FUMC_RICPR
ID FUMC_RICPR Reviewed; 461 AA.
AC Q9ZCQ4;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Fumarate hydratase class II {ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000303|PubMed:21904061};
DE Short=Fumarase C {ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000303|PubMed:21904061};
DE EC=4.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00743};
DE AltName: Full=Aerobic fumarase {ECO:0000255|HAMAP-Rule:MF_00743};
DE AltName: Full=Iron-independent fumarase {ECO:0000255|HAMAP-Rule:MF_00743};
GN Name=fumC {ECO:0000255|HAMAP-Rule:MF_00743}; OrderedLocusNames=RP665;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP AND SUBUNIT.
RX PubMed=21904061; DOI=10.1107/s174430911102690x;
RA Phan I., Subramanian S., Olsen C., Edwards T.E., Guo W., Zhang Y.,
RA Van Voorhis W.C., Stewart L.J., Myler P.J.;
RT "Structure of fumarate hydratase from Rickettsia prowazekii, the agent of
RT typhus and suspected relative of the mitochondria.";
RL Acta Crystallogr. F 67:1123-1128(2011).
CC -!- FUNCTION: Involved in the TCA cycle. Catalyzes the stereospecific
CC interconversion of fumarate to L-malate. {ECO:0000255|HAMAP-
CC Rule:MF_00743}.
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 -!- 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 ECO:0000269|PubMed:21904061}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00743}.
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, ECO:0000305}.
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DR EMBL; AJ235272; CAA15103.1; -; Genomic_DNA.
DR PIR; E71672; E71672.
DR RefSeq; NP_221027.1; NC_000963.1.
DR RefSeq; WP_004596191.1; NC_000963.1.
DR PDB; 3GTD; X-ray; 2.40 A; A/B=1-461.
DR PDBsum; 3GTD; -.
DR AlphaFoldDB; Q9ZCQ4; -.
DR SMR; Q9ZCQ4; -.
DR STRING; 272947.RP665; -.
DR EnsemblBacteria; CAA15103; CAA15103; CAA15103.
DR GeneID; 57569790; -.
DR KEGG; rpr:RP665; -.
DR PATRIC; fig|272947.5.peg.685; -.
DR eggNOG; COG0114; Bacteria.
DR HOGENOM; CLU_021594_4_1_5; -.
DR OMA; HDSMGEV; -.
DR BRENDA; 4.2.1.2; 5447.
DR UniPathway; UPA00223; UER01007.
DR EvolutionaryTrace; Q9ZCQ4; -.
DR Proteomes; UP000002480; Chromosome.
DR GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro.
DR GO; GO:0004333; F:fumarate hydratase activity; IEA:UniProtKB-UniRule.
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 TIGRFAMs; TIGR00979; fumC_II; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lyase; Reference proteome;
KW Tricarboxylic acid cycle.
FT CHAIN 1..461
FT /note="Fumarate hydratase class II"
FT /id="PRO_0000161307"
FT ACT_SITE 188
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT ACT_SITE 318
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 98..100
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743,
FT ECO:0000269|PubMed:21904061, ECO:0007744|PDB:3GTD"
FT BINDING 129..132
FT /ligand="substrate"
FT /note="in site B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 139..141
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743,
FT ECO:0000305|PubMed:21904061, ECO:0007744|PDB:3GTD"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 324..326
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743,
FT ECO:0000269|PubMed:21904061, ECO:0007744|PDB:3GTD"
FT SITE 331
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:3GTD"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:3GTD"
FT HELIX 24..32
FT /evidence="ECO:0007829|PDB:3GTD"
FT HELIX 42..61
FT /evidence="ECO:0007829|PDB:3GTD"
FT HELIX 67..82
FT /evidence="ECO:0007829|PDB:3GTD"
FT TURN 83..87
FT /evidence="ECO:0007829|PDB:3GTD"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:3GTD"
FT HELIX 100..119
FT /evidence="ECO:0007829|PDB:3GTD"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:3GTD"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:3GTD"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:3GTD"
FT HELIX 140..158
FT /evidence="ECO:0007829|PDB:3GTD"
FT HELIX 160..175
FT /evidence="ECO:0007829|PDB:3GTD"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:3GTD"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:3GTD"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:3GTD"
FT HELIX 197..219
FT /evidence="ECO:0007829|PDB:3GTD"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:3GTD"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:3GTD"
FT HELIX 242..254
FT /evidence="ECO:0007829|PDB:3GTD"
FT HELIX 264..269
FT /evidence="ECO:0007829|PDB:3GTD"
FT HELIX 272..298
FT /evidence="ECO:0007829|PDB:3GTD"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:3GTD"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:3GTD"
FT HELIX 328..351
FT /evidence="ECO:0007829|PDB:3GTD"
FT HELIX 362..386
FT /evidence="ECO:0007829|PDB:3GTD"
FT TURN 387..390
FT /evidence="ECO:0007829|PDB:3GTD"
FT HELIX 395..404
FT /evidence="ECO:0007829|PDB:3GTD"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:3GTD"
FT HELIX 409..416
FT /evidence="ECO:0007829|PDB:3GTD"
FT HELIX 418..431
FT /evidence="ECO:0007829|PDB:3GTD"
FT HELIX 435..441
FT /evidence="ECO:0007829|PDB:3GTD"
FT HELIX 447..454
FT /evidence="ECO:0007829|PDB:3GTD"
SQ SEQUENCE 461 AA; 51008 MW; C9929CC94E7E617D CRC64;
MKNYRIESDS FGEIQIEEKF YWGAQTQRSL NNFKISKQKM PKILIRALAI LKKCAAQVNY
EFGDLEYKIA TSIDKAIDRI LAGEFEDNFP LVVWQTGSGT QTNMNMNEVI ASIANEELTG
KKGGKFPVHP NDHVNKGQSS NDSFPTAMHI ATVLATKQQL IPALNNLLTY LQDKSKDWDK
IIKIGRTHLQ DATPLTLKQE FSGYITQIEY ALERIEDALK KVYLLAQGGT AVGTGINSKI
GFDIKFAQKV AEFTQQPFKT APNKFESLAA HDALVEFSGT LNTIAVSLMK IANDIRLLGS
GPRCGLGELH LPENEPGSSI MPGKVNPTQV EALTMVCTQV MGNHVTVTIA GSNGHLELNV
FKPVIIYNIL QSIELLSDSV NSFVTHCVKG LEPNIARINT LRDKSLMLVT VLNPHIGYDN
AAKIAKEAHK YGITLKEAAK KLNFLSEEEF DKIVVPEKMI S
