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Links from Protein

Items: 6

1.

fumarate hydratase C-terminal domain-containing protein

This family consists of the C terminal region of several bacterial fumarate hydratase proteins (FumA and FumB). Fumarase, or fumarate hydratase (EC 4.2.1.2), is a component of the citric acid cycle. In facultative anaerobes such as Escherichia coli, fumarase also engages in the reductive pathway from oxaloacetate to succinate during anaerobic growth [1]. [1]. 11133938. Oxygen- and growth rate-dependent regulation of Escherichia coli fumarase (FumA, FumB, and FumC) activity. Tseng CP, Yu CC, Lin HH, Chang CY, Kuo JT;. J Bacteriol 2001;183:461-467. (from Pfam)

GO Terms:
Molecular Function:
hydro-lyase activity (GO:0016836)
Date:
2024-10-16
Family Accession:
NF017494.5
Method:
HMM
2.
new record, indexing in progress
Family Accession:
3.
new record, indexing in progress
Family Accession:
4.

L(+)-tartrate dehydratase subunit beta

L(+)-tartrate dehydratase (L-TTD) catalyzes the conversion from (R,R)-tartrate to oxaloacetate

Date:
2019-06-24
Family Accession:
10013023
Method:
Sparcle
5.

L(+)-tartrate dehydratase subunit beta

Involved in the tartrate degradation pathway

Gene:
ttdB
GO Terms:
Molecular Function:
hydro-lyase activity (GO:0016836)
Date:
2022-02-09
Family Accession:
NF006082.0
Method:
HMM
6.

FumA C-terminus/TtdB family hydratase beta subunit

A number of Fe-S cluster-containing hydro-lyases share a conserved motif, including argininosuccinate lyase, adenylosuccinate lyase, aspartase, class I fumarate hydratase (fumarase), and tartrate dehydratase (see PROSITE:PDOC00147). This model represents a subset of closely related proteins or modules, including the E. coli tartrate dehydratase beta chain and the C-terminal region of the class I fumarase (where the N-terminal region is homologous to the tartrate dehydratase alpha chain). The activity of archaeal proteins in this subfamily has not been established.

GO Terms:
Molecular Function:
hydro-lyase activity (GO:0016836)
Date:
2022-03-28
Family Accession:
TIGR00723.1
Method:
HMM
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