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Q7V5R2

- FUMC_PROMM

UniProt

Q7V5R2 - FUMC_PROMM

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Protein
Fumarate hydratase class II
Gene
fumC, PMT_1485
Organism
Prochlorococcus marinus (strain MIT 9313)
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 sitei190 – 1901Proton donor/acceptor By similarity
Active sitei320 – 3201 By similarity
Binding sitei321 – 3211Substrate By similarity
Sitei333 – 3331Important 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

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:PMT_1485
OrganismiProchlorococcus marinus (strain MIT 9313)
Taxonomic identifieri74547 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000001423: 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 – 466466Fumarate hydratase class IIUniRule annotation
PRO_0000161297Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi74547.PMT1485.

Structurei

3D structure databases

ProteinModelPortaliQ7V5R2.
SMRiQ7V5R2. Positions 6-461.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni100 – 1023Substrate binding By similarity
Regioni131 – 1344B site By similarity
Regioni141 – 1433Substrate binding By similarity
Regioni189 – 1902Substrate binding By similarity
Regioni326 – 3283Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0114.
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.

Q7V5R2-1 [UniParc]FASTAAdd to Basket

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MMADLMRIEH DSMGTIEVPA GVLWGAQTQR SLLNFAISTD RMPVELIHAL    50
ALIKQAAASV NCRLGVLDEV QRDQIIKAAS AVASGLHDDQ FPLRVWQTGS 100
GTHTNMNVNE VISNLASQAN DEPLGSHRPV HPNDHVNRSQ STNDAFPTAI 150
HIAAVQGITN NLLPELEQLI AAFARKSDAW SDIIKIGRTH LQDAVPLTLG 200
QEASAWRDQI ASAHSRIQSS LIELYPLPLG GTAVGTGLNA PARFGQETAA 250
QLASITGLPF SSAKNKFAVM ASHDGLVNAM AQLRMLAVAL FKISNDLRLL 300
ACGPRAGLAE LHLPENEPGS SIMPGKVNPS QCEAMAMVCL QVIGLDSAVT 350
MAGGSGHLQM NVYKPLIGFN LLHSIELLHD ACRKYRLAMV QGIEPNRIKI 400
QHDLEQSLML VTALAPEIGY DKASEIAHLA HEKGFSLREA ALKLGYVSKE 450
DFDRIVNPAL MTSARL 466
Length:466
Mass (Da):50,233
Last modified:October 1, 2003 - v1
Checksum:i395908D8DD84B12D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX548175 Genomic DNA. Translation: CAE21660.1.
RefSeqiNP_895312.1. NC_005071.1.
WP_011130853.1. NC_005071.1.

Genome annotation databases

EnsemblBacteriaiCAE21660; CAE21660; PMT_1485.
GeneIDi1728513.
KEGGipmt:PMT1485.
PATRICi23011523. VBIProMar135351_1905.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX548175 Genomic DNA. Translation: CAE21660.1 .
RefSeqi NP_895312.1. NC_005071.1.
WP_011130853.1. NC_005071.1.

3D structure databases

ProteinModelPortali Q7V5R2.
SMRi Q7V5R2. Positions 6-461.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 74547.PMT1485.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAE21660 ; CAE21660 ; PMT_1485 .
GeneIDi 1728513.
KEGGi pmt:PMT1485.
PATRICi 23011523. VBIProMar135351_1905.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .

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: MIT 9313.

Entry informationi

Entry nameiFUMC_PROMM
AccessioniPrimary (citable) accession number: Q7V5R2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: September 3, 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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