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Conserved domains on  [gi|1937882689|ref|NP_954528|]
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acireductone dioxygenase [Rattus norvegicus]

Protein Classification

1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase( domain architecture ID 14388757)

1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase, also called acireductone dioxygenase, catalyzes the oxidation of 1,2-dihydroxy-3-keto-5-methylthiopentene to yield two different products depending on which active site metal is present (Fe2+ or Ni2+) as part of the methionine salvage pathway

CATH:  2.60.120.10
EC:  1.13.11.54|1.13.11.53
Gene Ontology:  GO:0019509|GO:0010309|GO:0005506|GO:0010308|GO:0016151
PubMed:  9880484|16989860|14697267|19478949
SCOP:  4002777

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cupin_ARD cd02232
acireductone dioxygenase (ARD), cupin domain; Acireductone dioxygenase (ARD; also known as 1, ...
 28-157 9.69e-73

acireductone dioxygenase (ARD), cupin domain; Acireductone dioxygenase (ARD; also known as 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase) catalyzes the oxidation of 1,2-dihydroxy-3-keto-5-methylthiopentene to yield two different products depending on which active site metal is present (Fe2+ or Ni2+) as part of the methionine salvage pathway. The ARD apo-enzyme, obtained after the metal is removed, is catalytically inactive. The Fe(II)-ARD reaction yields an alpha-keto acid and formic acid, while Ni(II)-ARD instead catalyzes a shunt out of the methionine salvage pathway, yielding methylthiocarboxylic acid, formic acid, and CO. ARD belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization


:

Pssm-ID: 380360  Cd Length: 134  Bit Score: 215.10  E-value: 9.69e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937882689  28 LEQLRTLGVLYWKLDADKYEN-----DPELEQIRKTRNYSWMDIITICKDSlPNYEEKIKMFFEEHLHLDEEIRYILEGS 102
Cdd:cd02232     1 AEELAELGVLYERWDADDLEAagaayDEELDALKKERGYKSRDVVTLSPET-PNYEEKLKKFFEEHLHEDDEVRFILDGS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1937882689 103 GYFDVRDKEDKWIRISMEKGDMITLPAGIYHRFTLDEKNYVKAMRLFVGEPVWTP 157
Cdd:cd02232    80 GYFDVRDKDDEWIRILVEKGDLIVVPAGIYHRFTLDENPYIKAVRLFKDEPGWVP 134
 
Name Accession Description Interval E-value
cupin_ARD cd02232
acireductone dioxygenase (ARD), cupin domain; Acireductone dioxygenase (ARD; also known as 1, ...
 28-157 9.69e-73

acireductone dioxygenase (ARD), cupin domain; Acireductone dioxygenase (ARD; also known as 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase) catalyzes the oxidation of 1,2-dihydroxy-3-keto-5-methylthiopentene to yield two different products depending on which active site metal is present (Fe2+ or Ni2+) as part of the methionine salvage pathway. The ARD apo-enzyme, obtained after the metal is removed, is catalytically inactive. The Fe(II)-ARD reaction yields an alpha-keto acid and formic acid, while Ni(II)-ARD instead catalyzes a shunt out of the methionine salvage pathway, yielding methylthiocarboxylic acid, formic acid, and CO. ARD belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization


Pssm-ID: 380360  Cd Length: 134  Bit Score: 215.10  E-value: 9.69e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937882689  28 LEQLRTLGVLYWKLDADKYEN-----DPELEQIRKTRNYSWMDIITICKDSlPNYEEKIKMFFEEHLHLDEEIRYILEGS 102
Cdd:cd02232     1 AEELAELGVLYERWDADDLEAagaayDEELDALKKERGYKSRDVVTLSPET-PNYEEKLKKFFEEHLHEDDEVRFILDGS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1937882689 103 GYFDVRDKEDKWIRISMEKGDMITLPAGIYHRFTLDEKNYVKAMRLFVGEPVWTP 157
Cdd:cd02232    80 GYFDVRDKDDEWIRILVEKGDLIVVPAGIYHRFTLDENPYIKAVRLFKDEPGWVP 134
ARD pfam03079
ARD/ARD' family; The two acireductone dioxygenase enzymes (ARD and ARD', previously known as ...
 3-157 1.08e-68

ARD/ARD' family; The two acireductone dioxygenase enzymes (ARD and ARD', previously known as E-2 and E-2') from Klebsiella pneumoniae share the same amino acid sequence, but bind different metal ions: ARD binds Ni2+, ARD' binds Fe2+. ARD and ARD' can be experimentally interconverted by removal of the bound metal ion and reconstitution with the appropriate metal ion. The two enzymes share the same substrate, 1,2-dihydroxy-3-keto-5-(methylthio)pentene, but yield different products. ARD' yields the alpha-keto precursor of methionine (and formate), thus forming part of the ubiquitous methionine salvage pathway that converts 5'-methylthioadenosine (MTA) to methionine. This pathway is responsible for the tight control of the concentration of MTA, which is a powerful inhibitor of polyamine biosynthesis and transmethylation reactions. ARD yields methylthiopropanoate, carbon monoxide and formate, and thus prevents the conversion of MTA to methionine. The role of the ARD catalyzed reaction is unclear: methylthiopropanoate is cytotoxic, and carbon monoxide can activate guanylyl cyclase, leading to increased intracellular cGMP levels. This family also contains other members, whose functions are not well characterized.


Pssm-ID: 281122  Cd Length: 157  Bit Score: 205.67  E-value: 1.08e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937882689   3 QAWYMDES-TADPRMPHRAQPDRPVGLEQLRTLGVLYWKLDADKYENDPELEQIRKTRNYSWMDII-TICKDSLPNYEEK 80
Cdd:pfam03079   1 RIWIMDDSpCGDQRLPHHTFPKEKAETDELAKLGVLYWKLDADDEETAEDLLRILKYKHYDDVDIDvTVCPETTPNFDEK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937882689  81 IKMFFEEHLHLDEEIRYILEGSGYFDVRDKEDKWIRISMEKGDMITLPAGIYHRFTLDEKNYVKAMRLFVGEPVWTP 157
Cdd:pfam03079  81 LEKFFEEHLHTDEEIRYIVEGTGYFDVRDKDDVWIRVFVEKGDLISLPAGIYHRFTTTPDNYVKALRLFVTKPGWTA 157
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
85-154 1.03e-06

Cupin domain protein related to quercetin dioxygenase [General function prediction only];


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 45.22  E-value: 1.03e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937882689  85 FEEHLHLDEEIRYILEGSGYFDVRDKEdkwirISMEKGDMITLPAGIYHRFTLDEKnyVKAMRLFVGEPV 154
Cdd:COG1917    36 TPWHSHPGEELIYVLEGEGEVEVGGEE-----YELKPGDVVFIPPGVPHAFRNLGD--EPAVLLVVFSPG 98
 
Name Accession Description Interval E-value
cupin_ARD cd02232
acireductone dioxygenase (ARD), cupin domain; Acireductone dioxygenase (ARD; also known as 1, ...
 28-157 9.69e-73

acireductone dioxygenase (ARD), cupin domain; Acireductone dioxygenase (ARD; also known as 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase) catalyzes the oxidation of 1,2-dihydroxy-3-keto-5-methylthiopentene to yield two different products depending on which active site metal is present (Fe2+ or Ni2+) as part of the methionine salvage pathway. The ARD apo-enzyme, obtained after the metal is removed, is catalytically inactive. The Fe(II)-ARD reaction yields an alpha-keto acid and formic acid, while Ni(II)-ARD instead catalyzes a shunt out of the methionine salvage pathway, yielding methylthiocarboxylic acid, formic acid, and CO. ARD belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization


Pssm-ID: 380360  Cd Length: 134  Bit Score: 215.10  E-value: 9.69e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937882689  28 LEQLRTLGVLYWKLDADKYEN-----DPELEQIRKTRNYSWMDIITICKDSlPNYEEKIKMFFEEHLHLDEEIRYILEGS 102
Cdd:cd02232     1 AEELAELGVLYERWDADDLEAagaayDEELDALKKERGYKSRDVVTLSPET-PNYEEKLKKFFEEHLHEDDEVRFILDGS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1937882689 103 GYFDVRDKEDKWIRISMEKGDMITLPAGIYHRFTLDEKNYVKAMRLFVGEPVWTP 157
Cdd:cd02232    80 GYFDVRDKDDEWIRILVEKGDLIVVPAGIYHRFTLDENPYIKAVRLFKDEPGWVP 134
ARD pfam03079
ARD/ARD' family; The two acireductone dioxygenase enzymes (ARD and ARD', previously known as ...
 3-157 1.08e-68

ARD/ARD' family; The two acireductone dioxygenase enzymes (ARD and ARD', previously known as E-2 and E-2') from Klebsiella pneumoniae share the same amino acid sequence, but bind different metal ions: ARD binds Ni2+, ARD' binds Fe2+. ARD and ARD' can be experimentally interconverted by removal of the bound metal ion and reconstitution with the appropriate metal ion. The two enzymes share the same substrate, 1,2-dihydroxy-3-keto-5-(methylthio)pentene, but yield different products. ARD' yields the alpha-keto precursor of methionine (and formate), thus forming part of the ubiquitous methionine salvage pathway that converts 5'-methylthioadenosine (MTA) to methionine. This pathway is responsible for the tight control of the concentration of MTA, which is a powerful inhibitor of polyamine biosynthesis and transmethylation reactions. ARD yields methylthiopropanoate, carbon monoxide and formate, and thus prevents the conversion of MTA to methionine. The role of the ARD catalyzed reaction is unclear: methylthiopropanoate is cytotoxic, and carbon monoxide can activate guanylyl cyclase, leading to increased intracellular cGMP levels. This family also contains other members, whose functions are not well characterized.


Pssm-ID: 281122  Cd Length: 157  Bit Score: 205.67  E-value: 1.08e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937882689   3 QAWYMDES-TADPRMPHRAQPDRPVGLEQLRTLGVLYWKLDADKYENDPELEQIRKTRNYSWMDII-TICKDSLPNYEEK 80
Cdd:pfam03079   1 RIWIMDDSpCGDQRLPHHTFPKEKAETDELAKLGVLYWKLDADDEETAEDLLRILKYKHYDDVDIDvTVCPETTPNFDEK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937882689  81 IKMFFEEHLHLDEEIRYILEGSGYFDVRDKEDKWIRISMEKGDMITLPAGIYHRFTLDEKNYVKAMRLFVGEPVWTP 157
Cdd:pfam03079  81 LEKFFEEHLHTDEEIRYIVEGTGYFDVRDKDDVWIRVFVEKGDLISLPAGIYHRFTTTPDNYVKALRLFVTKPGWTA 157
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
85-154 1.03e-06

Cupin domain protein related to quercetin dioxygenase [General function prediction only];


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 45.22  E-value: 1.03e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937882689  85 FEEHLHLDEEIRYILEGSGYFDVRDKEdkwirISMEKGDMITLPAGIYHRFTLDEKnyVKAMRLFVGEPV 154
Cdd:COG1917    36 TPWHSHPGEELIYVLEGEGEVEVGGEE-----YELKPGDVVFIPPGVPHAFRNLGD--EPAVLLVVFSPG 98
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 85-135 4.18e-06

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 42.63  E-value: 4.18e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1937882689  85 FEEHLHLDE-EIRYILEGSGYFDVRDKEdkwirISMEKGDMITLPAGIYHRF 135
Cdd:pfam07883  11 SPPHRHPGEdEFFYVLEGEGELTVDGEE-----VVLKAGDSVYFPAGVPHRF 57
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 84-144 7.90e-06

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.


Pssm-ID: 380338 [Multi-domain]  Cd Length: 73  Bit Score: 42.08  E-value: 7.90e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937882689  84 FFEEHLH-LDEEIRYILEGSGYFDVRDKEdkwiRISMEKGDMITLPAGIYHRFTLDEKNYVK 144
Cdd:cd02208    11 SSPPHWHpEQDEIFYVLSGEGELTLDDGE----TVELKAGDIVLIPPGVPHSFVNTSDEPAV 68
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 86-135 1.10e-05

Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate transport and metabolism]; Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 441743 [Multi-domain]  Cd Length: 115  Bit Score: 42.65  E-value: 1.10e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1937882689  86 EEHLHLDE-EIRYILEGSGYFDVRDKEDKWIRISMEKGDMITLPAGIYHRF 135
Cdd:COG2140    17 EEHWHPNAaEWYYVLSGEARMTVQDPPGRARTVDVGPGDVVYVPPGYGHYI 67
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
85-135 4.22e-05

Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 40.90  E-value: 4.22e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1937882689  85 FEEHLHLD-EEIRYILEGSGYFDVRDKEdkwirISMEKGDMITLPAGIYHRF 135
Cdd:COG0662    40 LSLHVHPHrDEFFYVLEGTGEVTIGDEE-----VELKAGDSVYIPAGVPHRL 86
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
88-135 8.73e-05

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 40.00  E-value: 8.73e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1937882689  88 HLHLD-EEIRYILEGSGYFDVRDKEdkwirISMEKGDMITLPAGIYHRF 135
Cdd:COG3837    45 HAHSAeEEFVYVLEGELTLRIGGEE-----YVLEPGDSVGFPAGVPHRL 88
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 85-155 1.15e-04

AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization domain of the bacterial gene regulatory protein AraC. The domain is found in conjunction with the helix-turn-helix (HTH) DNA-binding motif pfam00165. This domain is distantly related to the Cupin domain pfam00190.


Pssm-ID: 396749 [Multi-domain]  Cd Length: 134  Bit Score: 40.11  E-value: 1.15e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937882689  85 FEEHLHLDEEIRYILEGSGYFDVRDKedkwiRISMEKGDMITLPAGIYHRFTLD-EKNYVKAMRLFVGEPVW 155
Cdd:pfam02311  16 FPPHVHDFYVIGYIERGVGRFRLNGR-----TYHLGPGDLFLLPPGEPHDYEPEsEDGWRYRWLYFEPELLE 82
cupin_Pac13-like cd20295
monomeric dehydratase Pac13 and related proteins, cupin domain; This family includes a small ...
 86-166 3.39e-04

monomeric dehydratase Pac13 and related proteins, cupin domain; This family includes a small monomeric dehydratase Pac13 that mediates the formation of the 3'-deoxynucleotide of pacidamycins, which are uradyl peptide antibiotics (UPAs). Pac13 is involved in the formation of the unique 3'-deoxyuridine moiety found in these UPAs; it catalyzes the dehydration of uridine-5'-aldehyde. The similarity of the 3'-deoxy pacidamycin moiety with synthetic anti-retrovirals, offers a potential opportunity for the utilization of Pac13 in the biocatalytic generation of antiviral compounds. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380429 [Multi-domain]  Cd Length: 101  Bit Score: 38.35  E-value: 3.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937882689  86 EEHLHLDE-EIRYILEGSGYFDVRDKedkwiRISMEKGDMITLPAGIYHRftldeknYVKAMRLFVgepVWTPYNRPAD- 163
Cdd:cd20295    34 EEHYHKKStEIYYVLEGEGIFELDGE-----AVPVKPGDLVLIPPGTRHR-------AVGKMKILL---IVIPAFDPEDe 98


                  ...
gi 1937882689 164 HFD 166
Cdd:cd20295    99 WHD 101
cupin_GDO-like_N cd02216
gentisate 1,2-dioxygenase, 1-hydroxy-2-naphthoate dioxygenase, and salicylate 1,2-dioxygenase, ...
 88-133 1.86e-03

gentisate 1,2-dioxygenase, 1-hydroxy-2-naphthoate dioxygenase, and salicylate 1,2-dioxygenase, N-terminal cupin domain; This family includes the N-terminal cupin domains of three closely related bicupin aromatic ring-cleaving dioxygenases: gentisate 1,2-dioxygenase (GDO), salicylate 1,2-dioxygenase (SDO), and 1-hydroxy-2-naphthoate dioxygenase (NDO). GDO catalyzes the cleavage of the gentisate (2,5-dihydroxybenzoate) aromatic ring, a key step in the gentisate degradation pathway allowing soil bacteria to utilize 2,5-xylenol, 3,5-xylenol, and m-cresol as sole carbon and energy sources. NDO catalyzes the cleavage of 1-hydroxy-2-naphthoate as part of the bacterial phenanthrene degradation pathway. SDO is a ring cleavage dioxygenase from Pseudaminobacter salicylatoxidans that oxidizes salicylate to 2-oxohepta-3,5-dienedioic acid via a novel ring fission mechanism. SDO differs from other known GDOs and NDOs in its unique ability to oxidatively cleave many different salicylate, gentisate and 1-hydroxy-2-naphthoate substrates with high catalytic efficiency. The active site of these enzymes is located in the N-terminal domain but could be influenced by changes in the C-terminal domain, which lacks the strictly conserved metal-binding residues found in other cupin domains and is thought to be an inactive vestigial remnant.


Pssm-ID: 380346 [Multi-domain]  Cd Length: 108  Bit Score: 36.38  E-value: 1.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1937882689  88 HLHLDEEIRYILEGSGYFDVRDKEdkwiRISMEKGDMITLPAGIYH 133
Cdd:cd02216    37 HRHTPNALRFVLEGPGAYTTVDGE----RCDMEPGDLILTPPGTWH 78
cupin_HQDO_large_C cd20492
hydroquinol 1,2-dioxygenase (HQDO) large subunit, C-terminal cupin domain; This model ...
 66-134 4.92e-03

hydroquinol 1,2-dioxygenase (HQDO) large subunit, C-terminal cupin domain; This model describes the C-terminal cupin domain of the large (or beta) subunit of hydroquinone 1,2-dioxygenase (HQDO), a heterotetramer of two alpha and two beta subunits of 19kDa and 38kDa, respectively. HQDO is a Fe(II) ring cleaving dioxygenase that is a key enzyme in the hydroquinone pathway of para-nitrophenol degradation, where it catalyzes the ring cleavage of hydroquinone to gamma-hydroxymuconic semialdehyde. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380449  Cd Length: 100  Bit Score: 34.90  E-value: 4.92e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937882689  66 IITICKDSL--PNYEEKIKMFF------EEHLHLDEEIRYilegsgyfDVRDKED--KWIRISMEKGDMITLPAGIYHR 134
Cdd:cd20492    14 VTSVCKDSLfcPTTEEFILPVFhgndrvEWFIQLSDEIVW--------DVKDKETgkPRARVTMRAGDVCAMPADIRHQ 84
cupin_BLL4011-like cd02235
Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes ...
 88-134 7.49e-03

Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to BLL4011, a Bradyrhizobium diazoefficiens protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380363 [Multi-domain]  Cd Length: 100  Bit Score: 34.48  E-value: 7.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1937882689  88 HLHLDEEIRYILEGSGYFDVRDKEDKWIRismeKGDMITLPAGIYHR 134
Cdd:cd02235    35 HTHPGEESGYVLEGSLELEVDGQPPVTLK----AGDSFFIPAGTVHN 77
cupin_PA3510-like cd02225
Pseudomonas aeruginosa PA3510 and related proteins, cupin domain; This family includes ...
 87-135 9.26e-03

Pseudomonas aeruginosa PA3510 and related proteins, cupin domain; This family includes bacterial proteins homologous to PA3510, a Pseudomonas aeruginosa protein of unknown function with a beta-barrel fold that belongs to the cupin superfamily.


Pssm-ID: 380354  Cd Length: 150  Bit Score: 34.94  E-value: 9.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1937882689  87 EHLHLDEEIRYILEGSGYFDVRDkEDKWIRISMEKGDMITLPAGIYHRF 135
Cdd:cd02225    68 LHTHEVEEVFFVLQGRLTVFWED-EGEEHERELGPRDMISVPAGVYRGF 115
COG3435 COG3435
Gentisate 1,2-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
86-133 9.53e-03

Gentisate 1,2-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442661 [Multi-domain]  Cd Length: 316  Bit Score: 35.60  E-value: 9.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1937882689  86 EEHLHLDEEIRYILEGSGYFDVRDKEdkwiRISMEKGDMITLPAGIYH 133
Cdd:COG3435    72 PAHRHTQSALRFVIEGEGAYTVVDGE----RVPMERGDFVLTPSWTWH 115
 
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.
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