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Q9A6I5

- FUMC_CAUCR

UniProt

Q9A6I5 - FUMC_CAUCR

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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Caulobacter crescentus (strain ATCC 19089 / CB15)
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 sitei188 – 1881Proton donor/acceptorBy similarity
Active sitei318 – 3181By similarity
Binding sitei319 – 3191SubstrateUniRule annotation
Sitei331 – 3311Important 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

BioCyciCAULO:CC2109-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:CC_2109
OrganismiCaulobacter crescentus (strain ATCC 19089 / CB15)
Taxonomic identifieri190650 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter
ProteomesiUP000001816: 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 – 463463Fumarate hydratase class IIPRO_0000161265Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ9A6I5.
SMRiQ9A6I5. Positions 3-462.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 1003Substrate bindingUniRule annotation
Regioni129 – 1324B siteUniRule annotation
Regioni139 – 1413Substrate bindingUniRule annotation
Regioni187 – 1882Substrate bindingUniRule annotation
Regioni324 – 3263Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
KOiK01679.
OMAiMESFNIH.
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.

Q9A6I5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTATRIETDT FGPIEVAADR YWGAQAQRSL GNFKIGWEKQ PLPVVRALGI
60 70 80 90 100
VKRAAAEANL ALGKLDPKIA ETIIAAANEV IEGKLNDHFP LVVWQTGSGT
110 120 130 140 150
QSNMNANEVI SNRAIEMLGG EMGSKKPVHP NDHVNMSQSS NDTFPTAMHI
160 170 180 190 200
ACAEQVVHDL LPALKHLHKA LAAKAAEWKD IIKIGRTHTQ DATPLTLGQE
210 220 230 240 250
FGGYAQQIEN GIARIEMTLP MLMQLAQGGT AVGTGLNAPV GFAELVAEQI
260 270 280 290 300
AGITGLGFTT APNKFEALAA HDAMVFTHGA INTVAASLFK IANDIRFLGS
310 320 330 340 350
GPRAGLGELS LPENEPGSSI MPGKVNPTQS EALTQVCAQV FGNHSTLTFA
360 370 380 390 400
GSQGHFELNV FNPVMAYNFL QSVRLVADAA ISFTDNCVVG IEPRVDNIKK
410 420 430 440 450
GVENSLMLVT ALNGKLGYDA CAKIAKTAHK NGTTLREEAV GGGYLTNEEF
460
EQYVRPEKMI SPG
Length:463
Mass (Da):49,344
Last modified:June 1, 2001 - v1
Checksum:i05A0286393EFE301
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005673 Genomic DNA. Translation: AAK24080.1.
PIRiD87510.
RefSeqiNP_420912.1. NC_002696.2.

Genome annotation databases

EnsemblBacteriaiAAK24080; AAK24080; CC_2109.
GeneIDi943033.
KEGGiccr:CC_2109.
PATRICi21301238. VBICauCre124313_2130.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005673 Genomic DNA. Translation: AAK24080.1 .
PIRi D87510.
RefSeqi NP_420912.1. NC_002696.2.

3D structure databases

ProteinModelPortali Q9A6I5.
SMRi Q9A6I5. Positions 3-462.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK24080 ; AAK24080 ; CC_2109 .
GeneIDi 943033.
KEGGi ccr:CC_2109.
PATRICi 21301238. VBICauCre124313_2130.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci CAULO:CC2109-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 19089 / CB15.

Entry informationi

Entry nameiFUMC_CAUCR
AccessioniPrimary (citable) accession number: Q9A6I5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2001
Last modified: October 1, 2014
This is version 83 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