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Q87DC2

- FUMC_XYLFT

UniProt

Q87DC2 - FUMC_XYLFT

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Protein

Fumarate hydratase class II

Gene
fumC, PD_0763
Organism
Xylella fastidiosa (strain Temecula1 / ATCC 700964)
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.UniRule annotation

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei189 – 1891Proton donor/acceptor By similarity
Active sitei319 – 3191 By similarity
Binding sitei320 – 3201Substrate By similarity
Sitei332 – 3321Important for catalytic activity By 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

BioCyciXFAS183190:GIX4-763-MONOMER.
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:PD_0763
OrganismiXylella fastidiosa (strain Temecula1 / ATCC 700964)
Taxonomic identifieri183190 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXylella
ProteomesiUP000002516: Chromosome

Subcellular locationi

Cytoplasm By similarity 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 – 473473Fumarate hydratase class IIUniRule annotationPRO_0000161330Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi183190.PD0763.

Structurei

3D structure databases

ProteinModelPortaliQ87DC2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni105 – 1073Substrate binding By similarity
Regioni130 – 1334B site By similarity
Regioni140 – 1423Substrate binding By similarity
Regioni188 – 1892Substrate binding By similarity
Regioni325 – 3273Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0114.
KOiK01679.
OMAiMFSGPMT.
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.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q87DC2-1 [UniParc]FASTAAdd to Basket

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MEMQMSNSDR YRIEHDSMGD LRVPIDALWG AQTQRAIENF PISGRSMPQG    50
FIHALGFIKA AAAKVNAELG LLPKSMAKEI EAAALDVAAG RYDAEFPVDI 100
YQTGSGTSSN MNANEVIATL AMRATKGPIH PNDHVNLGQS SNDVVPTAIR 150
ISATLAVQGR LLPALKHLRK MINKRARGLG SVVKTGRTHL MDAMPLTFAQ 200
EFGAWSAQIV SAEARLNDTL KRLHRLPLGG TAIGTGINTD PHFGRNAVKV 250
LSALTGIHFE SANNKFEGLA AQDDLVELSG QFNTLAVALM KIANDLRWMN 300
AGPLAGLGEI ELPALQPGSS IMPGKVNPVI PEAVVMVASQ VIGHHTAVTV 350
AGQSGNFQLN VTLPLIAYNL LESATLLGNV VMLLADKVIV GLKVRQDRVQ 400
EVLERNPILV TALNPIIGYE KAAVIAKRAY KEHRPVLEVA CEESNLNPVE 450
LARLLDPAAL TEGGIHVVGG GGG 473
Length:473
Mass (Da):50,411
Last modified:June 1, 2003 - v1
Checksum:i2524DE56009C298D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE009442 Genomic DNA. Translation: AAO28632.1.
RefSeqiNP_778983.2. NC_004556.1.

Genome annotation databases

EnsemblBacteriaiAAO28632; AAO28632; PD_0763.
GeneIDi1143485.
KEGGixft:PD0763.
PATRICi24149343. VBIXylFas71109_0986.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE009442 Genomic DNA. Translation: AAO28632.1 .
RefSeqi NP_778983.2. NC_004556.1.

3D structure databases

ProteinModelPortali Q87DC2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 183190.PD0763.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAO28632 ; AAO28632 ; PD_0763 .
GeneIDi 1143485.
KEGGi xft:PD0763.
PATRICi 24149343. VBIXylFas71109_0986.

Phylogenomic databases

eggNOGi COG0114.
KOi K01679.
OMAi MFSGPMT.
OrthoDBi EOG6V1M4M.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci XFAS183190:GIX4-763-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.
PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Comparative analyses of the complete genome sequences of Pierce's disease and citrus variegated chlorosis strains of Xylella fastidiosa."
    Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y., Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A., Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S., Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M.
    , Carrer H., Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L., Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L., Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S., Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F., Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G., Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A., Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L., Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.
    J. Bacteriol. 185:1018-1026(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Temecula1 / ATCC 700964.

Entry informationi

Entry nameiFUMC_XYLFT
AccessioniPrimary (citable) accession number: Q87DC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 74 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.

Keywords - Technical termi

Allosteric enzyme, Complete proteome

Documents

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

External Data

Dasty 3

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