIVGKKGQR
VWTGGGDEAA LARGVYNTYI EDNLRYSQNA PLDMYKEVNT GTNLPAQIDL YAVDGDEYKF
LCIAKGGGSA NKTYLYQETK ALLTPGKLKN YLVEKMRTLG TAACPPYHIA FVIGGTSAET
NLKTVKLASA KYYDELPTEG NEHGQAFRDV ELEKELLIEA QNLGLGAQFG GKYFAHDIRV
IRLPRHGASC PVGMGVSCSA DRNIKAKINR QGIWIEKLEH NPGKYIPEEL RKAGEGEAVR
VDLNRPMKEI LAQLSQYPVS TRLSLNGTII VGRDIAHAKL KERMDNGEGL PQYIKDHPIY
YAGPAKTPEG YASGSLGPTT AGRMDSYVDQ LQALGGSMIM LAKGNRSQQV TDACKKHGGF
YLGSIGGPAA VLAQGSIKSL ECVEYPELGM EAIWKIEVED FPAFILVDDK GNDFFQQIQL
TQCTRCVK
