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Q83ML8

- FUMC_SHIFL

UniProt

Q83ML8 - FUMC_SHIFL

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Protein
Fumarate hydratase class II
Gene
fumC, SF1634, S1765
Organism
Shigella flexneri
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 sitei188 – 1881Proton donor/acceptor By similarity
Active sitei318 – 3181 By similarity
Binding sitei319 – 3191Substrate By similarity
Sitei331 – 3311Important 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

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:SF1634, S1765
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
ProteomesiUP000001006: Chromosome, UP000002673: 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 – 467467Fumarate hydratase class IIUniRule annotation
PRO_0000161310Add
BLAST

Proteomic databases

PaxDbiQ83ML8.

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi198214.SF1634.

Structurei

3D structure databases

ProteinModelPortaliQ83ML8.
SMRiQ83ML8. Positions 4-460.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 1003Substrate binding By similarity
Regioni129 – 1324B site By similarity
Regioni139 – 1413Substrate binding By similarity
Regioni187 – 1882Substrate binding By similarity
Regioni324 – 3263Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
KOiK01679.
OMAiNAHPEYH.
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.

Q83ML8-1 [UniParc]FASTAAdd to Basket

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MNTVRSEKDS MGAIDVPADK LWGAQTQRSL EHFRISTEKM PTSLIHALAL    50
TKRAAAKVNE DLDLLSEEKA SAIRQAADEV LAGQHDDEFP LAIWQTGSGT 100
QSNMNMNEVL ANRASELLGG VRGMERKVHP NDDVNKSQSS NDVFPTAMHV 150
AALLALRKQL IPQLKTLTQT LSEKSRAFAD IVKIGRTHLQ DATPLTLGQE 200
ISGWVAMLEH NLKHIEYSLP HVAELALGGT AVGTGLNTHP EYARRVADEL 250
AVITCAPFVT APNKFEALAT CDALVQAHGA LKGLAASLMK IANDVRWLAS 300
GPRCGIGEIS IPENEPGSSI MPGKVNPTQC EALTMLCCQV MGNDVAINMG 350
GASGNFELNV FRPMVIHNFL QSVRLLADGM ESFNKHCAVG IEPNRERINQ 400
LLNESLMLVT ALNTHIGYDK AAEIAKKAHK EGLTLKAAAL ALGYLSEAEF 450
DSWVRPEQMV GSMKAGR 467
Length:467
Mass (Da):50,520
Last modified:June 1, 2003 - v1
Checksum:i865CBAE31CB2768D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005674 Genomic DNA. Translation: AAN43217.1.
AE014073 Genomic DNA. Translation: AAP17104.1.
RefSeqiNP_707510.1. NC_004337.2.
NP_837297.1. NC_004741.1.

Genome annotation databases

EnsemblBacteriaiAAN43217; AAN43217; SF1634.
AAP17104; AAP17104; S1765.
GeneIDi1027791.
1078103.
KEGGisfl:SF1634.
sfx:S1765.
PATRICi18704911. VBIShiFle31049_1954.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005674 Genomic DNA. Translation: AAN43217.1 .
AE014073 Genomic DNA. Translation: AAP17104.1 .
RefSeqi NP_707510.1. NC_004337.2.
NP_837297.1. NC_004741.1.

3D structure databases

ProteinModelPortali Q83ML8.
SMRi Q83ML8. Positions 4-460.
ModBasei Search...

Protein-protein interaction databases

STRINGi 198214.SF1634.

Proteomic databases

PaxDbi Q83ML8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN43217 ; AAN43217 ; SF1634 .
AAP17104 ; AAP17104 ; S1765 .
GeneIDi 1027791.
1078103.
KEGGi sfl:SF1634.
sfx:S1765.
PATRICi 18704911. VBIShiFle31049_1954.

Phylogenomic databases

eggNOGi COG0114.
HOGENOMi HOG000061736.
KOi K01679.
OMAi NAHPEYH.
OrthoDBi EOG6V1M4M.

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.
TIGRFAMsi TIGR00979. fumC_II. 1 hit.
PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
    Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
    , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
    Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 301 / Serotype 2a.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700930 / 2457T / Serotype 2a.

Entry informationi

Entry nameiFUMC_SHIFL
AccessioniPrimary (citable) accession number: Q83ML8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 84 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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