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Conserved domains on  [gi|489600732|ref|WP_003505173|]
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RidA family protein [[Clostridium] symbiosum]

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 ...
 1-122 1.89e-41

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: 133.38  E-value: 1.89e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489600732   1 MKQVFNENSPS--GHYTPGMISNGVLYISGQTSADPATGLPAvGGIEAETKMALAKMESVLKAAGCEKEDVVMCRIYVSS 78
Cdd:COG0251    2 TRELINPPAPApiGPYSQAVRVGNLVFVSGQVPLDPDTGELG-GDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489600732  79 MDYWGDVNKVYSEFFGEHKPARIVLPVGRLNKGCLLELEATAEV 122
Cdd:COG0251   81 MADFAAVNEVYAEYFGEGRPARTAVGVAALPKGALVEIEAIAAL 124
 
Name Accession Description Interval E-value
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 1-122 1.89e-41

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: 133.38  E-value: 1.89e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489600732   1 MKQVFNENSPS--GHYTPGMISNGVLYISGQTSADPATGLPAvGGIEAETKMALAKMESVLKAAGCEKEDVVMCRIYVSS 78
Cdd:COG0251    2 TRELINPPAPApiGPYSQAVRVGNLVFVSGQVPLDPDTGELG-GDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489600732  79 MDYWGDVNKVYSEFFGEHKPARIVLPVGRLNKGCLLELEATAEV 122
Cdd:COG0251   81 MADFAAVNEVYAEYFGEGRPARTAVGVAALPKGALVEIEAIAAL 124
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 14-120 2.97e-38

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: 124.59  E-value: 2.97e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489600732  14 YTPGMISNGVLYISGQTSADPATGLpAVGGIEAETKMALAKMESVLKAAGCEKEDVVMCRIYVSSMDYWGDVNKVYSEFF 93
Cdd:cd00448    1 YSQAVRVGNLVFVSGQIPLDPDGEL-VPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFF 79

                         90       100
                 ....*....|....*....|....*...
gi 489600732  94 GE-HKPARIVLPVGRLNKGCLLELEATA 120
Cdd:cd00448   80 GEgPPPARTAVGVAALPPGALVEIEAIA 107
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 6-121 2.58e-33

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: 112.39  E-value: 2.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489600732    6 NENSPSGHYTPGMISNGVLYISGQTSADPATGLPAVGGIEAETKMALAKMESVLKAAGCEKEDVVMCRIYVSSMDYWGDV 85
Cdd:pfam01042   1 NAPAAAGPYSQAVKAGNLVYVSGQIPLDPDTGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 489600732   86 NKVYSEFFGEHK-PARIVLPVGRLNKGCLLELEATAE 121
Cdd:pfam01042  81 NEVYAEYFDADKaPARSAVGVAALPLGALVEIEAIAV 117
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 1-122 4.07e-32

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: 109.69  E-value: 4.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489600732    1 MKQVFNENSPS--GHYTPGMISNGVLYISGQTSADPATGLPAVGGIEAETKMALAKMESVLKAAGCEKEDVVMCRIYVSS 78
Cdd:TIGR00004   1 KKIISTDKAPAaiGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 489600732   79 MDYWGDVNKVYSEFFGEHKPARIVLPVGRLNKGCLLELEATAEV 122
Cdd:TIGR00004  81 LNDFAEVNEVYGQYFDEHYPARSAVQVAALPKGVLVEIEAIAVK 124
PRK11401 PRK11401
enamine/imine deaminase;
1-120 2.29e-13

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 62.01  E-value: 2.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489600732   1 MKQVF-NENSPS--GHYTPGMISNGVLYISGQTSADPATG-LPAvgGIEAETKMALAKMESVLKAAGCEKEDVVMCRIYV 76
Cdd:PRK11401   1 MKKIIeTQRAPGaiGPYVQGVDLGSMVFTSGQIPVCPQTGeIPA--DVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFI 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489600732  77 SSMDYWGDVNKVYSEFFGEHK---PARIVLPVGRLNKGCLLELEATA 120
Cdd:PRK11401  79 TDLNDFATINEVYKQFFDEHQatyPTRSCVQVARLPKDVKLEIEAIA 125
 
Name Accession Description Interval E-value
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 1-122 1.89e-41

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: 133.38  E-value: 1.89e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489600732   1 MKQVFNENSPS--GHYTPGMISNGVLYISGQTSADPATGLPAvGGIEAETKMALAKMESVLKAAGCEKEDVVMCRIYVSS 78
Cdd:COG0251    2 TRELINPPAPApiGPYSQAVRVGNLVFVSGQVPLDPDTGELG-GDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489600732  79 MDYWGDVNKVYSEFFGEHKPARIVLPVGRLNKGCLLELEATAEV 122
Cdd:COG0251   81 MADFAAVNEVYAEYFGEGRPARTAVGVAALPKGALVEIEAIAAL 124
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 14-120 2.97e-38

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: 124.59  E-value: 2.97e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489600732  14 YTPGMISNGVLYISGQTSADPATGLpAVGGIEAETKMALAKMESVLKAAGCEKEDVVMCRIYVSSMDYWGDVNKVYSEFF 93
Cdd:cd00448    1 YSQAVRVGNLVFVSGQIPLDPDGEL-VPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFF 79

                         90       100
                 ....*....|....*....|....*...
gi 489600732  94 GE-HKPARIVLPVGRLNKGCLLELEATA 120
Cdd:cd00448   80 GEgPPPARTAVGVAALPPGALVEIEAIA 107
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 6-121 2.58e-33

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: 112.39  E-value: 2.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489600732    6 NENSPSGHYTPGMISNGVLYISGQTSADPATGLPAVGGIEAETKMALAKMESVLKAAGCEKEDVVMCRIYVSSMDYWGDV 85
Cdd:pfam01042   1 NAPAAAGPYSQAVKAGNLVYVSGQIPLDPDTGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 489600732   86 NKVYSEFFGEHK-PARIVLPVGRLNKGCLLELEATAE 121
Cdd:pfam01042  81 NEVYAEYFDADKaPARSAVGVAALPLGALVEIEAIAV 117
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 1-122 4.07e-32

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: 109.69  E-value: 4.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489600732    1 MKQVFNENSPS--GHYTPGMISNGVLYISGQTSADPATGLPAVGGIEAETKMALAKMESVLKAAGCEKEDVVMCRIYVSS 78
Cdd:TIGR00004   1 KKIISTDKAPAaiGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 489600732   79 MDYWGDVNKVYSEFFGEHKPARIVLPVGRLNKGCLLELEATAEV 122
Cdd:TIGR00004  81 LNDFAEVNEVYGQYFDEHYPARSAVQVAALPKGVLVEIEAIAVK 124
YjgF_YER057c_UK114_like_6 cd06154
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 24-120 1.81e-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: 79.91  E-value: 1.81e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489600732  24 LYISGQTSADPATGLpAVGGIEAETKMALAKMESVLKAAGCEKEDVVMCRIYVSSMDYWGDVNKVYSEFFGEHKPARIVL 103
Cdd:cd06154   23 VFVSGTTGYDYDGMV-MPGDAYEQTRQCLEIIEAALAEAGASLEDVVRTRMYVTDIADFEAVGRAHGEVFGDIRPAATMV 101

                         90
                 ....*....|....*...
gi 489600732 104 PVGRL-NKGCLLELEATA 120
Cdd:cd06154  102 VVSLLvDPEMLVEIEVTA 119
YjgF_YER057c_UK114_like_2 cd06150
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 19-120 9.14e-19

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: 74.88  E-value: 9.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489600732  19 ISNGVLYISGQTSADPAtglpavGGIEAETKMALAKMESVLKAAGCEKEDVVMCRIYVSSMDYWGDVNKVYSEFFGE-HK 97
Cdd:cd06150    8 VHNGTVYLAGQVADDTS------ADITGQTRQVLAKIDALLAEAGSDKSRILSATIWLADMADFAAMNAVWDAWVPPgHA 81

                         90       100
                 ....*....|....*....|...
gi 489600732  98 PARIVLPVGRLNKGCLLELEATA 120
Cdd:cd06150   82 PARACVEAKLADPGYLVEIVVTA 104
YjgH_like cd02198
YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, ...
 13-120 2.97e-14

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: 63.82  E-value: 2.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489600732  13 HYTPGMISNGVLYISGQTSADPATGLPavGGIEAETKMALAKMESVLKAAGCEKEDVVMCRIY-VSSMDYWGDVNKVYSE 91
Cdd:cd02198    2 GYSPAVRVGDTLFVSGQVGSDADGSVA--EDFEAQFRLAFQNLGAVLEAAGCSFDDVVELTTFhVDMAAHLPAFAAVKDE 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 489600732  92 FFGEHKPARIVLPVGRL-NKGCLLELEATA 120
Cdd:cd02198   80 YFKEPYPAWTAVGVAWLaRPGLLVEIKVVA 109
PRK11401 PRK11401
enamine/imine deaminase;
1-120 2.29e-13

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 62.01  E-value: 2.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489600732   1 MKQVF-NENSPS--GHYTPGMISNGVLYISGQTSADPATG-LPAvgGIEAETKMALAKMESVLKAAGCEKEDVVMCRIYV 76
Cdd:PRK11401   1 MKKIIeTQRAPGaiGPYVQGVDLGSMVFTSGQIPVCPQTGeIPA--DVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFI 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489600732  77 SSMDYWGDVNKVYSEFFGEHK---PARIVLPVGRLNKGCLLELEATA 120
Cdd:PRK11401  79 TDLNDFATINEVYKQFFDEHQatyPTRSCVQVARLPKDVKLEIEAIA 125
YjgF_YER057c_UK114_like_3 cd06151
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 23-120 1.98e-12

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: 59.26  E-value: 1.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489600732  23 VLYISGQT-----SADPATGLPAVGGIEAETKMALAKMESVLKAAGCEKEDVVMCRIYV-------SSMDYWGdVNKVYS 90
Cdd:cd06151   13 TIYLSGTVpavvnASAPKGSPARYGDTETQTISVLKRIETILQSQGLTMGDVVKMRVFLvadpaldGKMDFAG-FMKAYR 91

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489600732  91 EFFG----EHKPARIVLPVGRL-NKGCLLELEATA 120
Cdd:cd06151   92 QFFGtaeqPNKPARSTLQVAGLvNPGWLVEIEVVA 126
eu_AANH_C_1 cd06155
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 20-120 9.13e-12

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: 56.88  E-value: 9.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489600732  20 SNGVLYISGQTSadPATGlpavGGIEAETKMALAKMESVLKAAGCEKEDVVMCRIYVSSMDYWGDVNKVYSEFFGEHKP- 98
Cdd:cd06155    6 TGGLLWISNVTA--SESD----ETVEEQMESIFSKLREILQSNGLSLSDILYVTLYLRDMSDFAEVNSVYGTFFDKPNPp 79

                         90       100
                 ....*....|....*....|..
gi 489600732  99 ARIVLPVGrLNKGCLLELEATA 120
Cdd:cd06155   80 SRVCVECG-LPEGCDVQLSCVA 100
YjgF_YER057c_UK114_like_1 cd02199
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 10-121 3.58e-06

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: 100006  Cd Length: 142  Bit Score: 43.22  E-value: 3.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489600732  10 PSGHYTPGMISNGVLYISGQTSADPATGLPA--VG-------GIEAeTKMALAKMESVLKAAGCEKEDVVmcRI-----Y 75
Cdd:cd02199   12 PVGNYVPAVRTGNLLYVSGQLPRVDGKLVYTgkVGadlsveeGQEA-ARLCALNALAALKAALGDLDRVK--RVvrltgF 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489600732  76 VSSMDYWGDVNKV---YSEF----FGEH-KPARIVLPVGRLNKGCLLELEATAE 121
Cdd:cd02199   89 VNSAPDFTEQPKVangASDLlvevFGEAgRHARSAVGVASLPLNAAVEVEAIVE 142
YjgF_YER057c_UK114_like_4 cd06152
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 13-120 1.61e-05

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: 100009  Cd Length: 114  Bit Score: 41.14  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489600732  13 HYTPGMISNGVLYISGQTSADPATG-LPAVggIEAETKMALAKMESVLKAAGCEK-EDVVMCRIY---VSSMDYWGDVNK 87
Cdd:cd06152    2 HYSQAVRIGDRIEISGQGGWDPDTGkIPED--LEEEIDQAFDNVELALKAAGGKGwEQVYKVNSYhvdIKNEEAFGLMVE 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 489600732  88 VYSEFFGEHKPARIVLPVGRLN-KGCLLELEATA 120
Cdd:cd06152   80 NFKKWMPNHQPIWTCVGVTALGlPGMRVEIEVDA 113
eu_AANH_C_2 cd06156
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 14-124 6.65e-05

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 second 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: 100013  Cd Length: 118  Bit Score: 39.23  E-value: 6.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489600732  14 YTPGMISNGVLYISGQTSADPATGLPAVGGIEAETKMALAKMESVLKAAGCekEDVVMCRIYVSSMDYWGDVNKVYSEFF 93
Cdd:cd06156    1 YSQAIVVPKVAYISGQIGLIPATMTLLEGGITLQAVLSLQHLERVAKAMNV--QWVLAAVCYVTDESSVPIARSAWSKYC 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 489600732  94 GEHKPARIVLPVGRLNKGCLLeleaTAEVHE 124
Cdd:cd06156   79 SELDLEDESRNESDDVNPPLV----IVVVPE 105
ASKHA_NBD_FGGY_RBK-like cd07768
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ...
 9-111 4.40e-03

nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family includes bacterial RBK, vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein), Saccharomyces cerevisiae D-ribulokinase YDR109C, and Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466788 [Multi-domain]  Cd Length: 522  Bit Score: 35.68  E-value: 4.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489600732   9 SPSGHYTPGMISNGVLYISGQTSA---DPATGLPAVGGIEAETKMALAKMESVLKAAGCEKEDVV--MCRIYVSSM--DY 81
Cdd:cd07768  226 TTSGVALPEMAEKMGLHPGTAVVVsciDAHASWFAVASPHLETSLFMIAGTSSCHMYGTTISDRIpgVWGPFDTIIdpDY 305

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489600732  82 WGD------VNKVYSEFFGEHKPARIVLPVgrLNKG 111
Cdd:cd07768  306 SVYeagqsaTGKLIEHLFESHPCARKFDEA--LKKG 339
 
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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