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Q8TS07

- FUMC_METAC

UniProt

Q8TS07 - FUMC_METAC

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Protein
Fumarate hydratase class II
Gene
fumC, MA_1001
Organism
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
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 sitei200 – 2001Proton donor/acceptor By similarity
Active sitei330 – 3301 By similarity
Binding sitei331 – 3311Substrate By similarity
Sitei343 – 3431Important 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

BioCyciMACE188937:GI2O-1012-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:MA_1001
OrganismiMethanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Taxonomic identifieri188937 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
ProteomesiUP000002487: 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 – 484484Fumarate hydratase class IIUniRule annotation
PRO_0000161333Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi188937.MA1001.

Structurei

3D structure databases

ProteinModelPortaliQ8TS07.
SMRiQ8TS07. Positions 16-473.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni110 – 1123Substrate binding By similarity
Regioni141 – 1444B site By similarity
Regioni151 – 1533Substrate binding By similarity
Regioni199 – 2002Substrate binding By similarity
Regioni336 – 3383Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0114.
KOiK01679.
OMAiMFSGPMT.
PhylomeDBiQ8TS07.

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.

Q8TS07-1 [UniParc]FASTAAdd to Basket

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MPSILDLPIG TGATGKRKES DSLGEVEVPA DHYWGAQTQR SLIHFSIGDD    50
YMPKEVYHAY GYVKKAAALV NEAAGIIPPW KAELIARVAD EVIAGKLDSE 100
FPLYVWQTGS GTQSNMNVNE VISNRAIQLV GGSLGSKHPV HPNDDVNMSQ 150
SSNDTFPTAM HIATVLEFSN RLIPAVTVLE ESIWAKAREW VDIVKIGRTH 200
LQDATPLTVG QEWSGYATQL DDALAFVKHS LRGLYRLAIG GTAVGTGINT 250
PPDFGEKVAD EIARLTGHPF VTAPNKFAAQ GSLDAMVTSS AALRTLAVAL 300
MKIANDLQWL GSGPRSGLHE LILPSDEPGS SIMPGKVNPT QEEAMLMVCI 350
QVIGEDNAVA FAGSQGNFEL NAMCPIIINN VLHSARTLGD ACVKFREYGI 400
NGIMLDRSRI DKFVGTSLML VTALSPVIGY DKASAIVQRA LDENTTLREA 450
AVKGGFISAE DFDRIVDPKK MVGDPRHDLK LASE 484
Length:484
Mass (Da):52,127
Last modified:December 15, 2003 - v2
Checksum:i06F0EFE5664BEEC8
GO

Sequence cautioni

The sequence AAM04432.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE010299 Genomic DNA. Translation: AAM04432.1. Different initiation.
RefSeqiNP_615952.1. NC_003552.1.

Genome annotation databases

EnsemblBacteriaiAAM04432; AAM04432; MA_1001.
GeneIDi1472891.
KEGGimac:MA1001.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE010299 Genomic DNA. Translation: AAM04432.1 . Different initiation.
RefSeqi NP_615952.1. NC_003552.1.

3D structure databases

ProteinModelPortali Q8TS07.
SMRi Q8TS07. Positions 16-473.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 188937.MA1001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAM04432 ; AAM04432 ; MA_1001 .
GeneIDi 1472891.
KEGGi mac:MA1001.

Phylogenomic databases

eggNOGi COG0114.
KOi K01679.
OMAi MFSGPMT.
PhylomeDBi Q8TS07.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci MACE188937:GI2O-1012-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. "The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity."
    Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.
    , McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., Metcalf W.W., Birren B.
    Genome Res. 12:532-542(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A.

Entry informationi

Entry nameiFUMC_METAC
AccessioniPrimary (citable) accession number: Q8TS07
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: May 14, 2014
This is version 79 of the entry and version 2 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

External Data

Dasty 3

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