fumC

Functionⁱ

Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate.UniRule annotation

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.UniRule annotation

Catalytic activityⁱ

(S)-malate = fumarate + H₂O.UniRule annotation

Pathwayⁱ: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes (S)-malate from fumarate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:

Fumarate hydratase class II (fumC), Fumarate hydratase class II (fumC), Fumarate hydratase class II (fumC)

This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-malate from fumarate, the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	126	SubstrateUniRule annotation	1
Binding siteⁱ	187	SubstrateUniRule annotation	1
Active siteⁱ	188	Proton donor/acceptorUniRule annotation	1
Active siteⁱ	318	UniRule annotation	1
Binding siteⁱ	319	SubstrateUniRule annotation	1
Siteⁱ	331	Important for catalytic activityUniRule annotation	1

GO - Molecular functionⁱ

fumarate hydratase activity Source: UniProtKB-EC

Complete GO annotation...

GO - Biological processⁱ

fumarate metabolic process Source: InterPro
tricarboxylic acid cycle Source: UniProtKB-UniPathway

Complete GO annotation...

Keywordsⁱ

Molecular function	Lyase
Biological process	Tricarboxylic acid cycle

Enzyme and pathway databases

UniPathwayⁱ	UPA00223; UER01007.

UniPathwayⁱ

UPA00223; UER01007.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Fumarate hydratase class IIUniRule annotation (EC:4.2.1.2UniRule annotation) Short name: Fumarase CUniRule annotation Alternative name(s): Aerobic fumaraseUniRule annotation Iron-independent fumaraseUniRule annotation
Gene namesⁱ	Name:fumCUniRule annotation Ordered Locus Names:SF1634, S1765
Organismⁱ	Shigella flexneri
Taxonomic identifierⁱ	623 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Shigella
Proteomesⁱ	UP000002673 Componentⁱ: Chromosome UP000001006 Componentⁱ: Chromosome

Subcellular locationⁱ

Cytoplasm
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00743

GO - Cellular componentⁱ

tricarboxylic acid cycle enzyme complex Source: InterPro

Complete GO annotation...

Keywords - Cellular componentⁱ

Cytoplasm

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000161310	1 – 467	Fumarate hydratase class IIAdd BLAST		467

Proteomic databases

PaxDbⁱ	Q83ML8.

PaxDbⁱ

Q83ML8.

Interactionⁱ

Subunit structureⁱ

Homotetramer.UniRule annotation

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q83ML8.
SMRⁱ	Q83ML8.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	98 – 100	Substrate bindingUniRule annotation	3
Regionⁱ	129 – 132	Substrate binding (B site)UniRule annotation	4
Regionⁱ	139 – 141	Substrate bindingUniRule annotation	3
Regionⁱ	324 – 326	Substrate bindingUniRule annotation	3

Sequence similaritiesⁱ

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

Phylogenomic databases

eggNOGⁱ	ENOG4105C9Q. Bacteria. COG0114. LUCA.
HOGENOMⁱ	HOG000061736.
KEGG Orthology (KO) More...KOⁱ	K01679.
OMAⁱ	VSFTDNC.

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd01362. Fumarase_classII. 1 hit.
Gene3Dⁱ	1.10.275.10. 1 hit.
HAMAPⁱ	MF_00743. FumaraseC. 1 hit.
InterProⁱ	View protein in InterPro 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.
PANTHERⁱ	PTHR11444. PTHR11444. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF10415. FumaraseC_C. 1 hit. PF00206. Lyase_1. 1 hit.
PRINTSⁱ	PR00149. FUMRATELYASE.
SUPFAMⁱ	SSF48557. SSF48557. 1 hit.
TIGRFAMsⁱ	TIGR00979. fumC_II. 1 hit.
PROSITEⁱ	View protein in PROSITE PS00163. FUMARATE_LYASES. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

Q83ML8-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MNTVRSEKDS MGAIDVPADK LWGAQTQRSL EHFRISTEKM PTSLIHALAL 
        60         70         80         90        100
TKRAAAKVNE DLDLLSEEKA SAIRQAADEV LAGQHDDEFP LAIWQTGSGT 
       110        120        130        140        150
QSNMNMNEVL ANRASELLGG VRGMERKVHP NDDVNKSQSS NDVFPTAMHV 
       160        170        180        190        200
AALLALRKQL IPQLKTLTQT LSEKSRAFAD IVKIGRTHLQ DATPLTLGQE 
       210        220        230        240        250
ISGWVAMLEH NLKHIEYSLP HVAELALGGT AVGTGLNTHP EYARRVADEL 
       260        270        280        290        300
AVITCAPFVT APNKFEALAT CDALVQAHGA LKGLAASLMK IANDVRWLAS 
       310        320        330        340        350
GPRCGIGEIS IPENEPGSSI MPGKVNPTQC EALTMLCCQV MGNDVAINMG 
       360        370        380        390        400
GASGNFELNV FRPMVIHNFL QSVRLLADGM ESFNKHCAVG IEPNRERINQ 
       410        420        430        440        450
LLNESLMLVT ALNTHIGYDK AAEIAKKAHK EGLTLKAAAL ALGYLSEAEF 
       460 
DSWVRPEQMV GSMKAGR

Length:467

Mass (Da):50,520

Last modified:June 1, 2003 - v1

Checksum:ⁱ865CBAE31CB2768D

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AE005674 Genomic DNA. Translation: AAN43217.1. AE014073 Genomic DNA. Translation: AAP17104.1.
NCBI Reference Sequences More...RefSeqⁱ	NP_707510.1. NC_004337.2. WP_001099068.1. NZ_MSKF02000043.1.

Genome annotation databases

EnsemblBacteriaⁱ	AAN43217; AAN43217; SF1634. AAP17104; AAP17104; S1765.
GeneIDⁱ	1027791.
KEGGⁱ	sfl:SF1634. sft:NCTC1_01771. sfx:S1765.
PATRICⁱ	fig\|198214.7.peg.1927.

Similar proteinsⁱ

Entry	Cluster members	Organisms	Length	Cluster ID	Cluster name	Size
Q83ML8	I6H3Z9 A0A1W2MU10 D2AGB0 A0A127GK46 Q0T4G5 I6BTI9	Shigella flexneri Shigella flexneri 1235-66 Shigella flexneri serotype X (strain 2002017) Shigella flexneri 4c Shigella flexneri serotype 5b (strain 8401) Shigella flexneri 2850-71	467	UniRef100_Q83ML8	Cluster: Fumarate hydratase class II	7

Entry	Cluster members	Organisms	Length	Cluster ID	Cluster name	Size
Q83ML8	P05042 W1B7T2 A0A024L3D9 F4SJL6 A0A073HGC8 M9GZM5 A0A1X3JG87 A0A073USD0 D6IAS3 T9DCY5 +914	Escherichia coli (strain K12) Klebsiella pneumoniae IS22 Escherichia coli Escherichia coli H736 Escherichia coli 5-366-08_S1_C3 Escherichia coli MP021561.2 Escherichia coli H386 Escherichia coli 5-366-08_S1_C1 Escherichia coli B185 Escherichia coli UMEA 3212-1 And more	467	UniRef90_P05042	Cluster: Fumarate hydratase class II	925

Entry	Cluster members	Organisms	Length	Cluster ID	Cluster name	Size
Q83ML8	P05042 W1B7T2 A0A024L3D9 F4SJL6 A0A073HGC8 M9GZM5 A0A1X3JG87 A0A073USD0 D6IAS3 T9DCY5 +7808	Escherichia coli (strain K12) Klebsiella pneumoniae IS22 Escherichia coli Escherichia coli H736 Escherichia coli 5-366-08_S1_C3 Escherichia coli MP021561.2 Escherichia coli H386 Escherichia coli 5-366-08_S1_C1 Escherichia coli B185 Escherichia coli UMEA 3212-1 And more	467	UniRef50_P05042	Cluster: Fumarate hydratase class II	7,819

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AE005674 Genomic DNA. Translation: AAN43217.1. AE014073 Genomic DNA. Translation: AAP17104.1.
NCBI Reference Sequences More...RefSeqⁱ	NP_707510.1. NC_004337.2. WP_001099068.1. NZ_MSKF02000043.1.

3D structure databases

ProteinModelPortalⁱ	Q83ML8.
SMRⁱ	Q83ML8.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Proteomic databases

PaxDbⁱ	Q83ML8.

PaxDbⁱ

Q83ML8.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAN43217; AAN43217; SF1634. AAP17104; AAP17104; S1765.
GeneIDⁱ	1027791.
KEGGⁱ	sfl:SF1634. sft:NCTC1_01771. sfx:S1765.
PATRICⁱ	fig\|198214.7.peg.1927.

Phylogenomic databases

eggNOGⁱ	ENOG4105C9Q. Bacteria. COG0114. LUCA.
HOGENOMⁱ	HOG000061736.
KEGG Orthology (KO) More...KOⁱ	K01679.
OMAⁱ	VSFTDNC.

Enzyme and pathway databases

UniPathwayⁱ	UPA00223; UER01007.

UniPathwayⁱ

UPA00223; UER01007.

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd01362. Fumarase_classII. 1 hit.
Gene3Dⁱ	1.10.275.10. 1 hit.
HAMAPⁱ	MF_00743. FumaraseC. 1 hit.
InterProⁱ	View protein in InterPro 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.
PANTHERⁱ	PTHR11444. PTHR11444. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF10415. FumaraseC_C. 1 hit. PF00206. Lyase_1. 1 hit.
PRINTSⁱ	PR00149. FUMRATELYASE.
SUPFAMⁱ	SSF48557. SSF48557. 1 hit.
TIGRFAMsⁱ	TIGR00979. fumC_II. 1 hit.
PROSITEⁱ	View protein in PROSITE PS00163. FUMARATE_LYASES. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	FUMC_SHIFL
Accessionⁱ	Q83ML8Primary (citable) accession number: Q83ML8
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
	Last sequence update:	June 1, 2003
	Last modified:	August 30, 2017
	This is version 103 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

UniProtKB

UniParc

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Proteomes

Annotation systems

Supporting data

UniProtKB - Q83ML8 (FUMC_SHIFL)

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Fumarate hydratase class II

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">‘Function’</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: tricarboxylic acid cycle

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

Pathwayⁱ: tricarboxylic acid cycle

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ