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Conserved domains on  [gi|1502692542|ref|WP_122316478|]
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RidA family protein [Pseudomonas cichorii]

Protein Classification

RidA family protein( domain architecture ID 10000806)

RidA (reactive intermediate/imine deaminase A) family protein similar to Pseudomonas sp. 2-aminomuconate deaminase that hydrolyzes 2-aminomuconate to 4-oxalocrotonate, and releases ammonia in the modified meta-cleavage pathway by forming various compounds including acetaldehyde, pyruvic acid, acetyl-CoA, and succinate, that may enter the Krebs cycle

CATH:  3.30.1330.40
PubMed:  14624641|22094463|25975565
SCOP:  3001733

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 1-127 3.73e-37

Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family [Defense mechanisms]; Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family is part of the Pathway/BioSystem: Pyrimidine degradation


:

Pssm-ID: 440021  Cd Length: 125  Bit Score: 122.59  E-value: 3.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692542   1 MSITRYgagSTAGGGQPRPFARAVEADGWLYVSGQVP--AQDGEIiVGGIVEQTHKTLQNLVEILTEAGYELKDVVRVGV 78
Cdd:COG0251     1 MTRELI---NPPAPAPIGPYSQAVRVGNLVFVSGQVPldPDTGEL-GGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTV 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1502692542  79 WLEDPRDFWSFNKVFGEYFsPEHAPARACVQ-ASMMVDCKVEIDCVAYKK 127
Cdd:COG0251    77 YLTDMADFAAVNEVYAEYF-GEGRPARTAVGvAALPKGALVEIEAIAALP 125
 
Name Accession Description Interval E-value
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 1-127 3.73e-37

Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family [Defense mechanisms]; Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440021  Cd Length: 125  Bit Score: 122.59  E-value: 3.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692542   1 MSITRYgagSTAGGGQPRPFARAVEADGWLYVSGQVP--AQDGEIiVGGIVEQTHKTLQNLVEILTEAGYELKDVVRVGV 78
Cdd:COG0251     1 MTRELI---NPPAPAPIGPYSQAVRVGNLVFVSGQVPldPDTGEL-GGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTV 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1502692542  79 WLEDPRDFWSFNKVFGEYFsPEHAPARACVQ-ASMMVDCKVEIDCVAYKK 127
Cdd:COG0251    77 YLTDMADFAAVNEVYAEYF-GEGRPARTAVGvAALPKGALVEIEAIAALP 125
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 20-124 5.21e-37

YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100004 [Multi-domain]  Cd Length: 107  Bit Score: 121.51  E-value: 5.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692542  20 FARAVEADGWLYVSGQVP-AQDGEIIVGGIVEQTHKTLQNLVEILTEAGYELKDVVRVGVWLEDPRDFWSFNKVFGEYFS 98
Cdd:cd00448     1 YSQAVRVGNLVFVSGQIPlDPDGELVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFFG 80

                          90       100
                  ....*....|....*....|....*..
gi 1502692542  99 PEHAPARACVQASMMV-DCKVEIDCVA 124
Cdd:cd00448    81 EGPPPARTAVGVAALPpGALVEIEAIA 107
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 19-126 3.92e-34

reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of protein synthesis intiation, then as an endoribonuclease active on single-stranded mRNA, endoribonuclease L-PSP. Members of this family, conserved in all domains of life and often with several members per bacterial genome, appear to catalyze a reaction that minimizes toxic by-products from reactions catalyzed by pyridoxal phosphate-dependent enzymes. [Cellular processes, Other]


Pssm-ID: 129116  Cd Length: 124  Bit Score: 115.08  E-value: 3.92e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692542  19 PFARAVEADGWLYVSGQVP--AQDGEIIVGGIVEQTHKTLQNLVEILTEAGYELKDVVRVGVWLEDPRDFWSFNKVFGEY 96
Cdd:TIGR00004  15 PYSQAVKVGNTVYVSGQIPldPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTDLNDFAEVNEVYGQY 94

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1502692542  97 FSpEHAPARACVQ-ASMMVDCKVEIDCVAYK 126
Cdd:TIGR00004  95 FD-EHYPARSAVQvAALPKGVLVEIEAIAVK 124
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 19-125 1.89e-32

Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein synthesis by cleavage of mRNA. Previously thought to inhibit protein synthesis initiation. This protein may also be involved in the regulation of purine biosynthesis. YjgF (renamed RidA) family members are enamine/imine deaminases. They hydrolyze reactive intermediates released by PLP-dependent enzymes, including threonine dehydratase. YjgF also prevents inhibition of transaminase B (IlvE) in Salmonella.


Pssm-ID: 426010  Cd Length: 117  Bit Score: 110.47  E-value: 1.89e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692542  19 PFARAVEADGWLYVSGQVP--AQDGEIIVGGIVEQTHKTLQNLVEILTEAGYELKDVVRVGVWLEDPRDFWSFNKVFGEY 96
Cdd:pfam01042   8 PYSQAVKAGNLVYVSGQIPldPDTGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEVNEVYAEY 87

                          90       100       110
                  ....*....|....*....|....*....|
gi 1502692542  97 FSPEHAPARACVQASMMV-DCKVEIDCVAY 125
Cdd:pfam01042  88 FDADKAPARSAVGVAALPlGALVEIEAIAV 117
PRK11401 PRK11401
enamine/imine deaminase;
19-126 4.52e-16

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 68.94  E-value: 4.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692542  19 PFARAVEADGWLYVSGQVPA--QDGEIiVGGIVEQTHKTLQNLVEILTEAGYELKDVVRVGVWLEDPRDFWSFNKVFGEY 96
Cdd:PRK11401   16 PYVQGVDLGSMVFTSGQIPVcpQTGEI-PADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDLNDFATINEVYKQF 94

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1502692542  97 FSPEHA--PARACVQ-ASMMVDCKVEIDCVAYK 126
Cdd:PRK11401   95 FDEHQAtyPTRSCVQvARLPKDVKLEIEAIAVR 127
 
Name Accession Description Interval E-value
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 1-127 3.73e-37

Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family [Defense mechanisms]; Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440021  Cd Length: 125  Bit Score: 122.59  E-value: 3.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692542   1 MSITRYgagSTAGGGQPRPFARAVEADGWLYVSGQVP--AQDGEIiVGGIVEQTHKTLQNLVEILTEAGYELKDVVRVGV 78
Cdd:COG0251     1 MTRELI---NPPAPAPIGPYSQAVRVGNLVFVSGQVPldPDTGEL-GGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTV 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1502692542  79 WLEDPRDFWSFNKVFGEYFsPEHAPARACVQ-ASMMVDCKVEIDCVAYKK 127
Cdd:COG0251    77 YLTDMADFAAVNEVYAEYF-GEGRPARTAVGvAALPKGALVEIEAIAALP 125
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 20-124 5.21e-37

YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100004 [Multi-domain]  Cd Length: 107  Bit Score: 121.51  E-value: 5.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692542  20 FARAVEADGWLYVSGQVP-AQDGEIIVGGIVEQTHKTLQNLVEILTEAGYELKDVVRVGVWLEDPRDFWSFNKVFGEYFS 98
Cdd:cd00448     1 YSQAVRVGNLVFVSGQIPlDPDGELVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFFG 80

                          90       100
                  ....*....|....*....|....*..
gi 1502692542  99 PEHAPARACVQASMMV-DCKVEIDCVA 124
Cdd:cd00448    81 EGPPPARTAVGVAALPpGALVEIEAIA 107
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 19-126 3.92e-34

reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of protein synthesis intiation, then as an endoribonuclease active on single-stranded mRNA, endoribonuclease L-PSP. Members of this family, conserved in all domains of life and often with several members per bacterial genome, appear to catalyze a reaction that minimizes toxic by-products from reactions catalyzed by pyridoxal phosphate-dependent enzymes. [Cellular processes, Other]


Pssm-ID: 129116  Cd Length: 124  Bit Score: 115.08  E-value: 3.92e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692542  19 PFARAVEADGWLYVSGQVP--AQDGEIIVGGIVEQTHKTLQNLVEILTEAGYELKDVVRVGVWLEDPRDFWSFNKVFGEY 96
Cdd:TIGR00004  15 PYSQAVKVGNTVYVSGQIPldPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTDLNDFAEVNEVYGQY 94

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1502692542  97 FSpEHAPARACVQ-ASMMVDCKVEIDCVAYK 126
Cdd:TIGR00004  95 FD-EHYPARSAVQvAALPKGVLVEIEAIAVK 124
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 19-125 1.89e-32

Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein synthesis by cleavage of mRNA. Previously thought to inhibit protein synthesis initiation. This protein may also be involved in the regulation of purine biosynthesis. YjgF (renamed RidA) family members are enamine/imine deaminases. They hydrolyze reactive intermediates released by PLP-dependent enzymes, including threonine dehydratase. YjgF also prevents inhibition of transaminase B (IlvE) in Salmonella.


Pssm-ID: 426010  Cd Length: 117  Bit Score: 110.47  E-value: 1.89e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692542  19 PFARAVEADGWLYVSGQVP--AQDGEIIVGGIVEQTHKTLQNLVEILTEAGYELKDVVRVGVWLEDPRDFWSFNKVFGEY 96
Cdd:pfam01042   8 PYSQAVKAGNLVYVSGQIPldPDTGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEVNEVYAEY 87

                          90       100       110
                  ....*....|....*....|....*....|
gi 1502692542  97 FSPEHAPARACVQASMMV-DCKVEIDCVAY 125
Cdd:pfam01042  88 FDADKAPARSAVGVAALPlGALVEIEAIAV 117
YjgF_YER057c_UK114_like_2 cd06150
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 20-124 1.52e-23

This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100007  Cd Length: 105  Bit Score: 87.21  E-value: 1.52e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692542  20 FARAVEADGWLYVSGQVPAQDGeiivGGIVEQTHKTLQNLVEILTEAGYELKDVVRVGVWLEDPRDFWSFNKVFGEYFSP 99
Cdd:cd06150     3 MSQAVVHNGTVYLAGQVADDTS----ADITGQTRQVLAKIDALLAEAGSDKSRILSATIWLADMADFAAMNAVWDAWVPP 78

                          90       100
                  ....*....|....*....|....*.
gi 1502692542 100 EHAPARACVQASMM-VDCKVEIDCVA 124
Cdd:cd06150    79 GHAPARACVEAKLAdPGYLVEIVVTA 104
YjgF_YER057c_UK114_like_6 cd06154
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 20-124 2.57e-20

This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100011  Cd Length: 119  Bit Score: 79.52  E-value: 2.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692542  20 FARAVEADGWLYVSGQVP-AQDGEIIVGGIVEQTHKTLQNLVEILTEAGYELKDVVRVGVWLEDPRDFWSFNKVFGEYFS 98
Cdd:cd06154    13 YSRAVRVGNWVFVSGTTGyDYDGMVMPGDAYEQTRQCLEIIEAALAEAGASLEDVVRTRMYVTDIADFEAVGRAHGEVFG 92

                          90       100
                  ....*....|....*....|....*...
gi 1502692542  99 pEHAPARACVQASMMVD--CKVEIDCVA 124
Cdd:cd06154    93 -DIRPAATMVVVSLLVDpeMLVEIEVTA 119
eu_AANH_C_1 cd06155
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 28-125 3.59e-19

A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine nucleotide alpha hydrolase (AANH)-like domain located N-terminal to two distinctly different YjgF-YER057c-UK114-like domains. This CD contains the first of these domains. The YjgF-YER057c-UK114 protein family is a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100012  Cd Length: 101  Bit Score: 76.14  E-value: 3.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692542  28 GWLYVSGQVPAQDGEiivgGIVEQTHKTLQNLVEILTEAGYELKDVVRVGVWLEDPRDFWSFNKVFGEYFSPEHAPARAC 107
Cdd:cd06155     8 GLLWISNVTASESDE----TVEEQMESIFSKLREILQSNGLSLSDILYVTLYLRDMSDFAEVNSVYGTFFDKPNPPSRVC 83

                          90
                  ....*....|....*...
gi 1502692542 108 VQASMMVDCKVEIDCVAY 125
Cdd:cd06155    84 VECGLPEGCDVQLSCVAA 101
PRK11401 PRK11401
enamine/imine deaminase;
19-126 4.52e-16

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 68.94  E-value: 4.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692542  19 PFARAVEADGWLYVSGQVPA--QDGEIiVGGIVEQTHKTLQNLVEILTEAGYELKDVVRVGVWLEDPRDFWSFNKVFGEY 96
Cdd:PRK11401   16 PYVQGVDLGSMVFTSGQIPVcpQTGEI-PADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDLNDFATINEVYKQF 94

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1502692542  97 FSPEHA--PARACVQ-ASMMVDCKVEIDCVAYK 126
Cdd:PRK11401   95 FDEHQAtyPTRSCVQvARLPKDVKLEIEAIAVR 127
RutC TIGR03610
pyrimidine utilization protein C; This protein is observed in operons extremely similar to ...
 12-125 1.90e-15

pyrimidine utilization protein C; This protein is observed in operons extremely similar to that characterized in E. coli K-12 responsible for the import and catabolism of pyrimidines, primarily uracil. This protein is a member of the endoribonuclease L-PSP family defined by pfam01042.


Pssm-ID: 274677  Cd Length: 127  Bit Score: 67.18  E-value: 1.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692542  12 AGGGQP-RPFARAVEADGWLYVSGQVP-AQDGEII-VGGIVEQTHKTLQNLVEILTEAGYELKDVVRVGVWLEDPRDFWS 88
Cdd:TIGR03610   9 AGTSKPlAPFVPGTLADGVVYVSGTLPfDKDNNVVhVGDAAAQTRHVLETIKSVIETAGGTMDDVTFNHIFIRDWADYAA 88

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1502692542  89 FNKVFGEYFsPEHAPARACVQASMMV-DCKVEIDCVAY 125
Cdd:TIGR03610  89 INEVYAEYF-PGEKPARYCIQCGLVKpDALVEIASVAH 125
YjgH_like cd02198
YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, ...
 20-126 4.30e-11

YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100005  Cd Length: 111  Bit Score: 55.73  E-value: 4.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692542  20 FARAVEADGWLYVSGQVPAQDGEIIVGGIVEQTHKTLQNLVEILTEAGYELKDVVRVGVWLEDP-RDFWSFNKVFGEYFS 98
Cdd:cd02198     3 YSPAVRVGDTLFVSGQVGSDADGSVAEDFEAQFRLAFQNLGAVLEAAGCSFDDVVELTTFHVDMaAHLPAFAAVKDEYFK 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1502692542  99 PEHaPARACVQASMMVDCK--VEIDCVAYK 126
Cdd:cd02198    83 EPY-PAWTAVGVAWLARPGllVEIKVVAVR 111
YjgF_YER057c_UK114_like_3 cd06151
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 20-124 1.07e-08

This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100008  Cd Length: 126  Bit Score: 49.63  E-value: 1.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692542  20 FARAVEADG---WLYVSGQVP------AQDGEIIVGGIVE-QTHKTLQNLVEILTEAGYELKDVVRVGVWL-EDPR---- 84
Cdd:cd06151     1 IAQAVEVPAgaaTIYLSGTVPavvnasAPKGSPARYGDTEtQTISVLKRIETILQSQGLTMGDVVKMRVFLvADPAldgk 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1502692542  85 -DFWSFNKVFGEYFSPEHAP---ARACVQASMMV--DCKVEIDCVA 124
Cdd:cd06151    81 mDFAGFMKAYRQFFGTAEQPnkpARSTLQVAGLVnpGWLVEIEVVA 126
YjgF_YER057c_UK114_like_5 cd06153
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 20-124 2.01e-08

This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100010  Cd Length: 114  Bit Score: 48.79  E-value: 2.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692542  20 FARAVEAD----GWLYVSGQ---VPAqdGEIIVGGIVEQTHKTLQNLVEILTEAG-----YELKDVVRVGVWLEDPRDFW 87
Cdd:cd06153     1 FSRATLLAaggrTHLFISGTasiVGH--GTVHPGDVEAQTRETLENIEALLEAAGrgggaQFLADLLRLKVYLRDREDLP 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1502692542  88 SFNKVFGEYFSPEHapARACVQASMmvdCK----VEIDCVA 124
Cdd:cd06153    79 AVRAILAARLGPAV--PAVFLQADV---CRpdllVEIEAVA 114
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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