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Items: 18

1.

PutA, RHH domain

This domain is found in the Bifunctional protein PutA from Escherichia coli and similar sequences mainly found in proteobacteria. PutA is both a bifunctional proline catabolic enzyme that oxidises proline to glutamate for use as a carbon and nitrogen source and an autogenous transcriptional repressor of the put operon. This entry represents the N-terminal ribbon-helix-helix (RHH) domain, which consists of a beta-strand and two alpha-helices. This domain has a Lys at the end of the beta-strand that interacts directly with DNA bases through the major groove, contributing to transcriptional regulation [1,3]. Paper describing PDB structure 2ay0. [1]. 17001030. Crystal structures of the DNA-binding domain of Escherichia coli proline utilization A flavoprotein and analysis of the role of Lys9 in DNA recognition. Larson JD, Jenkins JL, Schuermann JP, Zhou Y, Becker DF, Tanner JJ;. Protein Sci. 2006;15:2630-2641. Paper describing PDB structure 2jxg. [2]. 18767154. Solution structure of the Pseudomonas putida protein PpPutA45 and its DNA complex. Halouska S, Zhou Y, Becker DF, Powers R;. Proteins. 2009;75:12-27. Paper describing PDB structure 2rbf. [3]. 18586269. Structural basis of the transcriptional regulation of the proline utilization regulon by multifunctional PutA. Zhou Y, Larson JD, Bottoms CA, Arturo EC, Henzl MT, Jenkins JL, Nix JC, Becker DF, Tanner JJ;. J Mol Biol. 2008;381:174-188. Paper describing PDB structure 4o8a. [4]. 12514740. Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein. Lee YH, Nadaraia S, Gu D, Becker DF, Tanner JJ;. Nat Struct Biol. 2003;10:109-114. (from Pfam)

Date:
2024-10-16

Family Accession:
NF044868.2
Method:
HMM

2.

Proline utilization A proline dehydrogenase N-terminal domain

This is the N-terminal domain found in Proline utilization A (PutA) proteins. Proline utilization A (PutA) is a flavoprotein that has mutually exclusive roles as a transcriptional repressor of the put regulon and a membrane-associated enzyme that catalyzes the oxidation of proline to glutamate [4]. The N-terminal region carries the flavoenzyme proline dehydrogenase (PRODH) domain which catalyzes the 2-electron oxidation of proline with the concomitant reduction of a flavin cofactor [9]. [1]. 15449943. Structures of the Escherichia coli PutA proline dehydrogenase domain in complex with competitive inhibitors. Zhang M, White TA, Schuermann JP, Baban BA, Becker DF, Tanner JJ;. Biochemistry. 2004;43:12539-12548. [2]. 17209558. Redox-induced changes in flavin structure and roles of flavin N(5) and the ribityl 2'-OH group in regulating PutA--membrane binding. Zhang W, Zhang M, Zhu W, Zhou Y, Wanduragala S, Rewinkel D, Tanner JJ, Becker DF;. Biochemistry. 2007;46:483-491. [3]. 19140736. A conserved active site tyrosine residue of proline dehydrogenase helps enforce the preference for proline over hydroxyproline as the substrate. Ostrander EL, Larson JD, Schuermann JP, Tanner JJ;. Biochemistry. 2009;48:951-959. [4]. 19994913. The structure of the proline utilization a proline dehydrogenase domain inactivated by N-propargylglycine provides insight into conformational changes induced by substrate binding and flavin reduction. Srivastava D, Zhu W, Johnson WH Jr, Whitman CP, Becker DF, Tanner JJ;. Biochemistry. 2010;49:560-569. [5]. 23713611. Involvement of the beta3-alpha3 loop of the proline dehydrogenase domain in allosteric regula. TRUNCATED at 1650 bytes (from Pfam)

Date:
2024-10-16

Family Accession:
NF037209.5
Method:
HMM

3.

DNA-binding domain of Proline dehydrogenase

This domain lies at the N-terminus of bifunctional proline-dehydrogenases and is found to bind DNA. [1]. 12514740. Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein. Lee YH, Nadaraia S, Gu D, Becker DF, Tanner JJ;. Nat Struct Biol. 2003;10:109-114. (from Pfam)

GO Terms:
Molecular Function:
1-pyrroline-5-carboxylate dehydrogenase activity (GO:0003842)
Date:
2024-10-16

Family Accession:
NF026200.5
Method:
HMM

4.

proline dehydrogenase family protein

Date:
2024-08-14

Family Accession:
NF013761.5
Method:
HMM

5.

aldehyde dehydrogenase family protein

This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases Swiss:P00352 EC:1.2.1.3. Succinate-semialdehyde dehydrogenase Swiss:P25526 EC:1.2.1.16. Lactaldehyde dehydrogenase Swiss:P25553 EC:1.2.1.22. Benzaldehyde dehydrogenase Swiss:P43503 EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase Swiss:Q02252 EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase Swiss:P81406 EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase Swiss:P30038 EC: 1.5.1.12. Acetaldehyde dehydrogenase Swiss:P17547 EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase Swiss:P07004 EC:1.2.1.41. This family also includes omega crystallin Swiss:P30842 an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity. [1]. 9195888. Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion. Steinmetz CG, Xie P, Weiner H, Hurley TD;. Structure 1997;5:701-711. (from Pfam)

GO Terms:
Molecular Function:
oxidoreductase activity (GO:0016491)
Date:
2024-10-16

Family Accession:
NF012398.5
Method:
HMM

6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.
new record, indexing in progress
Family Accession:
11.
new record, indexing in progress
Family Accession:
12.
new record, indexing in progress
Family Accession:
13.
new record, indexing in progress
Family Accession:
14.
new record, indexing in progress
Family Accession:
15.

bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA

Proline utilization protein A; multifunctional protein that functions in proline catabolism in the first two enzymatic steps resulting in the conversion of proline to glutamate

Gene:
putA
GO Terms:
Molecular Function:
DNA-binding transcription factor activity (GO:0003700)
Molecular Function:
1-pyrroline-5-carboxylate dehydrogenase activity (GO:0003842)
Molecular Function:
proline dehydrogenase activity (GO:0004657)
Biological Process:
regulation of DNA-templated transcription (GO:0006355)
Biological Process:
proline catabolic process to glutamate (GO:0010133)
Molecular Function:
oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor (GO:0016620)
Date:
2021-07-30

Family Accession:
NF008869.0
Method:
HMM

16.

trifunctional transcriptional regulator/proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase

Gene:
putA
GO Terms:
Molecular Function:
DNA-binding transcription factor activity (GO:0003700)
Molecular Function:
1-pyrroline-5-carboxylate dehydrogenase activity (GO:0003842)
Molecular Function:
proline dehydrogenase activity (GO:0004657)
Biological Process:
regulation of DNA-templated transcription (GO:0006355)
Biological Process:
proline biosynthetic process (GO:0006561)
Molecular Function:
oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor (GO:0016620)
Date:
2021-07-28

Family Accession:
NF008772.0
Method:
HMM

17.

L-glutamate gamma-semialdehyde dehydrogenase

This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase.

GO Terms:
Molecular Function:
1-pyrroline-5-carboxylate dehydrogenase activity (GO:0003842)
Biological Process:
proline biosynthetic process (GO:0006561)
Date:
2024-06-04

Family Accession:
TIGR01238.1
Method:
HMM

18.

trifunctional transcriptional regulator/proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase

trifunctional transcriptional regulator/proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA functions as a transcriptional repressor of the put operon and also has two enzymatic activities (proline dehydrogenase and L-glutamate gamma-semialdehyde dehydrogenase), catalyzing the two-step oxidation of proline to glutamate

Date:
2018-05-03

Family Accession:
11485522
Method:
Sparcle

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