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Q7SX99

- FUMH_DANRE

UniProt

Q7SX99 - FUMH_DANRE

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Protein

Fumarate hydratase, mitochondrial

Gene

fh

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Catalytic activityi

(S)-malate = fumarate + H2O.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei146 – 1461SubstrateBy similarity

GO - Molecular functioni

  1. fumarate hydratase activity Source: UniProtKB-EC

GO - Biological processi

  1. fumarate metabolic process Source: InterPro
  2. tricarboxylic acid cycle Source: UniProtKB-UniPathway
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, mitochondrial (EC:4.2.1.2)
Short name:
Fumarase
Gene namesi
Name:fh
ORF Names:zgc:66253
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
ProteomesiUP000000437: Unplaced

Organism-specific databases

ZFINiZDB-GENE-010724-6. fh.

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-KW
  2. tricarboxylic acid cycle enzyme complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4343MitochondrionBy similarityAdd
BLAST
Chaini44 – 509466Fumarate hydratase, mitochondrialPRO_0000010327Add
BLAST

Proteomic databases

PRIDEiQ7SX99.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi7955.ENSDARP00000097494.

Structurei

3D structure databases

ProteinModelPortaliQ7SX99.
SMRiQ7SX99. Positions 48-509.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni175 – 1784B siteBy similarity
Regioni185 – 1873Substrate bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
HOVERGENiHBG002183.
InParanoidiQ7SX99.
KOiK01679.
PhylomeDBiQ7SX99.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q7SX99-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MYRSARSLHR FSASLSDLRA AQRSIKARNV CPAPGLRHQT VRMASSEAFR
60 70 80 90 100
IERDTFGELK VPSDKYYGAQ TVRSTMNFRI GGVTERMPIQ VIRAFGILKK
110 120 130 140 150
AAAEVNKDYG LDPKIADAIM KAADEVESGK LDDHFPLVVW QTGSGTQTNM
160 170 180 190 200
NVNEVISNRA IEMLGGKLGS KDPVHPNDHV NKSQSSNDTF PTAMHIAAAK
210 220 230 240 250
EVHEVLLPGL QTLHDALAAK AEQFKDIIKI GRTHTQDAVP LSLGQEFGGY
260 270 280 290 300
VQQVKYSIAR VKASLPRVYE LAAGGTAVGT GLNTRIGFAE KVADKVSALT
310 320 330 340 350
GLPFVTAANK FEALAAHDAL VELSGALNTV AVSMMKIAND IRFLGSGPRS
360 370 380 390 400
GLGELILPEN EPGSSIMPGK VNPTQCEAMT MVAAQVMGNH VAVTVGGSNG
410 420 430 440 450
HFELNVFKPM IIKNVLNSAR LLGDASVSFT NNCVVGIEAN TERINKLMSE
460 470 480 490 500
SLMLVTALNP HIGYDKAAKI AKTAHKDGST LKEAALKLGF LNEQQFEEWV

RPHDMLGPK
Length:509
Mass (Da):54,861
Last modified:October 1, 2003 - v1
Checksum:i36A829D58EE18678
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC055566 mRNA. Translation: AAH55566.1.
BC066484 mRNA. Translation: AAH66484.1.
RefSeqiNP_957257.1. NM_200963.1.
UniGeneiDr.104452.

Genome annotation databases

GeneIDi393938.
KEGGidre:393938.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC055566 mRNA. Translation: AAH55566.1 .
BC066484 mRNA. Translation: AAH66484.1 .
RefSeqi NP_957257.1. NM_200963.1.
UniGenei Dr.104452.

3D structure databases

ProteinModelPortali Q7SX99.
SMRi Q7SX99. Positions 48-509.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 7955.ENSDARP00000097494.

Proteomic databases

PRIDEi Q7SX99.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 393938.
KEGGi dre:393938.

Organism-specific databases

CTDi 2271.
ZFINi ZDB-GENE-010724-6. fh.

Phylogenomic databases

eggNOGi COG0114.
HOGENOMi HOG000061736.
HOVERGENi HBG002183.
InParanoidi Q7SX99.
KOi K01679.
PhylomeDBi Q7SX99.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .

Miscellaneous databases

NextBioi 20814910.
PROi Q7SX99.

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. NIH - Zebrafish Gene Collection (ZGC) project
    Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: AB.
    Tissue: Kidney.

Entry informationi

Entry nameiFUMH_DANRE
AccessioniPrimary (citable) accession number: Q7SX99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: October 29, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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

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