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Q9HQ29

- FUMC_HALSA

UniProt

Q9HQ29 - FUMC_HALSA

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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium)
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 sitei188 – 1881Proton donor/acceptorBy similarity
Active sitei318 – 3181By similarity
Binding sitei319 – 3191SubstrateUniRule annotation
Sitei331 – 3311Important 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

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:VNG_1356G
OrganismiHalobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium)
Taxonomic identifieri64091 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHalobacterium
ProteomesiUP000000554: 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 – 470470Fumarate hydratase class IIPRO_0000161332Add
BLAST

Proteomic databases

PaxDbiQ9HQ29.
PRIDEiQ9HQ29.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi64091.VNG1356G.

Structurei

3D structure databases

ProteinModelPortaliQ9HQ29.
SMRiQ9HQ29. Positions 5-459.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni99 – 1013Substrate bindingUniRule annotation
Regioni129 – 1324B siteUniRule annotation
Regioni139 – 1413Substrate bindingUniRule annotation
Regioni187 – 1882Substrate bindingUniRule annotation
Regioni324 – 3263Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0114.
InParanoidiQ9HQ29.
KOiK01679.
OMAiLNVMLPI.
PhylomeDBiQ9HQ29.

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.

Q9HQ29 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSEDYRTEQD SLGEMQVPAD AYWGAQTQRA IENFPISGIA FGRRFVRALG
60 70 80 90 100
VVKKAAAQAN RDLGLVDDER ADAIVAAADE VIAGEHDDQF PVDVFQTGSG
110 120 130 140 150
TSSNMNANEV IANRAAELLG EEIGDRVVHP NDHVNYGQSS NDVIPTAMHV
160 170 180 190 200
ASLDALVNDV KPGLETLAAE LDDKADAFDG VVKTGRTHLQ DATPVRLGQE
210 220 230 240 250
FGGYRTQVEK GIDRIEAVAP RLSELALGGT AVGTGLNTHP EFPETAAGYI
260 270 280 290 300
SEETGVTFRE ADNHFEAQAA HDAMNEAHGA LRTVAGSLNK IANDLRLLAS
310 320 330 340 350
GPRNGLGEIE QPENQPGSSI MPGKINPVVA EAVNQVHKQV VGNDAAIAAG
360 370 380 390 400
AAEGQIDLNL YKPVLAHNFL QSADMLANAS AAFGEKFVAK LEANEAACEA
410 420 430 440 450
QVERSMALAT ALNPTIGYDK ASEVAKAALK EGKTVTEVVV EKGYLSEAEA
460 470
ADVLDPEGMT HRGILSGDDT
Length:470
Mass (Da):49,597
Last modified:March 1, 2001 - v1
Checksum:i31FF468F0B4FC261
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE004437 Genomic DNA. Translation: AAG19688.1.
PIRiD84290.
RefSeqiNP_280208.1. NC_002607.1.

Genome annotation databases

EnsemblBacteriaiAAG19688; AAG19688; VNG_1356G.
GeneIDi1447987.
KEGGihal:VNG1356G.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE004437 Genomic DNA. Translation: AAG19688.1 .
PIRi D84290.
RefSeqi NP_280208.1. NC_002607.1.

3D structure databases

ProteinModelPortali Q9HQ29.
SMRi Q9HQ29. Positions 5-459.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 64091.VNG1356G.

Proteomic databases

PaxDbi Q9HQ29.
PRIDEi Q9HQ29.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG19688 ; AAG19688 ; VNG_1356G .
GeneIDi 1447987.
KEGGi hal:VNG1356G.

Phylogenomic databases

eggNOGi COG0114.
InParanoidi Q9HQ29.
KOi K01679.
OMAi LNVMLPI.
PhylomeDBi Q9HQ29.

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.
PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700922 / JCM 11081 / NRC-1.

Entry informationi

Entry nameiFUMC_HALSA
AccessioniPrimary (citable) accession number: Q9HQ29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2001
Last modified: October 29, 2014
This is version 81 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