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Conserved domains on  [gi|18422379|ref|NP_568630|]
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RmlC-like cupins superfamily protein [Arabidopsis thaliana]

Protein Classification

acireductone dioxygenase family protein( domain architecture ID 10503704)

acireductone dioxygenase family protein, such as 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:  1.13.11.53|1.13.11.54
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
ARD pfam03079
ARD/ARD' family; The two acireductone dioxygenase enzymes (ARD and ARD', previously known as ...
 4-158 2.96e-70

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: 209.90  E-value: 2.96e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422379     4 EAWFMDDSNE-DQRLPHHRNPKELVSLDYLAELGVLYWKLNPENYENDSELSKIREDRGYDYMDLL-DLCPEKVSNYEEK 81
Cdd:pfam03079   1 RIWIMDDSPCgDQRLPHHTFPKEKAETDELAKLGVLYWKLDADDEETAEDLLRILKYKHYDDVDIDvTVCPETTPNFDEK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18422379    82 LKNFFTEHIHKDEEIRYCLAGSGYFDVRDKDDRWIRIWMQPGDLIVLPAGIYHRFTLDASNYIKLMRLFVGEPVWTP 158
Cdd:pfam03079  81 LEKFFEEHLHTDEEIRYIVEGTGYFDVRDKDDVWIRVFVEKGDLISLPAGIYHRFTTTPDNYVKALRLFVTKPGWTA 157
 
Name Accession Description Interval E-value
ARD pfam03079
ARD/ARD' family; The two acireductone dioxygenase enzymes (ARD and ARD', previously known as ...
 4-158 2.96e-70

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: 209.90  E-value: 2.96e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422379     4 EAWFMDDSNE-DQRLPHHRNPKELVSLDYLAELGVLYWKLNPENYENDSELSKIREDRGYDYMDLL-DLCPEKVSNYEEK 81
Cdd:pfam03079   1 RIWIMDDSPCgDQRLPHHTFPKEKAETDELAKLGVLYWKLDADDEETAEDLLRILKYKHYDDVDIDvTVCPETTPNFDEK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18422379    82 LKNFFTEHIHKDEEIRYCLAGSGYFDVRDKDDRWIRIWMQPGDLIVLPAGIYHRFTLDASNYIKLMRLFVGEPVWTP 158
Cdd:pfam03079  81 LEKFFEEHLHTDEEIRYIVEGTGYFDVRDKDDVWIRVFVEKGDLISLPAGIYHRFTTTPDNYVKALRLFVTKPGWTA 157
cupin_ARD cd02232
acireductone dioxygenase (ARD), cupin domain; Acireductone dioxygenase (ARD; also known as 1, ...
 29-158 9.81e-70

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: 207.78  E-value: 9.81e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422379  29 LDYLAELGVLYWKLNPENYEN-----DSELSKIREDRGYDYMDLLDLCPEKVsNYEEKLKNFFTEHIHKDEEIRYCLAGS 103
Cdd:cd02232   1 AEELAELGVLYERWDADDLEAagaayDEELDALKKERGYKSRDVVTLSPETP-NYEEKLKKFFEEHLHEDDEVRFILDGS 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18422379 104 GYFDVRDKDDRWIRIWMQPGDLIVLPAGIYHRFTLDASNYIKLMRLFVGEPVWTP 158
Cdd:cd02232  80 GYFDVRDKDDEWIRILVEKGDLIVVPAGIYHRFTLDENPYIKAVRLFKDEPGWVP 134
Adi1 COG1791
Acireductone dioxygenase (methionine salvage), cupin superfamily [Amino acid transport and ...
 7-158 1.21e-19

Acireductone dioxygenase (methionine salvage), cupin superfamily [Amino acid transport and metabolism];


Pssm-ID: 441396  Cd Length: 180  Bit Score: 81.39  E-value: 1.21e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422379   7 FMDDSNEDQRLpHHRNPKELVslDYLAELGVLY--WK-----LNPENYEN-----DSELSKIREDRGYDYMDLLDLCPEk 74
Cdd:COG1791   6 IYPDDGPEQPT-TITDLEEIA--RELAPLGVRFerWDagqdlLTDAEKEEvlaayRSEIERLKAERGYQSVDVISLHPD- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422379  75 VSNYEEKLKNFFTEHIHKDEEIRYCLAGSGYFDVRdKDDRWIRIWMQPGDLIVLPAGIYHRFTLDASNYIKLMRLFVGEP 154
Cdd:COG1791  82 TPNLDALRAKFLSEHTHTEDEVRFFVAGEGLFGLH-LGGKVYEVLCEAGDLISVPAGTEHWFDMGPSPRFKAIRLFTNPE 160


                ....
gi 18422379 155 VWTP 158
Cdd:COG1791 161 GWVA 164
PRK04190 PRK04190
glucose-6-phosphate isomerase; Provisional
 85-135 5.27e-03

glucose-6-phosphate isomerase; Provisional


Pssm-ID: 179774  Cd Length: 191  Bit Score: 36.16  E-value: 5.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 18422379   85 FFTE-HIHKDE---EIRYCLAGSGYFDVRDKDDRWIRIWMQPGDLIVLPAGIYHR 135
Cdd:PRK04190  85 FMTKgHFHAKAdraEIYYGLKGKGLMLLQDPEGEARWIEMEPGTVVYVPPYWAHR 139
 
Name Accession Description Interval E-value
ARD pfam03079
ARD/ARD' family; The two acireductone dioxygenase enzymes (ARD and ARD', previously known as ...
 4-158 2.96e-70

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: 209.90  E-value: 2.96e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422379     4 EAWFMDDSNE-DQRLPHHRNPKELVSLDYLAELGVLYWKLNPENYENDSELSKIREDRGYDYMDLL-DLCPEKVSNYEEK 81
Cdd:pfam03079   1 RIWIMDDSPCgDQRLPHHTFPKEKAETDELAKLGVLYWKLDADDEETAEDLLRILKYKHYDDVDIDvTVCPETTPNFDEK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18422379    82 LKNFFTEHIHKDEEIRYCLAGSGYFDVRDKDDRWIRIWMQPGDLIVLPAGIYHRFTLDASNYIKLMRLFVGEPVWTP 158
Cdd:pfam03079  81 LEKFFEEHLHTDEEIRYIVEGTGYFDVRDKDDVWIRVFVEKGDLISLPAGIYHRFTTTPDNYVKALRLFVTKPGWTA 157
cupin_ARD cd02232
acireductone dioxygenase (ARD), cupin domain; Acireductone dioxygenase (ARD; also known as 1, ...
 29-158 9.81e-70

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: 207.78  E-value: 9.81e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422379  29 LDYLAELGVLYWKLNPENYEN-----DSELSKIREDRGYDYMDLLDLCPEKVsNYEEKLKNFFTEHIHKDEEIRYCLAGS 103
Cdd:cd02232   1 AEELAELGVLYERWDADDLEAagaayDEELDALKKERGYKSRDVVTLSPETP-NYEEKLKKFFEEHLHEDDEVRFILDGS 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18422379 104 GYFDVRDKDDRWIRIWMQPGDLIVLPAGIYHRFTLDASNYIKLMRLFVGEPVWTP 158
Cdd:cd02232  80 GYFDVRDKDDEWIRILVEKGDLIVVPAGIYHRFTLDENPYIKAVRLFKDEPGWVP 134
Adi1 COG1791
Acireductone dioxygenase (methionine salvage), cupin superfamily [Amino acid transport and ...
 7-158 1.21e-19

Acireductone dioxygenase (methionine salvage), cupin superfamily [Amino acid transport and metabolism];


Pssm-ID: 441396  Cd Length: 180  Bit Score: 81.39  E-value: 1.21e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422379   7 FMDDSNEDQRLpHHRNPKELVslDYLAELGVLY--WK-----LNPENYEN-----DSELSKIREDRGYDYMDLLDLCPEk 74
Cdd:COG1791   6 IYPDDGPEQPT-TITDLEEIA--RELAPLGVRFerWDagqdlLTDAEKEEvlaayRSEIERLKAERGYQSVDVISLHPD- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422379  75 VSNYEEKLKNFFTEHIHKDEEIRYCLAGSGYFDVRdKDDRWIRIWMQPGDLIVLPAGIYHRFTLDASNYIKLMRLFVGEP 154
Cdd:COG1791  82 TPNLDALRAKFLSEHTHTEDEVRFFVAGEGLFGLH-LGGKVYEVLCEAGDLISVPAGTEHWFDMGPSPRFKAIRLFTNPE 160


                ....
gi 18422379 155 VWTP 158
Cdd:COG1791 161 GWVA 164
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
88-137 5.32e-07

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 46.00  E-value: 5.32e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 18422379  88 EHIHKDEEIRYCLAGSGYFDVrdkDDRWIRIwmQPGDLIVLPAGIYHRFT 137
Cdd:COG1917  38 WHSHPGEELIYVLEGEGEVEV---GGEEYEL--KPGDVVFIPPGVPHAFR 82
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 86-136 3.40e-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: 43.02  E-value: 3.40e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 18422379    86 FTEHIHKDE-EIRYCLAGSGYFDVrdkDDRWIRiwMQPGDLIVLPAGIYHRF 136
Cdd:pfam07883  11 SPPHRHPGEdEFFYVLEGEGELTV---DGEEVV--LKAGDSVYFPAGVPHRF 57
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 88-136 9.90e-06

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: 43.03  E-value: 9.90e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 18422379  88 EHIHKDE-EIRYCLAGSGYFDVRDKDDRWIRIWMQPGDLIVLPAGIYHRF 136
Cdd:COG2140  18 EHWHPNAaEWYYVLSGEARMTVQDPPGRARTVDVGPGDVVYVPPGYGHYI 67
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 88-136 1.59e-05

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: 41.31  E-value: 1.59e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 18422379  88 EHIHKD-EEIRYCLAGSGYFDVRDKDdrwiRIWMQPGDLIVLPAGIYHRF 136
Cdd:cd02208  14 PHWHPEqDEIFYVLSGEGELTLDDGE----TVELKAGDIVLIPPGVPHSF 59
cupin_YdbB-like cd02226
Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial ...
 81-135 6.70e-05

Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial proteins homologous to YdbB, a Bacillus subtilis protein of unknown function. It also includes protein Nmb1881 From Neisseria meningitidis, also 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: 380355 [Multi-domain]  Cd Length: 94  Bit Score: 40.12  E-value: 6.70e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18422379  81 KLKNFFTEHIHKDE-EIRYCLAGSGYFDVRDKDdrwirIWMQPGDLIVLPAGIYHR 135
Cdd:cd02226  30 KLKGEFVWHKHDDEdELFLVLEGELTIDFRDRD-----VTLGPGEFFVVPKGVEHR 80
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 86-142 1.02e-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: 40.50  E-value: 1.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18422379    86 FTEHIHKDEEIRYCLAGSGYFDVRDKddRWIriwMQPGDLIVLPAGIYHRFTLDASN 142
Cdd:pfam02311  16 FPPHVHDFYVIGYIERGVGRFRLNGR--TYH---LGPGDLFLLPPGEPHDYEPESED 67
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
86-136 2.40e-04

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 38.97  E-value: 2.40e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 18422379  86 FTEHIHKD-EEIRYCLAGSGYFDVRDKddrwiRIWMQPGDLIVLPAGIYHRF 136
Cdd:COG0662  40 LSLHVHPHrDEFFYVLEGTGEVTIGDE-----EVELKAGDSVYIPAGVPHRL 86
cupin_HNL-like cd02233
Granulicella tundricola hydroxynitrile lyase (GtHNL) and related proteins, cupin domain; This ...
 89-134 2.49e-04

Granulicella tundricola hydroxynitrile lyase (GtHNL) and related proteins, cupin domain; This family includes archaeal, eukaryotic, and bacterial proteins homologous to hydroxynitrile lyase from Granulicella tundricola (GtHNL), a novel class of HNLs that does not show any sequence or structural similarity to any other HNL and does not contain conserved motifs typical of HNLs. HNLs comprise a diverse group of enzymes that vary in terms of their substrate specificity, enantioselectivity and the need for a co-factor. In plants, they catalyze the reversible cleavage of cyanohydrins, yielding HCN and aldehydes or ketones. Also included in this family is TM1010 from Thermotoga maritima, a protein of unknown function. Some but not all members of this family have N- or C-terminal carboxymuconolactone decarboxylase domains in addition to the cupin domain. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380361 [Multi-domain]  Cd Length: 106  Bit Score: 38.69  E-value: 2.49e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 18422379  89 HIHKDEEIRYCLAGSGYFDVRDKDDRWIRiwmqPGDLIVLPAGIYH 134
Cdd:cd02233  35 HTHPGGQILIVTSGVGWVQEEGGPPQELR----PGDVVWIPPGVKH 76
RmlC COG4101
Uncharacterized conserved protein, RmlC-like cupin domain [General function prediction only];
89-136 1.93e-03

Uncharacterized conserved protein, RmlC-like cupin domain [General function prediction only];


Pssm-ID: 443277  Cd Length: 146  Bit Score: 36.87  E-value: 1.93e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 18422379  89 HIHKD-EEIRYCLAGSGYFdvrdkddRW-----IRIWMQPGDLIVLPAGIYHRF 136
Cdd:COG4101  62 HHHGEhETAIYVLSGRAET-------RYgerleHRVVTEPGDFIFIPPGVPHQE 108
cupin_PGI cd02218
cupin-type phosphoglucose isomerase; The cupin-type phosphoglucose isomerase (also called ...
 89-135 2.59e-03

cupin-type phosphoglucose isomerase; The cupin-type phosphoglucose isomerase (also called cupin-like glucose-6-phosphate isomerase or cPGI; EC 5.3.1.9) family is found in archaea and certain prokaryotes where they catalyze the reversible aldose-ketose isomerization of glucose 6-phosphate (G6P) and fructose 6-phosphate (F6P) as part of a unique variation of the Embden-Meyerhof glycolytic pathway. Cupin-PGIs represent a separate lineage in the evolution of phosphoglucose isomerases. Pyrococcus furiosus phosphoglucose isomerase (PfPGI) has been shown to be a metal-containing enzyme which catalyzes the interconversion of glucose 6-phosphate (G6P) and fructose 6-phosphate (F6P). These domains have a cupin beta-barrel fold capable of homodimerization.


Pssm-ID: 380347  Cd Length: 168  Bit Score: 36.77  E-value: 2.59e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 18422379  89 HIHKDE---EIRYCLAGSGYF---DVRDKDDRWIRiwMQPGDLIVLPAGIYHR 135
Cdd:cd02218  67 HYHAKRdypEVYEVLSGEGLLllqKEDVGEVILVE--AKPGDKVYIPPGYAHR 117
PRK04190 PRK04190
glucose-6-phosphate isomerase; Provisional
 85-135 5.27e-03

glucose-6-phosphate isomerase; Provisional


Pssm-ID: 179774  Cd Length: 191  Bit Score: 36.16  E-value: 5.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 18422379   85 FFTE-HIHKDE---EIRYCLAGSGYFDVRDKDDRWIRIWMQPGDLIVLPAGIYHR 135
Cdd:PRK04190  85 FMTKgHFHAKAdraEIYYGLKGKGLMLLQDPEGEARWIEMEPGTVVYVPPYWAHR 139
cupin_Pac13-like cd20295
monomeric dehydratase Pac13 and related proteins, cupin domain; This family includes a small ...
 87-168 6.36e-03

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: 34.89  E-value: 6.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422379  87 TEHIHKDE-EIRYCLAGSGYFDVrdkDDRWIRIwmQPGDLIVLPAGIYHRftldasnYIKLMRLFVgepVWTPYNRPQEE 165
Cdd:cd20295  34 EEHYHKKStEIYYVLEGEGIFEL---DGEAVPV--KPGDLVLIPPGTRHR-------AVGKMKILL---IVIPAFDPEDE 98


                ...
gi 18422379 166 HPV 168
Cdd:cd20295  99 WHD 101
cupin_QDO_N_C cd02215
quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known ...
 89-140 7.38e-03

quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known as quercetin 2,3-dioxygenase, 2,3QD, QDO and YxaG; EC 1.13.11.24), a mononuclear copper-dependent dioxygenase that catalyzes the cleavage of the flavonol quercetin (5,7,3',4'-tetrahydroxyflavonol) heterocyclic ring to produce 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon monoxide. Bacillus subtilis quercetin 2,3-dioxygenase (QDO) is a homodimer that shows oxygenase activity with several divalent metals such as Mn2+, Co2+, Fe2+, and Cu2+, although the preferred one appears to be Mn2+. The dioxygen binds to the metal ion of the Cu-QDO-quercetin complex, yielding a Cu2+-superoxo quercetin radical intermediate, which then forms a Cu2+-alkylperoxo complex which then evolves into endoperoxide intermediate that decomposes to the product. Quercetinase is a bicupin with two tandem cupin beta-barrel domains, both of which are included in this alignment model. The pirins, which also belong to the cupin domain family, have been shown to catalyze a reaction involving quercetin and may have a function similar to that of quercetinase.


Pssm-ID: 380345 [Multi-domain]  Cd Length: 122  Bit Score: 34.82  E-value: 7.38e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422379  89 HIHKDE-EIRYCLAGSgyfdvrdkddrwIRIWMQ-------PGDLIVLPAGIYHRFTLDA 140
Cdd:cd02215  48 HYHKRHhETFYVLEGR------------LQLWLDgesrlltPGDFASVPPGTIHAYRMLS 95
 
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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