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Q7V024

- FUMC_PROMP

UniProt

Q7V024 - FUMC_PROMP

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Protein

Fumarate hydratase class II

Gene

fumC

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

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

  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 IIUniRule annotation (EC:4.2.1.2UniRule annotation)
Short name:
Fumarase CUniRule annotation
Gene namesi
Name:fumCUniRule annotation
Ordered Locus Names:PMM1466
OrganismiProchlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4)
Taxonomic identifieri59919 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000001026: Chromosome

Subcellular locationi

Cytoplasm 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 IIPRO_0000161298Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi59919.PMM1466.

Structurei

3D structure databases

ProteinModelPortaliQ7V024.
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.
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

        10         20         30         40         50
MTKNFRFEKD SMGQIKVPSE ALWGAQTQRS IINFSIGEEL IPIELIYSLT
60 70 80 90 100
VIKRAAAISN FKLGLINNVK KDLIIEACTE ILDGKHDSQF PLKIWQTGSG
110 120 130 140 150
TQTNMNINEV ISNIAALKTN SGLGSHHPIH PNDDVNKSQS TNDTFPAAIQ
160 170 180 190 200
ISVVTQIIKK LVPSIKELTK VLDSKSNKWK DLIKIGRTHF QDAVPISLGQ
210 220 230 240 250
EVSAWSKQLK DAEDALIISL NELCFLPLGG TAVGTGINCP KDFSKESIKS
260 270 280 290 300
ISEYTGLFFY KSKNHFSLMA SHDRLAQVMG QIKILASALF KISNDIKILS
310 320 330 340 350
SGPRSGIYEL IIPKNEPGSS IMPGKVNPTQ CEALSMVCTQ VMGFEYAVSI
360 370 380 390 400
ANASGTLQMN EYKPLIGFNI LTSIKLLNHA ISNFRLKLVE GIQPNPKTIK
410 420 430 440 450
ANLENSLMLV TALVPKIGYE KAAEIANLAF NESINLKEAT IKLGYLTANE
460
FEDAINTNKM I
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: October 1, 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).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