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Conserved domains on  [gi|489119392|ref|WP_003029233|]
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MULTISPECIES: RidA family protein [Citrobacter]

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 ...
 15-129 5.09e-40

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: 129.91  E-value: 5.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489119392  15 PPAGHYSHSTTAGGFVFISGQLPVTfDGEKKADASFEDQTRLVLQNIDACLAGAGVSRQHLVSVRVYVTDMNQWPTFNKI 94
Cdd:COG0251   12 APIGPYSQAVRVGNLVFVSGQVPLD-PDTGELGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTDMADFAAVNEV 90

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489119392  95 YGEWIGDFRPSRAVAGVAELHYGFALEVEAMALAP 129
Cdd:COG0251   91 YAEYFGEGRPARTAVGVAALPKGALVEIEAIAALP 125
 
Name Accession Description Interval E-value
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 15-129 5.09e-40

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: 129.91  E-value: 5.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489119392  15 PPAGHYSHSTTAGGFVFISGQLPVTfDGEKKADASFEDQTRLVLQNIDACLAGAGVSRQHLVSVRVYVTDMNQWPTFNKI 94
Cdd:COG0251   12 APIGPYSQAVRVGNLVFVSGQVPLD-PDTGELGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTDMADFAAVNEV 90

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489119392  95 YGEWIGDFRPSRAVAGVAELHYGFALEVEAMALAP 129
Cdd:COG0251   91 YAEYFGEGRPARTAVGVAALPKGALVEIEAIAALP 125
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 20-126 2.56e-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: 122.67  E-value: 2.56e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489119392  20 YSHSTTAGGFVFISGQLPVTFDGEKKADaSFEDQTRLVLQNIDACLAGAGVSRQHLVSVRVYVTDMNQWPTFNKIYGEWI 99
Cdd:cd00448    1 YSQAVRVGNLVFVSGQIPLDPDGELVPG-DIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFF 79

                         90       100
                 ....*....|....*....|....*...
gi 489119392 100 GDF-RPSRAVAGVAELHYGFALEVEAMA 126
Cdd:cd00448   80 GEGpPPARTAVGVAALPPGALVEIEAIA 107
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 13-126 3.51e-35

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: 117.40  E-value: 3.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489119392   13 SFPPAGHYSHSTTAGGFVFISGQLPVTFDGEKKADASFEDQTRLVLQNIDACLAGAGVSRQHLVSVRVYVTDMNQWPTFN 92
Cdd:pfam01042   2 APAAAGPYSQAVKAGNLVYVSGQIPLDPDTGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEVN 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 489119392   93 KIYGEWI-GDFRPSRAVAGVAELHYGFALEVEAMA 126
Cdd:pfam01042  82 EVYAEYFdADKAPARSAVGVAALPLGALVEIEAIA 116
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 15-126 5.19e-31

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: 107.00  E-value: 5.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489119392   15 PPAGHYSHSTTAGGFVFISGQLPVTFDGEKKADASFEDQTRLVLQNIDACLAGAGVSRQHLVSVRVYVTDMNQWPTFNKI 94
Cdd:TIGR00004  11 AAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTDLNDFAEVNEV 90

                          90       100       110
                  ....*....|....*....|....*....|..
gi 489119392   95 YGEWIGDFRPSRAVAGVAELHYGFALEVEAMA 126
Cdd:TIGR00004  91 YGQYFDEHYPARSAVQVAALPKGVLVEIEAIA 122
PRK11401 PRK11401
enamine/imine deaminase;
18-127 4.66e-16

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 69.32  E-value: 4.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489119392  18 GHYSHSTTAGGFVFISGQLPVTFD-GEKKADAsfEDQTRLVLQNIDACLAGAGVSRQHLVSVRVYVTDMNQWPTFNKIYG 96
Cdd:PRK11401  15 GPYVQGVDLGSMVFTSGQIPVCPQtGEIPADV--QDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDLNDFATINEVYK 92

                         90       100       110
                 ....*....|....*....|....*....|....
gi 489119392  97 EWIGDFR---PSRAVAGVAELHYGFALEVEAMAL 127
Cdd:PRK11401  93 QFFDEHQatyPTRSCVQVARLPKDVKLEIEAIAV 126
 
Name Accession Description Interval E-value
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 15-129 5.09e-40

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: 129.91  E-value: 5.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489119392  15 PPAGHYSHSTTAGGFVFISGQLPVTfDGEKKADASFEDQTRLVLQNIDACLAGAGVSRQHLVSVRVYVTDMNQWPTFNKI 94
Cdd:COG0251   12 APIGPYSQAVRVGNLVFVSGQVPLD-PDTGELGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTDMADFAAVNEV 90

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489119392  95 YGEWIGDFRPSRAVAGVAELHYGFALEVEAMALAP 129
Cdd:COG0251   91 YAEYFGEGRPARTAVGVAALPKGALVEIEAIAALP 125
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 20-126 2.56e-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: 122.67  E-value: 2.56e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489119392  20 YSHSTTAGGFVFISGQLPVTFDGEKKADaSFEDQTRLVLQNIDACLAGAGVSRQHLVSVRVYVTDMNQWPTFNKIYGEWI 99
Cdd:cd00448    1 YSQAVRVGNLVFVSGQIPLDPDGELVPG-DIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFF 79

                         90       100
                 ....*....|....*....|....*...
gi 489119392 100 GDF-RPSRAVAGVAELHYGFALEVEAMA 126
Cdd:cd00448   80 GEGpPPARTAVGVAALPPGALVEIEAIA 107
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 13-126 3.51e-35

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: 117.40  E-value: 3.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489119392   13 SFPPAGHYSHSTTAGGFVFISGQLPVTFDGEKKADASFEDQTRLVLQNIDACLAGAGVSRQHLVSVRVYVTDMNQWPTFN 92
Cdd:pfam01042   2 APAAAGPYSQAVKAGNLVYVSGQIPLDPDTGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEVN 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 489119392   93 KIYGEWI-GDFRPSRAVAGVAELHYGFALEVEAMA 126
Cdd:pfam01042  82 EVYAEYFdADKAPARSAVGVAALPLGALVEIEAIA 116
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 15-126 5.19e-31

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: 107.00  E-value: 5.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489119392   15 PPAGHYSHSTTAGGFVFISGQLPVTFDGEKKADASFEDQTRLVLQNIDACLAGAGVSRQHLVSVRVYVTDMNQWPTFNKI 94
Cdd:TIGR00004  11 AAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTDLNDFAEVNEV 90

                          90       100       110
                  ....*....|....*....|....*....|..
gi 489119392   95 YGEWIGDFRPSRAVAGVAELHYGFALEVEAMA 126
Cdd:TIGR00004  91 YGQYFDEHYPARSAVQVAALPKGVLVEIEAIA 122
YjgF_YER057c_UK114_like_2 cd06150
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 18-126 1.04e-21

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: 82.97  E-value: 1.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489119392  18 GHYSHSTTAGGFVFISGQLPVtfdgekKADASFEDQTRLVLQNIDACLAGAGVSRQHLVSVRVYVTDMNQWPTFNKIYGE 97
Cdd:cd06150    1 ARMSQAVVHNGTVYLAGQVAD------DTSADITGQTRQVLAKIDALLAEAGSDKSRILSATIWLADMADFAAMNAVWDA 74

                         90       100       110
                 ....*....|....*....|....*....|
gi 489119392  98 WIGD-FRPSRAVAGVAELHYGFALEVEAMA 126
Cdd:cd06150   75 WVPPgHAPARACVEAKLADPGYLVEIVVTA 104
YjgF_YER057c_UK114_like_6 cd06154
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 9-124 3.17e-17

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: 71.82  E-value: 3.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489119392   9 SSAGSFPPAGHYSHSTTAGGFVFISGQLPVTFDGEKKADaSFEDQTRLVLQNIDACLAGAGVSRQHLVSVRVYVTDMNQW 88
Cdd:cd06154    2 SSGSPWEEQAGYSRAVRVGNWVFVSGTTGYDYDGMVMPG-DAYEQTRQCLEIIEAALAEAGASLEDVVRTRMYVTDIADF 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489119392  89 PTFNKIYGEWIGDFRPSR---AVAGVAELHYGFALEVEA 124
Cdd:cd06154   81 EAVGRAHGEVFGDIRPAAtmvVVSLLVDPEMLVEIEVTA 119
PRK11401 PRK11401
enamine/imine deaminase;
18-127 4.66e-16

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 69.32  E-value: 4.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489119392  18 GHYSHSTTAGGFVFISGQLPVTFD-GEKKADAsfEDQTRLVLQNIDACLAGAGVSRQHLVSVRVYVTDMNQWPTFNKIYG 96
Cdd:PRK11401  15 GPYVQGVDLGSMVFTSGQIPVCPQtGEIPADV--QDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDLNDFATINEVYK 92

                         90       100       110
                 ....*....|....*....|....*....|....
gi 489119392  97 EWIGDFR---PSRAVAGVAELHYGFALEVEAMAL 127
Cdd:PRK11401  93 QFFDEHQatyPTRSCVQVARLPKDVKLEIEAIAV 126
YjgH_like cd02198
YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, ...
 19-126 9.66e-16

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: 67.67  E-value: 9.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489119392  19 HYSHSTTAGGFVFISGQLPVTFDGEKKADasFEDQTRLVLQNIDACLAGAGVSRQHLVSVRVYVTDM-NQWPTFNKIYGE 97
Cdd:cd02198    2 GYSPAVRVGDTLFVSGQVGSDADGSVAED--FEAQFRLAFQNLGAVLEAAGCSFDDVVELTTFHVDMaAHLPAFAAVKDE 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 489119392  98 WIGDFRPSRAVAGVAEL-HYGFALEVEAMA 126
Cdd:cd02198   80 YFKEPYPAWTAVGVAWLaRPGLLVEIKVVA 109
eu_AANH_C_1 cd06155
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 21-107 1.08e-10

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: 54.57  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489119392  21 SHSTTAGGFVFISGQLPvtfdgeKKADASFEDQTRLVLQNIDACLAGAGVSRQHLVSVRVYVTDMNQWPTFNKIYGEWIG 100
Cdd:cd06155    1 LSQNRTGGLLWISNVTA------SESDETVEEQMESIFSKLREILQSNGLSLSDILYVTLYLRDMSDFAEVNSVYGTFFD 74


                 ....*...
gi 489119392 101 DFRP-SRA 107
Cdd:cd06155   75 KPNPpSRV 82
YjgF_YER057c_UK114_like_4 cd06152
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 19-126 4.53e-08

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: 48.07  E-value: 4.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489119392  19 HYSHSTTAGGFVFISGQLPVTFDGEKkADASFEDQTRLVLQNIDACLAGAGVSR-QHLVSVRVYVTDMNQWPTFN---KI 94
Cdd:cd06152    2 HYSQAVRIGDRIEISGQGGWDPDTGK-IPEDLEEEIDQAFDNVELALKAAGGKGwEQVYKVNSYHVDIKNEEAFGlmvEN 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489119392  95 YGEWIGDFRPSRAVAGVAELHY-GFALEVEAMA 126
Cdd:cd06152   81 FKKWMPNHQPIWTCVGVTALGLpGMRVEIEVDA 113
YjgF_YER057c_UK114_like_3 cd06151
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 30-126 1.26e-05

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: 41.54  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489119392  30 VFISGQLPVTFDGEKKAD--ASF---EDQTRLVLQNIDACLAGAGVSRQHLVSVRVY-VTD--MNQWPTF---NKIYGEW 98
Cdd:cd06151   14 IYLSGTVPAVVNASAPKGspARYgdtETQTISVLKRIETILQSQGLTMGDVVKMRVFlVADpaLDGKMDFagfMKAYRQF 93

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489119392  99 IGD----FRPSRAVAGVAEL-HYGFALEVEAMA 126
Cdd:cd06151   94 FGTaeqpNKPARSTLQVAGLvNPGWLVEIEVVA 126
YjgF_YER057c_UK114_like_1 cd02199
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 15-126 1.84e-05

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: 41.29  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489119392  15 PPAGHYSHSTTAGGFVFISGQLPVTfDGEKK------ADASFED---QTRLVLQNIDACLAGA-----GVSRqhLVSVRV 80
Cdd:cd02199   11 APVGNYVPAVRTGNLLYVSGQLPRV-DGKLVytgkvgADLSVEEgqeAARLCALNALAALKAAlgdldRVKR--VVRLTG 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489119392  81 YVT---DMNQWPT--------FNKIYGEwIGdfRPSRAVAGVAELHYGFALEVEAMA 126
Cdd:cd02199   88 FVNsapDFTEQPKvangasdlLVEVFGE-AG--RHARSAVGVASLPLNAAVEVEAIV 141
eu_AANH_C_2 cd06156
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 20-84 4.66e-03

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: 34.61  E-value: 4.66e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489119392  20 YSHSTTAGGFVFISGQLPVTFDGEKKADASFEDQTRLVLQNIDACLAGAGVsrQHLVSVRVYVTD 84
Cdd:cd06156    1 YSQAIVVPKVAYISGQIGLIPATMTLLEGGITLQAVLSLQHLERVAKAMNV--QWVLAAVCYVTD 63
YjgF_YER057c_UK114_like_5 cd06153
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 53-126 5.52e-03

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: 34.15  E-value: 5.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489119392  53 QTRLVLQNIDACL--AGAGVSRQHL---VSVRVYVTDMNQWPTFNKIYGEwigDFRPSRAVAGV------AELhygfALE 121
Cdd:cd06153   37 QTRETLENIEALLeaAGRGGGAQFLadlLRLKVYLRDREDLPAVRAILAA---RLGPAVPAVFLqadvcrPDL----LVE 109


                 ....*
gi 489119392 122 VEAMA 126
Cdd:cd06153  110 IEAVA 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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