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P28894

- FUMC1_BRADU

UniProt

P28894 - FUMC1_BRADU

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Protein

Fumarate hydratase class II 1

Gene

fumC1

Organism
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
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 sitei198 – 1981Proton donor/acceptorBy similarity
Active sitei328 – 3281By similarity
Binding sitei329 – 3291SubstrateUniRule annotation
Sitei341 – 3411Important 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

BioCyciBJAP224911:GJEJ-6569-MONOMER.
UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase class II 1UniRule annotation (EC:4.2.1.2UniRule annotation)
Short name:
Fumarase C 1UniRule annotation
Gene namesi
Name:fumC1UniRule annotation
Synonyms:fumC
Ordered Locus Names:blr6519
OrganismiBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Taxonomic identifieri224911 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium
ProteomesiUP000002526: 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 – 473473Fumarate hydratase class II 1PRO_0000161259Add
BLAST

Proteomic databases

PRIDEiP28894.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi224911.blr6519.

Structurei

3D structure databases

ProteinModelPortaliP28894.
SMRiP28894. Positions 15-472.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni108 – 1103Substrate bindingUniRule annotation
Regioni139 – 1424B siteUniRule annotation
Regioni149 – 1513Substrate bindingUniRule annotation
Regioni197 – 1982Substrate bindingUniRule annotation
Regioni334 – 3363Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
InParanoidiP28894.
KOiK01679.
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.

P28894-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKSARTKTA RPATRTETDS FGPIEVPSDR YWGAQTERSR QNFRIGTDRM
60 70 80 90 100
PISLVHALGI VKLAAAQSNR ELGLLDQRRA SAIIRAAREV IDGSLDDHFP
110 120 130 140 150
LVVWQTGSGT QTNMNLNEVI ANRANELLGG ELGAKKPVHP NDHVNMSQSS
160 170 180 190 200
NDSFPTAMHI AAASRITADL VPALGELLRA LRKKEKEFAK IVKIGRTHTQ
210 220 230 240 250
DATPLTLGQE FSGYAAQVES GIARLKVAVK ELYPLAQGGT AVGTGLNAKP
260 270 280 290 300
RFARLFAKHV AGITKLPFTS AANKFEALAS NDAYVLAHGA ISSVATGLFK
310 320 330 340 350
IANDIRLLGS GPRSGLGELI LPENEPGSSI MPGKVNPTQC EAMTMVCCQV
360 370 380 390 400
FGNHTAITVA GSQGHFELNV YKPVLAYNML HSIRLMADAA RSFTEHCVSG
410 420 430 440 450
IRADEKRISE LMQRSLMLVT ALAPKIGYDN AAKVAKTAHA NGTTLKEEAL
460 470
RLGFVTADEF DRLVQPEKMT KPG
Length:473
Mass (Da):50,924
Last modified:December 15, 2003 - v3
Checksum:iCDB35CFA32062957
GO

Sequence cautioni

The sequence AAA26211.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAC51784.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 944IDGS → STAD in AAA26211. (PubMed:1856685)Curated
Sequence conflicti91 – 944IDGS → STAD in AAA26212. (PubMed:1856685)Curated
Sequence conflicti220 – 2201S → R in AAA26211. (PubMed:1856685)Curated
Sequence conflicti220 – 2201S → R in AAA26212. (PubMed:1856685)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M79457 Genomic DNA. Translation: AAA26211.1. Different initiation.
M79457 Genomic DNA. Translation: AAA26212.1.
BA000040 Genomic DNA. Translation: BAC51784.1. Different initiation.
RefSeqiNP_773159.2. NC_004463.1.

Genome annotation databases

EnsemblBacteriaiBAC51784; BAC51784; BAC51784.
GeneIDi1054478.
KEGGibja:blr6519.
PATRICi21196868. VBIBraJap65052_6668.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M79457 Genomic DNA. Translation: AAA26211.1 . Different initiation.
M79457 Genomic DNA. Translation: AAA26212.1 .
BA000040 Genomic DNA. Translation: BAC51784.1 . Different initiation.
RefSeqi NP_773159.2. NC_004463.1.

3D structure databases

ProteinModelPortali P28894.
SMRi P28894. Positions 15-472.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224911.blr6519.

Proteomic databases

PRIDEi P28894.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC51784 ; BAC51784 ; BAC51784 .
GeneIDi 1054478.
KEGGi bja:blr6519.
PATRICi 21196868. VBIBraJap65052_6668.

Phylogenomic databases

eggNOGi COG0114.
HOGENOMi HOG000061736.
InParanoidi P28894.
KOi K01679.
OrthoDBi EOG6V1M4M.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci BJAP224911:GJEJ-6569-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

« Hide 'large scale' publications
  1. "Cloning, sequencing, and mutational analysis of the Bradyrhizobium japonicum fumC-like gene: evidence for the existence of two different fumarases."
    Acuna G., Ebeling S., Hennecke H.
    J. Gen. Microbiol. 137:991-1000(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: USDA 110spc4.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110.

Entry informationi

Entry nameiFUMC1_BRADU
AccessioniPrimary (citable) accession number: P28894
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 15, 2003
Last modified: October 29, 2014
This is version 104 of the entry and version 3 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