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P71384

- FUMC_HAEIN

UniProt

P71384 - FUMC_HAEIN

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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
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:HI_1398
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
ProteomesiUP000000579: 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 – 464464Fumarate hydratase class IIPRO_0000161279Add
BLAST

Proteomic databases

PRIDEiP71384.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi71421.HI1398.

Structurei

3D structure databases

ProteinModelPortaliP71384.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 1003Substrate 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.
KOiK01679.
OMAiNAHPEYH.
OrthoDBiEOG6V1M4M.
PhylomeDBiP71384.

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.

P71384-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAFRIEKDTM GEVQVLADKY WAAQTERSRN NFKIGPAASM PHEIIEAFGY
60 70 80 90 100
LKKAAAFANH DLGVLPLEKR DLIALACDEI LANKLDDQFP LVIWQTGSGT
110 120 130 140 150
QSNMNVNEVV ANRAHVLNGG KLGEKSIIHP NDDVNKSQSS NDTFPTAMHI
160 170 180 190 200
AAYKKVVEHT IPCVERLQKT FAAKSEAFKN VVKIGRTHLM DATPLTLGQE
210 220 230 240 250
FSAYAAQLDF GLKALKNTLP HLSQLALGGT AVGTGLNTPK GYDLKVVDYI
260 270 280 290 300
AKFTALPFVT ADNKFEALAA HDAIVETHGA LRQLAMSLFK IANDIRLLAS
310 320 330 340 350
GPRSGIGEIL IPENEPGSSI MPGKVNPTQC EXMTMVCAQV FGNDTTIAFV
360 370 380 390 400
GSQGHFQLNV FNPVMIANFL QSAQLLGDAC VSFDEHCAVG IEPNYPRIKQ
410 420 430 440 450
QLENSLMLVT ALNTHIGYEN AAKIAKTAHK NGTTLREEAI NLGLVSAEDF
460
DKWVRPEDMV GSLK
Length:464
Mass (Da):50,482
Last modified:February 1, 1997 - v1
Checksum:iAC836336DA7457CE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L42023 Genomic DNA. Translation: AAC23045.1.
RefSeqiNP_439551.1. NC_000907.1.
WP_010869204.1. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC23045; AAC23045; HI_1398.
GeneIDi950314.
KEGGihin:HI1398.
PATRICi20191495. VBIHaeInf48452_1458.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L42023 Genomic DNA. Translation: AAC23045.1 .
RefSeqi NP_439551.1. NC_000907.1.
WP_010869204.1. NC_000907.1.

3D structure databases

ProteinModelPortali P71384.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 71421.HI1398.

Proteomic databases

PRIDEi P71384.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC23045 ; AAC23045 ; HI_1398 .
GeneIDi 950314.
KEGGi hin:HI1398.
PATRICi 20191495. VBIHaeInf48452_1458.

Phylogenomic databases

eggNOGi COG0114.
KOi K01679.
OMAi NAHPEYH.
OrthoDBi EOG6V1M4M.
PhylomeDBi P71384.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Entry informationi

Entry nameiFUMC_HAEIN
AccessioniPrimary (citable) accession number: P71384
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 1, 1997
Last modified: October 29, 2014
This is version 105 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. Haemophilus influenzae
    Haemophilus influenzae (strain Rd): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3