FUMC2_PSEAE
ID FUMC2_PSEAE Reviewed; 458 AA.
AC Q51404; P72168;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Fumarate hydratase class II 2 {ECO:0000255|HAMAP-Rule:MF_00743};
DE Short=Fumarase C 2 {ECO:0000255|HAMAP-Rule:MF_00743};
DE EC=4.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:8806672};
DE AltName: Full=Aerobic fumarase 2 {ECO:0000255|HAMAP-Rule:MF_00743};
DE AltName: Full=Iron-independent fumarase 2 {ECO:0000255|HAMAP-Rule:MF_00743};
GN Name=fumC2 {ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000303|Ref.1};
GN OrderedLocusNames=PA4470;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FRD1;
RA Hassett D.J., Klotz M.G., Howell M.L.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP INDUCTION.
RC STRAIN=CHA;
RX PubMed=8806672; DOI=10.1006/bbrc.1996.1393;
RA Polack B., Dacheux D., Delic-Attree I., Toussaint B., Vignais P.M.;
RT "The Pseudomonas aeruginosa fumC and sodA genes belong to an iron-
RT responsive operon.";
RL Biochem. Biophys. Res. Commun. 226:555-560(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Involved in the TCA cycle. Catalyzes the stereospecific
CC interconversion of fumarate to L-malate. {ECO:0000255|HAMAP-
CC Rule:MF_00743, ECO:0000269|PubMed:8806672}.
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:0000255|HAMAP-Rule:MF_00743,
CC ECO:0000269|PubMed:8806672};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate
CC from fumarate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00743}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00743}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00743}.
CC -!- INDUCTION: Part of the fumC-PA4469-sodA operon which is repressed by
CC iron (at protein level). {ECO:0000269|PubMed:8806672}.
CC -!- MISCELLANEOUS: There are 2 substrate-binding sites: the catalytic A
CC site, and the non-catalytic B site that may play a role in the transfer
CC of substrate or product between the active site and the solvent.
CC Alternatively, the B site may bind allosteric effectors.
CC {ECO:0000255|HAMAP-Rule:MF_00743}.
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00743}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB17389.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U59458; AAB02830.1; -; Genomic_DNA.
DR EMBL; U72494; AAB17389.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE004091; AAG07858.1; -; Genomic_DNA.
DR PIR; F83088; F83088.
DR PIR; JC4982; JC4982.
DR RefSeq; NP_253160.1; NC_002516.2.
DR RefSeq; WP_003112741.1; NZ_QZGE01000004.1.
DR AlphaFoldDB; Q51404; -.
DR SMR; Q51404; -.
DR STRING; 287.DR97_1649; -.
DR PaxDb; Q51404; -.
DR PRIDE; Q51404; -.
DR EnsemblBacteria; AAG07858; AAG07858; PA4470.
DR GeneID; 881033; -.
DR KEGG; pae:PA4470; -.
DR PATRIC; fig|208964.12.peg.4680; -.
DR PseudoCAP; PA4470; -.
DR HOGENOM; CLU_021594_4_1_6; -.
DR InParanoid; Q51404; -.
DR OMA; RIATIWN; -.
DR PhylomeDB; Q51404; -.
DR BioCyc; PAER208964:G1FZ6-4559-MON; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro.
DR GO; GO:0004333; F:fumarate hydratase activity; IDA:PseudoCAP.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IDA:PseudoCAP.
DR GO; GO:0006106; P:fumarate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR CDD; cd01362; Fumarase_classII; 1.
DR Gene3D; 1.10.275.10; -; 1.
DR HAMAP; MF_00743; FumaraseC; 1.
DR InterPro; IPR005677; Fum_hydII.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR018951; Fumarase_C_C.
DR InterPro; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR PANTHER; PTHR11444; PTHR11444; 1.
DR Pfam; PF10415; FumaraseC_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; SSF48557; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lyase; Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..458
FT /note="Fumarate hydratase class II 2"
FT /id="PRO_0000161299"
FT ACT_SITE 182
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT ACT_SITE 312
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 98..100
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 123..126
FT /ligand="substrate"
FT /note="in site B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 133..135
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 318..320
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT SITE 325
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT CONFLICT 156
FT /note="P -> S (in Ref. 2; AAB17389)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="G -> A (in Ref. 2; AAB17389)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="A -> G (in Ref. 2; AAB17389)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="Missing (in Ref. 2; AAB17389)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="N -> T (in Ref. 2; AAB17389)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 458 AA; 48696 MW; 48D87C8B1C76B708 CRC64;
MTDTRIERDS MGELAVPATA LYGAQTQRAV NNFPVSGQRM PQAFVRALLL AKAAAARANV
SLQQLDAPMG EAIADTCLQL LQEDFMQHFP VDVFQTGSGT SSNMNANEVV ATLASRRLGG
KVNPNDHVNC GQSSNDIIPS TIHISAALEI SERLLPALRH LEQTIQSKAG EVHAYVKTGR
THLMDAMPVR MSQVLGGWAQ QVRQAGVHIE SVLPALQQLA QGGTAVGTGI NAHPRFAERF
SQELNDLTGL AFRPGDDFFA LIGSQDTAVA ASGQLKTLAV TLMKLANDLR WMNSGPLAGL
GEIELEALQP GSSIMPGKVN PVIPEATAMV AAQVIGNDAA IAVAGQSGNF ELNVMLPLVA
DNLLHSIQLL ANVSRLLADK AIASFKVNQG KLSEALARNP ILVTALNPII GYQKAAEIAK
QAYREGRPII DVALENTDLD RARLEVLLDP EKLTAGGL
