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Conserved domains on  [gi|90111702|ref|NP_418613|]
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L-ascorbate-6-phosphate lactonase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

L-ascorbate-6-phosphate lactonase UlaG( domain architecture ID 10013869)

L-ascorbate-6-phosphate lactonase similar to Escherichia coli UlaG, which is likely to catalyze the hydrolysis of L-ascorbate-6-P into 3-keto-L-gulonate-6-P

CATH:  3.60.15.10
EC:  3.1.1.-
Gene Symbol:  ulaG
Gene Ontology:  GO:0046872|GO:0035460|GO:0019854
PubMed:  20359483|17597585|11471246
SCOP:  3001057

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11709 PRK11709
putative L-ascorbate 6-phosphate lactonase; Provisional
 1-354 0e+00

putative L-ascorbate 6-phosphate lactonase; Provisional


:

Pssm-ID: 236958  Cd Length: 355  Bit Score: 795.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702    1 MSKVKSITRESWILSTFPEWGSWLNEEIEQEQVAPGTFAMWWLGCTGIWLKSEGGTNVCVDFWCGTGKQSHGNPLMKQGH 80
Cdd:PRK11709   1 MSKVKEITRESWILSTFPEWGTWLNEEIEQEVVPPGTFAMWWLGCTGIWLKTEGGTNVCVDLWCGTGKQTHGNPLMKRGH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702   81 QMQRMAGVKKLQPNLRTTPFVLDPFAIRQIDAVLATHDHNDHIDVNVAAAVMQNCADDVPFIGPKTCVDLWIGWGVPKER 160
Cdd:PRK11709  81 QMARMAGVRKLQPNLRTQPFVLDPFAIREIDAVLATHDHSDHIDVNVAAAVLQNCADHVKFIGPQACVDLWIGWGVPKER 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702  161 CIVVKPGDVVKVKDIEIHALDAFDRTALITLPADQKAA-GVLPDGMDDRAVNYLFKTPGGSLYHSGDSHYSNYYAKHGNE 239
Cdd:PRK11709 161 CIVVKPGDVVKVKDIKIHALDSFDRTALVTLPADGKAAgGVLPDDMDRRAVNYLFKTPGGNIYHSGDSHYSNYFAKHGND 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702  240 HQIDVALGSYGENPRGITDKMTSADMLRMGEALNAKVVIPFHHDIWSNFQADPQEIRVLWEMKKDRLKYGFKPFIWQVGG 319
Cdd:PRK11709 241 HQIDVALGSYGENPRGITDKMTSIDILRMAESLNAKVVIPVHHDIWSNFQADPQEILVLWKMRKDRLQYGFHPFIWQVGG 320

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 90111702  320 KFTWPLDKDNFEYHYPRGFDDCFTIEPDLPFKSFL 354
Cdd:PRK11709 321 KFTYPQDKDRFEYHYPRGFDDCFTIEPDLPFKSFL 355
 
Name Accession Description Interval E-value
PRK11709 PRK11709
putative L-ascorbate 6-phosphate lactonase; Provisional
 1-354 0e+00

putative L-ascorbate 6-phosphate lactonase; Provisional


Pssm-ID: 236958  Cd Length: 355  Bit Score: 795.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702    1 MSKVKSITRESWILSTFPEWGSWLNEEIEQEQVAPGTFAMWWLGCTGIWLKSEGGTNVCVDFWCGTGKQSHGNPLMKQGH 80
Cdd:PRK11709   1 MSKVKEITRESWILSTFPEWGTWLNEEIEQEVVPPGTFAMWWLGCTGIWLKTEGGTNVCVDLWCGTGKQTHGNPLMKRGH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702   81 QMQRMAGVKKLQPNLRTTPFVLDPFAIRQIDAVLATHDHNDHIDVNVAAAVMQNCADDVPFIGPKTCVDLWIGWGVPKER 160
Cdd:PRK11709  81 QMARMAGVRKLQPNLRTQPFVLDPFAIREIDAVLATHDHSDHIDVNVAAAVLQNCADHVKFIGPQACVDLWIGWGVPKER 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702  161 CIVVKPGDVVKVKDIEIHALDAFDRTALITLPADQKAA-GVLPDGMDDRAVNYLFKTPGGSLYHSGDSHYSNYYAKHGNE 239
Cdd:PRK11709 161 CIVVKPGDVVKVKDIKIHALDSFDRTALVTLPADGKAAgGVLPDDMDRRAVNYLFKTPGGNIYHSGDSHYSNYFAKHGND 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702  240 HQIDVALGSYGENPRGITDKMTSADMLRMGEALNAKVVIPFHHDIWSNFQADPQEIRVLWEMKKDRLKYGFKPFIWQVGG 319
Cdd:PRK11709 241 HQIDVALGSYGENPRGITDKMTSIDILRMAESLNAKVVIPVHHDIWSNFQADPQEILVLWKMRKDRLQYGFHPFIWQVGG 320

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 90111702  320 KFTWPLDKDNFEYHYPRGFDDCFTIEPDLPFKSFL 354
Cdd:PRK11709 321 KFTYPQDKDRFEYHYPRGFDDCFTIEPDLPFKSFL 355
UlaG-like_MBL-fold cd16284
UlaG a putative l-ascorbate-6-P lactonase and related proteins; MBL-fold metallo hydrolase ...
 37-249 5.66e-127

UlaG a putative l-ascorbate-6-P lactonase and related proteins; MBL-fold metallo hydrolase domain; UlaG is essential for L-ascorbate utilization under anaerobic conditions; it is a putative l-ascorbate-6-P lactonase thought to catalyze the hydrolysis of L-ascorbate-6-phosphate to 3-keto-L-gulonate-6-phosphate. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293842  Cd Length: 178  Bit Score: 361.40  E-value: 5.66e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702  37 TFAMWWLGCTGIWLKSEGGTNVCVDFWCgtgkqshgnplmkqghqmqrmagvkklqpnlrttpFVLDPFAIRQIDAVLAT 116
Cdd:cd16284   1 TFAMWWLGCTGIWLKSEGNTNICIDFWC-----------------------------------FVLDPFAIKQIDAVLAT 45

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702 117 HDHNDHIDVNVAAAVMQNCADDVPFIGPKTCVDLWIGWGVPKERCIVVKPGDVVKVKDIEIHALDAFDRTALITLPADQK 196
Cdd:cd16284  46 HDHNDHIDVNVAAAVLQNCAPDVPFIGPQACVDLWIGWGVPKERCIVVKPGDVVKIKDIEIHVLDSFDRTALVTLPADQK 125

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 90111702 197 AAGVLPDGMDDRAVNYLFKTPGGSLYHSGDSHYSNYYAKHGNEHQIDVALGSY 249
Cdd:cd16284 126 LAGKMPDDMDERAVNYLFKTPGGSLYHSGDSHYSNYYAKHGNDHKIDVALGSY 178
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 35-294 1.55e-46

L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 157.77  E-value: 1.55e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702  35 PGTFAMWWLGCTGIWLKSeGGTNVCVDFWCgTGKQSHGNPLmkqghqmqrmagvkklqpnlrttpfVLDPFAIRQIDAVL 114
Cdd:COG2220   1 PGGMKITWLGHATFLIET-GGKRILIDPVF-SGRASPVNPL-------------------------PLDPEDLPKIDAVL 53

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702 115 ATHDHNDHIDVNVAAAVMQNCAddvPFIGPKTCVDLWIGWGVPkeRCIVVKPGDVVKVKDIEIHALDAFDRTALitlpad 194
Cdd:COG2220  54 VTHDHYDHLDDATLRALKRTGA---TVVAPLGVAAWLRAWGFP--RVTELDWGESVELGGLTVTAVPARHSSGR------ 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702 195 qkaagvlPDGMDDRAVNYLFKTPGGSLYHSGDSHYSNYYAKHGNEHQIDVALGSYGenprGITDKMTSADMLRMGEALNA 274
Cdd:COG2220 123 -------PDRNGGLWVGFVIETDGKTIYHAGDTGYFPEMKEIGERFPIDVALLPIG----AYPFTMGPEEAAEAARDLKP 191

                       250       260
                ....*....|....*....|
gi 90111702 275 KVVIPFHHDIWSNFQADPQE 294
Cdd:COG2220 192 KVVIPIHYGTFPLLDEDPLE 211
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 91-282 2.99e-08

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 53.08  E-value: 2.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702    91 LQPNLRTTPFVLDPfaIRQIDAVLATHDHNDHI-DVNVAAAVMQNcaddvPFIGPKTCVDLWIGWGVPkercIVVKPGDV 169
Cdd:pfam12706  12 RQQALPALQPGRLR--DDPIDAVLLTHDHYDHLaGLLDLREGRPR-----PLYAPLGVLAHLRRNFPY----LFLLEHYG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702   170 VKVKDIEIH---ALDAFDRTALITlPADQKaAGVLPDGMDDRAVNYLFKTPGGSLYHSGDshySNYYAKHGNE--HQIDV 244
Cdd:pfam12706  81 VRVHEIDWGesfTVGDGGLTVTAT-PARHG-SPRGLDPNPGDTLGFRIEGPGKRVYYAGD---TGYFPDEIGErlGGADL 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 90111702   245 AL---GSYGENPRGITDKMTSADMLRMGEALNAKVVIPFHH 282
Cdd:pfam12706 156 LLldgGAWRDDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 107-180 2.65e-03

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 38.30  E-value: 2.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702    107 IRQIDAVLATHDHNDHIdvNVAAAVMQncADDVPFIGPKTCVDLW----------IGWGVPKERCIVVKPGDVVKVKDIE 176
Cdd:smart00849  33 PKKIDAIILTHGHPDHI--GGLPELLE--APGAPVYAPEGTAELLkdllallgelGAEAEPAPPDRTLKDGDELDLGGGE 108


                   ....
gi 90111702    177 IHAL 180
Cdd:smart00849 109 LEVI 112
 
Name Accession Description Interval E-value
PRK11709 PRK11709
putative L-ascorbate 6-phosphate lactonase; Provisional
 1-354 0e+00

putative L-ascorbate 6-phosphate lactonase; Provisional


Pssm-ID: 236958  Cd Length: 355  Bit Score: 795.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702    1 MSKVKSITRESWILSTFPEWGSWLNEEIEQEQVAPGTFAMWWLGCTGIWLKSEGGTNVCVDFWCGTGKQSHGNPLMKQGH 80
Cdd:PRK11709   1 MSKVKEITRESWILSTFPEWGTWLNEEIEQEVVPPGTFAMWWLGCTGIWLKTEGGTNVCVDLWCGTGKQTHGNPLMKRGH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702   81 QMQRMAGVKKLQPNLRTTPFVLDPFAIRQIDAVLATHDHNDHIDVNVAAAVMQNCADDVPFIGPKTCVDLWIGWGVPKER 160
Cdd:PRK11709  81 QMARMAGVRKLQPNLRTQPFVLDPFAIREIDAVLATHDHSDHIDVNVAAAVLQNCADHVKFIGPQACVDLWIGWGVPKER 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702  161 CIVVKPGDVVKVKDIEIHALDAFDRTALITLPADQKAA-GVLPDGMDDRAVNYLFKTPGGSLYHSGDSHYSNYYAKHGNE 239
Cdd:PRK11709 161 CIVVKPGDVVKVKDIKIHALDSFDRTALVTLPADGKAAgGVLPDDMDRRAVNYLFKTPGGNIYHSGDSHYSNYFAKHGND 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702  240 HQIDVALGSYGENPRGITDKMTSADMLRMGEALNAKVVIPFHHDIWSNFQADPQEIRVLWEMKKDRLKYGFKPFIWQVGG 319
Cdd:PRK11709 241 HQIDVALGSYGENPRGITDKMTSIDILRMAESLNAKVVIPVHHDIWSNFQADPQEILVLWKMRKDRLQYGFHPFIWQVGG 320

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 90111702  320 KFTWPLDKDNFEYHYPRGFDDCFTIEPDLPFKSFL 354
Cdd:PRK11709 321 KFTYPQDKDRFEYHYPRGFDDCFTIEPDLPFKSFL 355
UlaG-like_MBL-fold cd16284
UlaG a putative l-ascorbate-6-P lactonase and related proteins; MBL-fold metallo hydrolase ...
 37-249 5.66e-127

UlaG a putative l-ascorbate-6-P lactonase and related proteins; MBL-fold metallo hydrolase domain; UlaG is essential for L-ascorbate utilization under anaerobic conditions; it is a putative l-ascorbate-6-P lactonase thought to catalyze the hydrolysis of L-ascorbate-6-phosphate to 3-keto-L-gulonate-6-phosphate. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293842  Cd Length: 178  Bit Score: 361.40  E-value: 5.66e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702  37 TFAMWWLGCTGIWLKSEGGTNVCVDFWCgtgkqshgnplmkqghqmqrmagvkklqpnlrttpFVLDPFAIRQIDAVLAT 116
Cdd:cd16284   1 TFAMWWLGCTGIWLKSEGNTNICIDFWC-----------------------------------FVLDPFAIKQIDAVLAT 45

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702 117 HDHNDHIDVNVAAAVMQNCADDVPFIGPKTCVDLWIGWGVPKERCIVVKPGDVVKVKDIEIHALDAFDRTALITLPADQK 196
Cdd:cd16284  46 HDHNDHIDVNVAAAVLQNCAPDVPFIGPQACVDLWIGWGVPKERCIVVKPGDVVKIKDIEIHVLDSFDRTALVTLPADQK 125

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 90111702 197 AAGVLPDGMDDRAVNYLFKTPGGSLYHSGDSHYSNYYAKHGNEHQIDVALGSY 249
Cdd:cd16284 126 LAGKMPDDMDERAVNYLFKTPGGSLYHSGDSHYSNYYAKHGNDHKIDVALGSY 178
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 35-294 1.55e-46

L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 157.77  E-value: 1.55e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702  35 PGTFAMWWLGCTGIWLKSeGGTNVCVDFWCgTGKQSHGNPLmkqghqmqrmagvkklqpnlrttpfVLDPFAIRQIDAVL 114
Cdd:COG2220   1 PGGMKITWLGHATFLIET-GGKRILIDPVF-SGRASPVNPL-------------------------PLDPEDLPKIDAVL 53

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702 115 ATHDHNDHIDVNVAAAVMQNCAddvPFIGPKTCVDLWIGWGVPkeRCIVVKPGDVVKVKDIEIHALDAFDRTALitlpad 194
Cdd:COG2220  54 VTHDHYDHLDDATLRALKRTGA---TVVAPLGVAAWLRAWGFP--RVTELDWGESVELGGLTVTAVPARHSSGR------ 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702 195 qkaagvlPDGMDDRAVNYLFKTPGGSLYHSGDSHYSNYYAKHGNEHQIDVALGSYGenprGITDKMTSADMLRMGEALNA 274
Cdd:COG2220 123 -------PDRNGGLWVGFVIETDGKTIYHAGDTGYFPEMKEIGERFPIDVALLPIG----AYPFTMGPEEAAEAARDLKP 191

                       250       260
                ....*....|....*....|
gi 90111702 275 KVVIPFHHDIWSNFQADPQE 294
Cdd:COG2220 192 KVVIPIHYGTFPLLDEDPLE 211
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 109-294 4.51e-09

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 55.97  E-value: 4.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702  109 QIDAVLATHDHNDHI-DvnvAAAVMQNCadDVPFIGPktcVDL--WIGW-GVPKerCIVVKPGDVVKVKDIEIHALDAFD 184
Cdd:PRK00685  40 KVDYILLTHGHGDHLgD---TVEIAKRT--GATVIAN---AELanYLSEkGVEK--THPMNIGGTVEFDGGKVKLTPALH 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702  185 RTALITLPadqkaaGVLPDGMddrAVNYLFKTPGGSLYHSGDSHYSNYYAKHGNEHQIDVALGSYGENprgITdkMTSAD 264
Cdd:PRK00685 110 SSSFIDED------GITYLGN---PTGFVITFEGKTIYHAGDTGLFSDMKLIGELHKPDVALLPIGDN---FT--MGPED 175

                        170       180       190
                 ....*....|....*....|....*....|
gi 90111702  265 MLRMGEALNAKVVIPFHHDIWSNFQADPQE 294
Cdd:PRK00685 176 AALAVELIKPKIVIPMHYNTFPLIEQDPEK 205
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 91-282 2.99e-08

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 53.08  E-value: 2.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702    91 LQPNLRTTPFVLDPfaIRQIDAVLATHDHNDHI-DVNVAAAVMQNcaddvPFIGPKTCVDLWIGWGVPkercIVVKPGDV 169
Cdd:pfam12706  12 RQQALPALQPGRLR--DDPIDAVLLTHDHYDHLaGLLDLREGRPR-----PLYAPLGVLAHLRRNFPY----LFLLEHYG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702   170 VKVKDIEIH---ALDAFDRTALITlPADQKaAGVLPDGMDDRAVNYLFKTPGGSLYHSGDshySNYYAKHGNE--HQIDV 244
Cdd:pfam12706  81 VRVHEIDWGesfTVGDGGLTVTAT-PARHG-SPRGLDPNPGDTLGFRIEGPGKRVYYAGD---TGYFPDEIGErlGGADL 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 90111702   245 AL---GSYGENPRGITDKMTSADMLRMGEALNAKVVIPFHH 282
Cdd:pfam12706 156 LLldgGAWRDDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 84-249 2.90e-06

Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293841  Cd Length: 181  Bit Score: 46.89  E-value: 2.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702  84 RMAGVKklqpnlRTTPFVLDPFAIRQIDAVLATHDHNDHIDVNVAAAVMQNCADDVPFiGPKtcvDLWIGWGVPKerciV 163
Cdd:cd16283  30 SFGGPK------RLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPPYLVPL-GLK---KWFLKKGITN----V 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702 164 VKP--GDVVKVKDIEIHALDA--FDRTALitlpadqkaagvlpdgMDDRAV---NYLFKTPGGSLYHSGDSHYSNYYAKH 236
Cdd:cd16283  96 VELdwWQSTEIGGVRITFVPAqhWSRRTL----------------FDTNESlwgGWVIEGEGFRIYFAGDTGYFPGFREI 159

                       170
                ....*....|....*..
gi 90111702 237 GNEHQ-IDVAL---GSY 249
Cdd:cd16283 160 GRRFGpIDLALlpiGAY 176
Lactamase_B_3 pfam13483
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 101-281 1.58e-05

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 433247 [Multi-domain]  Cd Length: 160  Bit Score: 44.50  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702   101 VLDPFAI--------RQIDAVLATHDHNDHidvnvaaavmqNCADDVPFIGPktcvdlwigwgvpkerciVVKPGDVVKV 172
Cdd:pfam13483  20 LTDPFRAtvgyrpppVTADLVLISHGHDDH-----------GHPETLPGNPH------------------VLDGGGSYTV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702   173 KDIEIHALdafdrtalitlPADQKAAGVLPDGmddRAVNYLFKTPGGSLYHSGDSHY---SNYYAKHGNehqIDVAL--- 246
Cdd:pfam13483  71 GGLEIRGV-----------PTDHDRVGGRRRG---GNSIFLFEQDGLTIYHLGHLGHplsDEQLAELGR---VDVLLipv 133

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 90111702   247 -GSYGenprgitdkMTSADMLRMGEALNAKVVIPFH 281
Cdd:pfam13483 134 gGPLT---------YGAEEALELAKRLRPRVVIPMH 160
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 108-180 3.27e-05

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 44.20  E-value: 3.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702 108 RQIDAVLATHDHNDHIDVNVAAAVMQNC-----ADDVPFI--GPKTCVDLWIGWGVPKERCIVVKPGDVVKVKDIEIHAL 180
Cdd:cd06262  44 LKIKAILLTHGHFDHIGGLAELKEAPGApvyihEADAELLedPELNLAFFGGGPLPPPEPDILLEDGDTIELGGLELEVI 123
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 107-123 2.51e-04

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry. Some members of this subgroup are named as octanoyltransferase (also known as lipoate-protein ligase B).


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 41.69  E-value: 2.51e-04
                        10
                ....*....|....*..
gi 90111702 107 IRQIDAVLATHDHNDHI 123
Cdd:cd16279  64 IRKLDAVLLTHAHADHI 80
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 110-226 2.85e-04

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized Enterococcus faecalis EF2904. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293818 [Multi-domain]  Cd Length: 202  Bit Score: 41.44  E-value: 2.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702 110 IDAVLATHDHNDHIdvnvaaAVMQNCADDVP-FIGPKTC-------VDLWIGWGVPKERcIVVKPGDVVKVKDIEIHAL- 180
Cdd:cd07732  76 VDAVLLSHAHLDHY------GLLNYLRPDIPvYMGEATKrilkallPFFGEGDPVPRNI-RVFESGKSFTIGDFTVTPYl 148

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 90111702 181 ---DAFDrtalitlpadqkaagvlpdgmddrAVNYLFKTPGGSLYHSGD 226
Cdd:cd07732 149 vdhSAPG------------------------AYAFLIEAPGKRIFYTGD 173
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 109-181 4.33e-04

hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293809 [Multi-domain]  Cd Length: 165  Bit Score: 40.52  E-value: 4.33e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111702 109 QIDAVLATHDHNDHIDVNvaAAVMQNCAdDVPFIGPKtcvdlwigwgvpKERC----IVVKPGDVVKVKDIEIHALD 181
Cdd:cd07723  43 TLTAILTTHHHWDHTGGN--AELKALFP-DAPVYGPA------------EDRIpgldHPVKDGDEIKLGGLEVKVLH 104
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 101-180 5.82e-04

DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 41.00  E-value: 5.82e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702 101 VLDPF----AIRQIDAVLATHDHNDHI--------DVNVAAAVMQNCADDVPFIgpKTCVDLWIGWGVPKERCivvKPGD 168
Cdd:COG2333  40 VVLPYlralGIRRLDLLVLTHPDADHIgglaavleAFPVGRVLVSGPPDTSETY--ERLLEALKEKGIPVRPC---RAGD 114

                        90
                ....*....|..
gi 90111702 169 VVKVKDIEIHAL 180
Cdd:COG2333 115 TWQLGGVRFEVL 126
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 107-123 2.29e-03

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 38.65  E-value: 2.29e-03
                        10
                ....*....|....*..
gi 90111702 107 IRQIDAVLATHDHNDHI 123
Cdd:cd07731  46 IKKLDYLILTHPDADHI 62
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 107-287 2.36e-03

Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism];


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 39.11  E-value: 2.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702 107 IRQIDAVLATHDHNDHI-DVNVAAAVMQNcaDDVPFIGP-------KTCVDLWIGWGVPKERCIVVKPGDVVKVKDIEIH 178
Cdd:COG1235  66 PSKIDAILLTHEHADHIaGLDDLRPRYGP--NPIPVYATpgtlealERRFPYLFAPYPGKLEFHEIEPGEPFEIGGLTVT 143

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702 179 AL----DAFDRTALiTLPADQKAAGVLPD--GMDDRAVNYLfktpggslyhSG------DSHYSNYYAKHgnehqidval 246
Cdd:COG1235 144 PFpvphDAGDPVGY-RIEDGGKKLAYATDtgYIPEEVLELL----------RGadllilDATYDDPEPGH---------- 202

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 90111702 247 gsygenprgitdkMTSADMLRMGEALNAKVVIPFHHDIWSN 287
Cdd:COG1235 203 -------------LSNEEALELLARLGPKRLVLTHLSPDNN 230
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 107-180 2.65e-03

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 38.30  E-value: 2.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702    107 IRQIDAVLATHDHNDHIdvNVAAAVMQncADDVPFIGPKTCVDLW----------IGWGVPKERCIVVKPGDVVKVKDIE 176
Cdd:smart00849  33 PKKIDAIILTHGHPDHI--GGLPELLE--APGAPVYAPEGTAELLkdllallgelGAEAEPAPPDRTLKDGDELDLGGGE 108


                   ....
gi 90111702    177 IHAL 180
Cdd:smart00849 109 LEVI 112
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 54-123 2.72e-03

Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; Includes the archaeal cleavage and polyadenylation specificity factors (CPSFs) such as Methanothermobacter thermautotrophicus MTH1203, and Pyrococcus horikoshii PH1404. In addition to the MBL-fold metallo-hydrolase nuclease and the beta-CASP domains, members of this subgroup contain two contiguous KH domains. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 38.59  E-value: 2.72e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702  54 GGTNVCVDfwCGtgkqshgnplMKQGhqmqrmagvKKLQPNLRTTPFvldPFAIRQIDAVLATHDHNDHI 123
Cdd:cd16295  20 GGKRILLD--CG----------LFQG---------GKELEELNNEPF---PFDPKEIDAVILTHAHLDHS 65
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 107-230 2.83e-03

Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudoalteromonas carrageenovora arylsulfatase AtsA may function as a glycosulfohydrolase involved with desulfation of sulfated polysaccharides, which catalyzes hydrolysis of the arylsulfate ester bond, producing the aryl compounds and inorganic sulfate. CD also includes some sequences annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily.


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 38.27  E-value: 2.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111702 107 IRQIDAVLATHDHNDHI----DVNVAAAVMQNcADDVPFIGPK------------TCVDLWIGWGVPKERciVVKPGDVV 170
Cdd:cd07719  49 LGDLDAVFLTHLHSDHVadlpALLLTAWLAGR-KTPLPVYGPPgtralvdgllaaYALDIDYRARIGDEG--RPDPGALV 125

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111702 171 KVKDIEIHAlDAFDRTAL-ITlpadqkAAGVlPDGMDDRAVNYLFKTPGGSLYHSGDSHYS 230
Cdd:cd07719 126 EVHEIAAGG-VVYEDDGVkVT------AFLV-DHGPVPPALAYRFDTPGRSVVFSGDTGPS 178
 
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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