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P39461

- FUMC_SULSO

UniProt

P39461 - FUMC_SULSO

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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

May function as an auxiliary aerobic enzyme in the citric acid cycle.1 Publication

Catalytic activityi

(S)-malate = fumarate + H2O.1 Publication

Kineticsi

  1. KM=0.125 mM for malate (at pH 7.5 and at 70 degrees Celsius)1 Publication
  2. KM=0.3 mM for malate (at pH 7.5 and at 70 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 8.0.1 Publication

Temperature dependencei

Optimum temperature is 85 degrees Celsius. Active from 40 to 90 degrees Celsius.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei160 – 1601Proton donor/acceptorBy similarity
Active sitei291 – 2911By similarity
Binding sitei292 – 2921SubstrateBy similarity
Sitei304 – 3041Important for catalytic activityBy similarity

GO - Molecular functioni

  1. fumarate hydratase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. fumarate metabolic process Source: InterPro
  2. tricarboxylic acid cycle Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciSSOL273057:GCH2-1024-MONOMER.
BRENDAi4.2.1.2. 6163.
UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase class II (EC:4.2.1.2)
Short name:
Fumarase C
Gene namesi
Name:fumC
Ordered Locus Names:SSO1077
OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifieri273057 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
ProteomesiUP000001974: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. tricarboxylic acid cycle enzyme complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 438438Fumarate hydratase class IIPRO_0000161334Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi273057.SSO1077.

Structurei

3D structure databases

ProteinModelPortaliP39461.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni76 – 783Substrate bindingBy similarity
Regioni101 – 1044B siteBy similarity
Regioni111 – 1133Substrate bindingBy similarity
Regioni159 – 1602Substrate bindingBy similarity
Regioni297 – 2993Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
InParanoidiP39461.
KOiK01679.
OMAiLEANEDH.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC.
InterProiIPR005677. Fum_hydII.
IPR024083. Fumarase/histidase_N.
IPR018951. Fumarase_C_C.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR001611. Leu-rich_rpt.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
PS51450. LRR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39461-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKYTDTAPKL FMNTGTKFPR RIIWSMGVLK KSCAKVNADL GLLDKKIADS
60 70 80 90 100
IIKASDDLID GKLDDKIVLD VFQTGSGTGL NMNVNEVIAE VASSYSNLKV
110 120 130 140 150
HPNDHVNFGQ SSNDTVPTAI RIAAVAEVTN RLLPALQQII SSLNKKAEEY
160 170 180 190 200
KDVIKAGRTH LRDALPVTLG QELSAYADAF QHEHEQVMNI LEYVKELPIG
210 220 230 240 250
GTATGTGLNS HPEFQERVIN EINRITGLGF KPANRFRAMR LLTDLLLLSG
260 270 280 290 300
ALRNIAVDLY RLGQDIRLMF SGPLTGLNEI DLPTQEEIAG SSIMPGKTNP
310 320 330 340 350
VTVEATLLIS AQVVGLDHAN QFASMLGEFE LSMGIPLVGY NIVTQVNFIS
360 370 380 390 400
EALEKMSRLV IDGMVANVEK MKRYAESSPS LITIVSPVIG YDKATEIGKK
410 420 430
LNKGMSIREA LRELGYSDNE INKILDLSKL VKPGFTAK
Length:438
Mass (Da):47,911
Last modified:February 1, 1995 - v1
Checksum:i8D2A9CF37817EA6C
GO

Sequence cautioni

The sequence AAK41339.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75402 Genomic DNA. Translation: CAA53156.1.
AE006641 Genomic DNA. Translation: AAK41339.1. Different initiation.
PIRiD90260.
S40448.
RefSeqiNP_342549.1. NC_002754.1.

Genome annotation databases

EnsemblBacteriaiAAK41339; AAK41339; SSO1077.
GeneIDi1454118.
KEGGisso:SSO1077.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75402 Genomic DNA. Translation: CAA53156.1 .
AE006641 Genomic DNA. Translation: AAK41339.1 . Different initiation.
PIRi D90260.
S40448.
RefSeqi NP_342549.1. NC_002754.1.

3D structure databases

ProteinModelPortali P39461.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 273057.SSO1077.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK41339 ; AAK41339 ; SSO1077 .
GeneIDi 1454118.
KEGGi sso:SSO1077.

Phylogenomic databases

eggNOGi COG0114.
HOGENOMi HOG000061736.
InParanoidi P39461.
KOi K01679.
OMAi LEANEDH.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci SSOL273057:GCH2-1024-MONOMER.
BRENDAi 4.2.1.2. 6163.

Family and domain databases

Gene3Di 1.10.275.10. 1 hit.
HAMAPi MF_00743. FumaraseC.
InterProi IPR005677. Fum_hydII.
IPR024083. Fumarase/histidase_N.
IPR018951. Fumarase_C_C.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR001611. Leu-rich_rpt.
[Graphical view ]
PANTHERi PTHR11444. PTHR11444. 1 hit.
Pfami PF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view ]
PRINTSi PR00149. FUMRATELYASE.
SUPFAMi SSF48557. SSF48557. 1 hit.
PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
PS51450. LRR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, nucleotide sequence and expression of a Sulfolobus solfataricus gene encoding a class II fumarase."
    Colombo S., Grisa M., Tortora P., Vanoni M.
    FEBS Lett. 337:93-98(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14.
    Strain: DSM 5833 / MT-4.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  3. "Purification and properties of a thermostable fumarate hydratase from the archaeobacterium Sulfolobus solfataricus."
    Puchegger S., Redl B., Stoeffler G.
    J. Gen. Microbiol. 136:1537-1541(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: ATCC 35091 / DSM 1616 / IFO 15331 / JCM 8930 / P1.

Entry informationi

Entry nameiFUMC_SULSO
AccessioniPrimary (citable) accession number: P39461
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: October 29, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

There are 2 substrate-binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors (By similarity).By similarity

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3