FUMA_SALTY
ID FUMA_SALTY Reviewed; 580 AA.
AC P40720;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 133.
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=STM1468;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
RC STRAIN=C5;
RX PubMed=1879695; DOI=10.1016/0378-1119(91)90406-2;
RA Collins L.V., Hackett J.;
RT "Sequence of the phosphomannose isomerase-encoding gene of Salmonella
RT typhimurium.";
RL Gene 103:135-136(1991).
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}.
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DR EMBL; AE006468; AAL20388.1; -; Genomic_DNA.
DR EMBL; X57117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_460429.2; NC_003197.2.
DR AlphaFoldDB; P40720; -.
DR SMR; P40720; -.
DR STRING; 99287.STM1468; -.
DR PaxDb; P40720; -.
DR EnsemblBacteria; AAL20388; AAL20388; STM1468.
DR GeneID; 1252986; -.
DR KEGG; stm:STM1468; -.
DR PATRIC; fig|99287.12.peg.1550; -.
DR HOGENOM; CLU_026758_0_0_6; -.
DR PhylomeDB; P40720; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000001014; 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 CHAIN 1..580
FT /note="Fumarate hydratase class I, aerobic"
FT /id="PRO_0000195659"
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 580 AA; 63825 MW; DF36C9E67D6FBE39 CRC64;
MSNKPFFYQD PFPLKKDDTE YYLLTSEHVS VAEFEGQEIL KVAPEALTLL ARQAFHDASF
MLRPAHQQQV ADILRDPQAS ENDKYVALQF LRNSDIAAKG VLPTCQDTGT AIIVGKKGQR
VWTGGGDEAA LARGVYNTYI EDNLRYSQNA ALDMYKEVNT GTNLPAQIDL YSVDGDEYKF
LCIAKGGGSA NKTYLYQETK ALLTPGKLKN YLVDKMRTLG TAACPPYHIA FVIGGTSAEA
NLKTVKLASA KYYDALPTEG NEHGQAFRDI ELEKELLLEA QNLGLGAQFG GKYFAHDIRV
IRLPRHGASC PVGMGVSCSA DRNIKAKINR DGIWIEKLER NPGKYIPEAL RQAGEGEAVR
VDLNRPMSEI LQQLSQYPVS TRLSLNGTII VGRDIAHAKL KERMDRGEGL PQYIKDHPIY
YAGPAKTPEG YASGSLGPTT AGRMDSYVDQ LQSQGGSMIM LAKGNRSQQV TDACKKHGGF
YLGSIGGPAA VLAQGSIKRL ECVEYPELGM EAIWKIEVED FPAFILVDDK GNDFFQQIQS
SQCGAALSNV AALRGGNMIR YFAGERRKRL IRSTPLCCYR
