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Q8NRN8

- FUMC_CORGL

UniProt

Q8NRN8 - FUMC_CORGL

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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

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 sitei187 – 1871Proton 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

BRENDAi4.2.1.2. 1648.
SABIO-RKQ8NRN8.
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
Synonyms:fum
Ordered Locus Names:Cgl1010, cg1145
OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Taxonomic identifieri196627 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
ProteomesiUP000000582: Chromosome, UP000001009: 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 – 473473Fumarate hydratase class IIPRO_0000161272Add
BLAST

2D gel databases

World-2DPAGE0001:Q8NRN8.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi196627.cg1145.

Structurei

3D structure databases

ProteinModelPortaliQ8NRN8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni104 – 1063Substrate bindingUniRule annotation
Regioni128 – 1314B siteUniRule annotation
Regioni138 – 1403Substrate bindingUniRule annotation
Regioni186 – 1872Substrate bindingUniRule annotation
Regioni324 – 3263Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061737.
KOiK01679.
OMAiENYRIES.
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.

Q8NRN8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSDFMTEQEF RIEHDTMGEV KVPAKALWQA QTQRAVENFP ISGRGLESAQ
60 70 80 90 100
IRAMGLLKAA CAQVNKDSGA LDAEKADAII AAGKEIASGK HDAEFPIDVF
110 120 130 140 150
QTGSGTSSNM NTNEVIASIA KANGVEVHPN DHVNMGQSSN DTFPTATHVA
160 170 180 190 200
ATEAAVNDLI PGLKVLHESL AKKANEWSEV VKSGRTHLMD AVPVTLGQEF
210 220 230 240 250
GGYARQIQLG IERVEATLPR LGELAIGGTA AGTGINTSAD FGGKVVAELI
260 270 280 290 300
NLTDVKELKE AENHFEAQAA RDALVEFSGA MRVIAVSLYK IANDIRLMGS
310 320 330 340 350
GPLTGLGEIR LPDLQPGSSI MPGKVNPVLC ETATQVSAQV IGNDAAVAFS
360 370 380 390 400
GTQGQFELNV FIPVMARNVL ESARLLANTS RVFATRLVDG IEPNEAHMKE
410 420 430 440 450
LAESSPSIVT PLNSAIGYEA AAKVAKTALA EGKTIRQTVI DLGLVDGEKL
460 470
TEEELDKRLD VLAMAHTERE NKF
Length:473
Mass (Da):50,244
Last modified:October 1, 2002 - v1
Checksum:i315AF884777A39F0
GO

Sequence cautioni

The sequence CAF19712.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000036 Genomic DNA. Translation: BAB98403.1.
BX927151 Genomic DNA. Translation: CAF19712.1. Different initiation.
RefSeqiNP_600233.1. NC_003450.3.
YP_225298.1. NC_006958.1.

Genome annotation databases

EnsemblBacteriaiBAB98403; BAB98403; BAB98403.
CAF19712; CAF19712; cg1145.
GeneIDi1018996.
3344954.
KEGGicgl:NCgl0967.
PATRICi21494066. VBICorGlu203724_0990.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000036 Genomic DNA. Translation: BAB98403.1 .
BX927151 Genomic DNA. Translation: CAF19712.1 . Different initiation.
RefSeqi NP_600233.1. NC_003450.3.
YP_225298.1. NC_006958.1.

3D structure databases

ProteinModelPortali Q8NRN8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 196627.cg1145.

2D gel databases

World-2DPAGE 0001:Q8NRN8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB98403 ; BAB98403 ; BAB98403 .
CAF19712 ; CAF19712 ; cg1145 .
GeneIDi 1018996.
3344954.
KEGGi cgl:NCgl0967.
PATRICi 21494066. VBICorGlu203724_0990.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BRENDAi 4.2.1.2. 1648.
SABIO-RK Q8NRN8.

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. "The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
    Ikeda M., Nakagawa S.
    Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Entry informationi

Entry nameiFUMC_CORGL
AccessioniPrimary (citable) accession number: Q8NRN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2002
Last modified: November 26, 2014
This is version 79 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