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Q9JTR0

- FUMC_NEIMA

UniProt

Q9JTR0 - FUMC_NEIMA

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Protein
Fumarate hydratase class II
Gene
fumC, NMA1670
Organism
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
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 sitei187 – 1871Proton donor/acceptor By similarity
Active sitei317 – 3171 By similarity
Binding sitei318 – 3181Substrate By similarity
Sitei330 – 3301Important for catalytic activity By similarity

GO - Molecular functioni

  1. fumarate hydratase activity Source: UniProtKB-HAMAP
Complete GO annotation...

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

BioCyciNMEN122587:GI3Q-1519-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:NMA1670
OrganismiNeisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Taxonomic identifieri122587 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
ProteomesiUP000000626: 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 – 462462Fumarate hydratase class IIUniRule annotation
PRO_0000161291Add
BLAST

Proteomic databases

PRIDEiQ9JTR0.

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi122587.NMA1670.

Structurei

3D structure databases

ProteinModelPortaliQ9JTR0.
SMRiQ9JTR0. Positions 4-459.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 993Substrate binding By similarity
Regioni128 – 1314B site By similarity
Regioni138 – 1403Substrate binding By similarity
Regioni186 – 1872Substrate binding By similarity
Regioni323 – 3253Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061737.
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.

Q9JTR0-1 [UniParc]FASTAAdd to Basket

« Hide

MNTRTEHDTM GNVEVPSEAY WGAQTQRSRN NFKIGGETLP QPLIYALALV    50
KKAAAATNVS LGRIKPEQAD LITQAADDVL NGKLDGQFPL VVWQTGSGTQ 100
SNMNMNEVLA NRANEIAGTG LAAYQPVHPN DHVNHAQSTN DAFPTAIHVA 150
AAIEINRHLI PAVKALRDTL DKKAQAFAPI VKIGRTHLQD ATPLTLGQEF 200
SGYVSQLDHG LGRLNDALKD LYELALGGTA VGTGLNSHPE YAEKAAAKLA 250
ELSGLPFVSA PNKFEALGGR DAAVAASGAL KTLAASLNKI ANDIRWLASG 300
PRCGLGEIKI PENEPGSSIM PGKVNPTQCE AMTMVCCQVF GNDVTIGMAG 350
ASGNFELNVY MPVIAYNLLQ SIRLLGDACN SFNEHCAVGI EPVPEKIDYF 400
LHHSLMLVTA LNRKIGYENA AKVAKTAYKN NKSLRETAVE LGLLTGEEFD 450
ELVVPADMVH PR 462
Length:462
Mass (Da):49,391
Last modified:October 1, 2000 - v1
Checksum:i6F63B3D506E26C85
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL157959 Genomic DNA. Translation: CAM08803.1.
PIRiB81862.
RefSeqiYP_002342970.1. NC_003116.1.

Genome annotation databases

EnsemblBacteriaiCAM08803; CAM08803; NMA1670.
GeneIDi908059.
KEGGinma:NMA1670.
PATRICi20364519. VBINeiMen132687_1961.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL157959 Genomic DNA. Translation: CAM08803.1 .
PIRi B81862.
RefSeqi YP_002342970.1. NC_003116.1.

3D structure databases

ProteinModelPortali Q9JTR0.
SMRi Q9JTR0. Positions 4-459.
ModBasei Search...

Protein-protein interaction databases

STRINGi 122587.NMA1670.

Proteomic databases

PRIDEi Q9JTR0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAM08803 ; CAM08803 ; NMA1670 .
GeneIDi 908059.
KEGGi nma:NMA1670.
PATRICi 20364519. VBINeiMen132687_1961.

Phylogenomic databases

eggNOGi COG0114.
HOGENOMi HOG000061737.
KOi K01679.
OMAi MESFNIH.
OrthoDBi EOG6V1M4M.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci NMEN122587:GI3Q-1519-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.
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: Z2491.

Entry informationi

Entry nameiFUMC_NEIMA
AccessioniPrimary (citable) accession number: Q9JTR0
Secondary accession number(s): A1ISP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 86 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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