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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Prochlorococcus marinus (strain SARG / CCMP1375 / SS120)
Status
Reviewed-Annotation score: 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 sitei189 – 1891Proton donor/acceptorBy similarity
Active sitei319 – 3191By similarity
Binding sitei320 – 3201SubstrateUniRule annotation
Sitei332 – 3321Important for catalytic activityBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciPMAR167539:GJN2-1656-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:Pro_1620
OrganismiProchlorococcus marinus (strain SARG / CCMP1375 / SS120)
Taxonomic identifieri167539 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000001420 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 465465Fumarate hydratase class IIPRO_0000161296Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi167539.Pro1620.

Structurei

3D structure databases

ProteinModelPortaliQ7VA47.
SMRiQ7VA47. Positions 4-462.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni99 – 1013Substrate bindingUniRule annotation
Regioni130 – 1334B siteUniRule annotation
Regioni140 – 1423Substrate bindingUniRule annotation
Regioni188 – 1892Substrate bindingUniRule annotation
Regioni325 – 3273Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0114.
KOiK01679.
OMAiNTPKGYD.
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.

Q7VA47-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQSFRIEND SMGTIKVPDQ ALWGAQTQRS LINFAIGHNK MPMKLIYSIV
60 70 80 90 100
QIKASAAIVN CRLGVLDKQR KNFILNACNE ISNGMHDEQF PLSVWQTGSG
110 120 130 140 150
TQTNMNVNEV ISNIASHLNG NKLGSHEPLH PNDHVNRSQS TNDVFPAAIQ
160 170 180 190 200
IATVQEILEN LLPELDQLIE TFDKKIIKWN RIIKTGRTHL QDAVPLTLGQ
210 220 230 240 250
EASAWKEQLI ASRNRLNKSL NELYPLPLGG TAIGTGLNAP AKFDKEIALE
260 270 280 290 300
IAKSTRSPFV SAQNKFAIMA SHDALVHTMS QLKLLAVSLF KIVNDLRLLS
310 320 330 340 350
CGPRGGLGEL RLPENEPGSS IMPGKVNPTQ CEAMAMVCTQ IMALDSAVTM
360 370 380 390 400
AGSGGHLQMN SYKPLIAFNL LESIDLLSSA CKSSRILMIE GIEPNLEKIQ
410 420 430 440 450
NSLQNSLMLI TSLTPIIGYE KASKIAQCAH EKDITLKEAT KLLGYLNEDD
460
FDRIVNPQSM TGMEN
Length:465
Mass (Da):51,045
Last modified:October 1, 2003 - v1
Checksum:iF2F17242168FDA54
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017126 Genomic DNA. Translation: AAQ00664.1.
RefSeqiNP_876011.1. NC_005042.1.
WP_011125770.1. NC_005042.1.

Genome annotation databases

EnsemblBacteriaiAAQ00664; AAQ00664; Pro_1620.
GeneIDi1463002.
KEGGipma:Pro_1620.
PATRICi23030061. VBIProMar8617_1712.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017126 Genomic DNA. Translation: AAQ00664.1.
RefSeqiNP_876011.1. NC_005042.1.
WP_011125770.1. NC_005042.1.

3D structure databases

ProteinModelPortaliQ7VA47.
SMRiQ7VA47. Positions 4-462.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi167539.Pro1620.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAQ00664; AAQ00664; Pro_1620.
GeneIDi1463002.
KEGGipma:Pro_1620.
PATRICi23030061. VBIProMar8617_1712.

Phylogenomic databases

eggNOGiCOG0114.
KOiK01679.
OMAiNTPKGYD.
OrthoDBiEOG6V1M4M.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.
BioCyciPMAR167539:GJN2-1656-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SARG / CCMP1375 / SS120.

Entry informationi

Entry nameiFUMC_PROMA
AccessioniPrimary (citable) accession number: Q7VA47
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: May 27, 2015
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).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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.