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Q55674

- FUMC_SYNY3

UniProt

Q55674 - FUMC_SYNY3

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Protein
Fumarate hydratase class II
Gene
fumC, slr0018
Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
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

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:slr0018
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
ProteomesiUP000001425: 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_0000161325Add
BLAST

Proteomic databases

PaxDbiQ55674.

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

IntActiQ55674. 1 interaction.
STRINGi1148.slr0018.

Structurei

3D structure databases

ProteinModelPortaliQ55674.
SMRiQ55674. Positions 6-461.

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.
OMAiAARHMKL.
OrthoDBiEOG6V1M4M.
PhylomeDBiQ55674.

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.

Q55674-1 [UniParc]FASTAAdd to Basket

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MVNSHRLETD SMGSLEVQAD RLWGAQTQRS LMFFDIGSDV MPPDLIRAFA    50
ILKKAAAITN QDLGKLPADK AELIITAADE IIAGQWLDHF PLRIWQTGSG 100
TQTNMNVNEV IANRAIAICG GELGSKNPIH PNDHVNMSQS SNDTFPTAMH 150
IAAVAGLQTK LIPSLQALRD SLNEKAECFA GITKIGRTHL MDAVPLTLGQ 200
EFSGYVAQLD QGLTQINYCL PGLLELALGG TAVGTGLNSH PQFAKKVAEE 250
IAQLTGYTFI SAPNKFAALA GHEAIAFASG VLKSIAASLM KIANDLRWMG 300
SGPRCGLGEL ALPANEPGSS IMPGKVNPTQ CEAMTMVCVQ VMGNDATIGF 350
AASQGNFELN VFKPVIIHNF LHSLHLLSDA CASFRQHLVV GLQVNESKVK 400
DFLDTSLMLV TALNPHIGYD NAALVAKTAF AQGITLKQAA VDLGLLTPAQ 450
FDAWVVPEQM IAPIAD 466
Length:466
Mass (Da):49,687
Last modified:November 1, 1996 - v1
Checksum:i7C46A68EA26233C7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000022 Genomic DNA. Translation: BAA10200.1.
PIRiS76348.
RefSeqiNP_442130.1. NC_000911.1.
YP_005652188.1. NC_017277.1.
YP_007452007.1. NC_020286.1.

Genome annotation databases

EnsemblBacteriaiBAA10200; BAA10200; BAA10200.
GeneIDi952663.
KEGGisyn:slr0018.
syy:SYNGTS_2235.
syz:MYO_122590.
PATRICi23841868. VBISynSp132158_2478.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000022 Genomic DNA. Translation: BAA10200.1 .
PIRi S76348.
RefSeqi NP_442130.1. NC_000911.1.
YP_005652188.1. NC_017277.1.
YP_007452007.1. NC_020286.1.

3D structure databases

ProteinModelPortali Q55674.
SMRi Q55674. Positions 6-461.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q55674. 1 interaction.
STRINGi 1148.slr0018.

Proteomic databases

PaxDbi Q55674.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAA10200 ; BAA10200 ; BAA10200 .
GeneIDi 952663.
KEGGi syn:slr0018.
syy:SYNGTS_2235.
syz:MYO_122590.
PATRICi 23841868. VBISynSp132158_2478.

Phylogenomic databases

eggNOGi COG0114.
HOGENOMi HOG000061736.
KOi K01679.
OMAi AARHMKL.
OrthoDBi EOG6V1M4M.
PhylomeDBi Q55674.

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. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome."
    Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S.
    DNA Res. 2:153-166(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 27184 / PCC 6803 / N-1.
  2. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
    Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.
    , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 6803 / Kazusa.

Entry informationi

Entry nameiFUMC_SYNY3
AccessioniPrimary (citable) accession number: Q55674
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 97 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Synechocystis PCC 6803
    Synechocystis (strain PCC 6803): entries and gene names

External Data

Dasty 3

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