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Q81SA0

- FUMC_BACAN

UniProt

Q81SA0 - FUMC_BACAN

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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Bacillus anthracis
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the reversible addition of water to fumarate to give L-malate.By similarity

Catalytic activityi

(S)-malate = fumarate + H2O.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei186 – 1861Proton donor/acceptorBy similarity
Active sitei316 – 3161By similarity
Binding sitei317 – 3171SubstrateUniRule annotation
Sitei329 – 3291Important 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

BioCyciANTHRA:FUMC-MONOMER.
BANT260799:GJAJ-1708-MONOMER.
BANT261594:GJ7F-1779-MONOMER.
UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase class IIUniRule annotation (EC:4.2.1.2UniRule annotation)
Short name:
Fumarase CUniRule annotation
Gene namesi
Name:fumCUniRule annotation
Ordered Locus Names:BA_1767, GBAA_1767, BAS1637
OrganismiBacillus anthracis
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000000427: Chromosome, UP000000594: Chromosome, UP000005639: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

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 – 462462Fumarate hydratase class IIPRO_0000161252Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi198094.BA_1767.

Structurei

3D structure databases

ProteinModelPortaliQ81SA0.
SMRiQ81SA0. Positions 4-458.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 993Substrate bindingUniRule annotation
Regioni127 – 1304B siteUniRule annotation
Regioni137 – 1393Substrate bindingUniRule annotation
Regioni185 – 1862Substrate bindingUniRule annotation
Regioni322 – 3243Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
KOiK01679.
OMAiIAFNDNC.
OrthoDBiEOG6V1M4M.

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.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00979. fumC_II. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q81SA0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEYRIERDTL GEIKVPADKL WAAQTQRSKE NFPIGTEQMP LEIVKAFAIL
60 70 80 90 100
KKSAALSNQK LGKLSEEKAE AIVVAADEII AGKWNEHFPL VVWQTGSGTQ
110 120 130 140 150
SNMNVNEVIA NRGNQILKEK GSDVHIHPND DVNMSQSSND TFPTALHVAC
160 170 180 190 200
VLAVENHVLP AITKLKETLA EKVTAFEHII KIGRTHLQDA TPLTLGQEIS
210 220 230 240 250
GWHRMLEKTE RMIAESNTYM KELAIGGTAV GTGINAHPKF GEMVSEEISQ
260 270 280 290 300
FTGKQFISAP NKFHALTSHD EVVYTHGALK ALAADLMKIA NDVRWLASGP
310 320 330 340 350
RSGLGEIIIP ANEPGSSIMP GKVNPTQSEA LTMVVAQVMG NDATIGFAAS
360 370 380 390 400
QGNFELNVFK PVIAYNFLQS AHLLADAIVS FNDNCAVGIE ADEEIIKENV
410 420 430 440 450
NRSLMLVTAL NPHIGYENAA KIAKHAHKEG LTLKEAALQS GLLTEEQFNE
460
IVDPKKMIAP KE
Length:462
Mass (Da):50,345
Last modified:June 1, 2003 - v1
Checksum:i0FB897C31FAC981D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016879 Genomic DNA. Translation: AAP25681.1.
AE017334 Genomic DNA. Translation: AAT30883.1.
AE017225 Genomic DNA. Translation: AAT53954.1.
RefSeqiNP_844195.1. NC_003997.3.
WP_000456617.1. NZ_JHDR01000058.1.
YP_018408.1. NC_007530.2.
YP_027903.1. NC_005945.1.

Genome annotation databases

EnsemblBacteriaiAAP25681; AAP25681; BA_1767.
AAT30883; AAT30883; GBAA_1767.
AAT53954; AAT53954; BAS1637.
GeneIDi1086574.
2818045.
2851297.
KEGGiban:BA_1767.
bar:GBAA_1767.
bat:BAS1637.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016879 Genomic DNA. Translation: AAP25681.1 .
AE017334 Genomic DNA. Translation: AAT30883.1 .
AE017225 Genomic DNA. Translation: AAT53954.1 .
RefSeqi NP_844195.1. NC_003997.3.
WP_000456617.1. NZ_JHDR01000058.1.
YP_018408.1. NC_007530.2.
YP_027903.1. NC_005945.1.

3D structure databases

ProteinModelPortali Q81SA0.
SMRi Q81SA0. Positions 4-458.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 198094.BA_1767.

Protocols and materials databases

DNASUi 1086574.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAP25681 ; AAP25681 ; BA_1767 .
AAT30883 ; AAT30883 ; GBAA_1767 .
AAT53954 ; AAT53954 ; BAS1637 .
GeneIDi 1086574.
2818045.
2851297.
KEGGi ban:BA_1767.
bar:GBAA_1767.
bat:BAS1637.

Phylogenomic databases

eggNOGi COG0114.
HOGENOMi HOG000061736.
KOi K01679.
OMAi IAFNDNC.
OrthoDBi EOG6V1M4M.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci ANTHRA:FUMC-MONOMER.
BANT260799:GJAJ-1708-MONOMER.
BANT261594:GJ7F-1779-MONOMER.

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.
[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.
TIGRFAMsi TIGR00979. fumC_II. 1 hit.
PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
    Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J.
    , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
    Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames / isolate Porton.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames ancestor.
  3. "Complete genome sequence of Bacillus anthracis Sterne."
    Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sterne.

Entry informationi

Entry nameiFUMC_BACAN
AccessioniPrimary (citable) accession number: Q81SA0
Secondary accession number(s): Q6I0I3, Q6KUE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: October 29, 2014
This is version 87 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

Allosteric enzyme, Complete proteome, 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