FUMC_SACS2
ID FUMC_SACS2 Reviewed; 438 AA.
AC P39461;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Fumarate hydratase class II {ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000303|PubMed:8276121};
DE Short=Fumarase C {ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000303|PubMed:8276121};
DE EC=4.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:2124611};
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, ECO:0000303|PubMed:8276121};
GN OrderedLocusNames=SSO1077;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14, FUNCTION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DSM 5833 / MT-4;
RX PubMed=8276121; DOI=10.1016/0014-5793(94)80636-5;
RA Colombo S., Grisa M., Tortora P., Vanoni M.;
RT "Molecular cloning, nucleotide sequence and expression of a Sulfolobus
RT solfataricus gene encoding a class II fumarase.";
RL FEBS Lett. 337:93-98(1994).
RN [2]
RP ERRATUM OF PUBMED:8276121.
RX PubMed=8119400; DOI=10.1016/0014-5793(94)80192-4;
RA Colombo S., Grisa M., Tortora P., Vanoni M.;
RL FEBS Lett. 340:151-153(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 35091 / DSM 1616 / IFO 15331 / JCM 8930 / P1;
RX PubMed=2124611; DOI=10.1099/00221287-136-8-1537;
RA Puchegger S., Redl B., Stoeffler G.;
RT "Purification and properties of a thermostable fumarate hydratase from the
RT archaeobacterium Sulfolobus solfataricus.";
RL J. Gen. Microbiol. 136:1537-1541(1990).
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:2124611, ECO:0000269|PubMed:8276121}.
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:2124611};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.125 mM for malate (at pH 7.5 and at 70 degrees Celsius)
CC {ECO:0000269|PubMed:2124611};
CC KM=0.3 mM for malate (at pH 7.5 and at 70 degrees Celsius)
CC {ECO:0000269|PubMed:2124611};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:2124611};
CC Temperature dependence:
CC Optimum temperature is 85 degrees Celsius. At 95 degrees Celsius, the
CC enzyme activity is still 66% of maximum, whereas at 40 degrees
CC Celsius the enzyme is almost inactive. Thermostable.
CC {ECO:0000269|PubMed:2124611, ECO:0000269|PubMed:8276121};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate
CC from fumarate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00743,
CC ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00743,
CC ECO:0000269|PubMed:2124611}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00743,
CC ECO:0000305}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK41339.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X75402; CAA53156.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK41339.1; ALT_INIT; Genomic_DNA.
DR PIR; D90260; D90260.
DR PIR; S40448; S40448.
DR AlphaFoldDB; P39461; -.
DR SMR; P39461; -.
DR STRING; 273057.SSO1077; -.
DR EnsemblBacteria; AAK41339; AAK41339; SSO1077.
DR KEGG; sso:SSO1077; -.
DR PATRIC; fig|273057.12.peg.1077; -.
DR eggNOG; arCOG01749; Archaea.
DR HOGENOM; CLU_021594_4_1_2; -.
DR InParanoid; P39461; -.
DR OMA; HDSMGEV; -.
DR PhylomeDB; P39461; -.
DR BRENDA; 4.2.1.2; 6163.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro.
DR GO; GO:0004333; F:fumarate hydratase activity; IDA:UniProtKB.
DR GO; GO:0006106; P:fumarate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
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 InterPro; IPR001611; Leu-rich_rpt.
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.
DR PROSITE; PS51450; LRR; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Lyase; Reference proteome;
KW Tricarboxylic acid cycle.
FT CHAIN 1..438
FT /note="Fumarate hydratase class II"
FT /id="PRO_0000161334"
FT ACT_SITE 160
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT ACT_SITE 291
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 76..78
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 101..104
FT /ligand="substrate"
FT /note="in site B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 111..113
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 297..299
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT SITE 304
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
SQ SEQUENCE 438 AA; 47911 MW; 8D2A9CF37817EA6C CRC64;
MKYTDTAPKL FMNTGTKFPR RIIWSMGVLK KSCAKVNADL GLLDKKIADS IIKASDDLID
GKLDDKIVLD VFQTGSGTGL NMNVNEVIAE VASSYSNLKV HPNDHVNFGQ SSNDTVPTAI
RIAAVAEVTN RLLPALQQII SSLNKKAEEY KDVIKAGRTH LRDALPVTLG QELSAYADAF
QHEHEQVMNI LEYVKELPIG GTATGTGLNS HPEFQERVIN EINRITGLGF KPANRFRAMR
LLTDLLLLSG ALRNIAVDLY RLGQDIRLMF SGPLTGLNEI DLPTQEEIAG SSIMPGKTNP
VTVEATLLIS AQVVGLDHAN QFASMLGEFE LSMGIPLVGY NIVTQVNFIS EALEKMSRLV
IDGMVANVEK MKRYAESSPS LITIVSPVIG YDKATEIGKK LNKGMSIREA LRELGYSDNE
INKILDLSKL VKPGFTAK
