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Q7V024

- FUMC_PROMP

UniProt

Q7V024 - FUMC_PROMP

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Protein
Fumarate hydratase class II
Gene
fumC, PMM1466
Organism
Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4)
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

BioCyciPMAR59919:GJMQ-1506-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:PMM1466
OrganismiProchlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4)
Taxonomic identifieri59919 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000001026: 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 – 461461Fumarate hydratase class IIUniRule annotation
PRO_0000161298Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi59919.PMM1466.

Structurei

3D structure databases

ProteinModelPortaliQ7V024.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni99 – 1013Substrate 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.
HOGENOMiHOG000061736.
KOiK01679.
OMAiGDECARI.
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.

Q7V024-1 [UniParc]FASTAAdd to Basket

« Hide

MTKNFRFEKD SMGQIKVPSE ALWGAQTQRS IINFSIGEEL IPIELIYSLT    50
VIKRAAAISN FKLGLINNVK KDLIIEACTE ILDGKHDSQF PLKIWQTGSG 100
TQTNMNINEV ISNIAALKTN SGLGSHHPIH PNDDVNKSQS TNDTFPAAIQ 150
ISVVTQIIKK LVPSIKELTK VLDSKSNKWK DLIKIGRTHF QDAVPISLGQ 200
EVSAWSKQLK DAEDALIISL NELCFLPLGG TAVGTGINCP KDFSKESIKS 250
ISEYTGLFFY KSKNHFSLMA SHDRLAQVMG QIKILASALF KISNDIKILS 300
SGPRSGIYEL IIPKNEPGSS IMPGKVNPTQ CEALSMVCTQ VMGFEYAVSI 350
ANASGTLQMN EYKPLIGFNI LTSIKLLNHA ISNFRLKLVE GIQPNPKTIK 400
ANLENSLMLV TALVPKIGYE KAAEIANLAF NESINLKEAT IKLGYLTANE 450
FEDAINTNKM I 461
Length:461
Mass (Da):50,624
Last modified:October 1, 2003 - v1
Checksum:iD696F9A39BF50149
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX548174 Genomic DNA. Translation: CAE19925.1.
RefSeqiNP_893583.1. NC_005072.1.

Genome annotation databases

EnsemblBacteriaiCAE19925; CAE19925; PMM1466.
GeneIDi1725618.
KEGGipmm:PMM1466.
PATRICi23034108. VBIProMar68066_1707.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX548174 Genomic DNA. Translation: CAE19925.1 .
RefSeqi NP_893583.1. NC_005072.1.

3D structure databases

ProteinModelPortali Q7V024.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 59919.PMM1466.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAE19925 ; CAE19925 ; PMM1466 .
GeneIDi 1725618.
KEGGi pmm:PMM1466.
PATRICi 23034108. VBIProMar68066_1707.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci PMAR59919:GJMQ-1506-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CCMP1986 / MED4.

Entry informationi

Entry nameiFUMC_PROMP
AccessioniPrimary (citable) accession number: Q7V024
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 73 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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