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Conserved domains on  [gi|1955861279|ref|XP_038888633|]
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bifunctional riboflavin kinase/FMN phosphatase-like [Benincasa hispida]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02940 super family cl31957
riboflavin kinase
 7-355 1.54e-114

riboflavin kinase


The actual alignment was detected with superfamily member PLN02940:

Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 338.35  E-value: 1.54e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   7 VSAVILDLDGTLLDTERATKDVLKDFLAKYGKVWDKkREEEKRLGMTQKESAAAIVRDYGLPLTPDQFIQEITPMYREKW 86
Cdd:PLN02940   11 VSHVILDLDGTLLNTDGIVSDVLKAFLVKYGKQWDG-REAQKIVGKTPLEAAATVVEDYGLPCSTDEFNSEITPLLSEQW 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  87 PSVKALPGADRLLKHLYSHKVPFGLASNSSSEFIHAKISCMKGWKDWFSVILGSDQVIEGKPAPYLFEEAAKRMGVDASH 166
Cdd:PLN02940   90 CNIKALPGANRLIKHLKSHGVPMALASNSPRANIEAKISCHQGWKESFSVIVGGDEVEKGKPSPDIFLEAAKRLNVEPSN 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279 167 CLVIEDSLIGVKAAKAAKMKVIAVPS--RGEIECSSlADKVLNSLLEFEPELWGLPPFEDWVDRTLPIDPIYLSSHYVNG 244
Cdd:PLN02940  170 CLVIEDSLPGVMAGKAAGMEVIAVPSipKQTHLYSS-ADEVINSLLDLQPEKWGLPPFNDWIEGTLPIEPWHIGGPVIKG 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279 245 -------------SMSEISEDASLPDQVFGTFFGWGGTVMAWTIKVVVNIGWNCSSCTKRNRIwKLWSVDGCDSKVFEQQ 311
Cdd:PLN02940  249 fgrgskvlgiptaNLSTENYSDVLSEHPSGVYFGWAGLSTRGVYKMVMSIGWNPYFNNTEKTI-EPWLLHDFGEDFYGEE 327

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1955861279 312 MQFMLVGYIR-RLNSTDLENIdVREIEEFKYIANTSLDRPMFVDH 355
Cdd:PLN02940  328 LRLVIVGYIRpEANFPSLESL-IAKIHEDRRIAEKALDLPLYAKY 371
 
Name Accession Description Interval E-value
PLN02940 PLN02940
riboflavin kinase
 7-355 1.54e-114

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 338.35  E-value: 1.54e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   7 VSAVILDLDGTLLDTERATKDVLKDFLAKYGKVWDKkREEEKRLGMTQKESAAAIVRDYGLPLTPDQFIQEITPMYREKW 86
Cdd:PLN02940   11 VSHVILDLDGTLLNTDGIVSDVLKAFLVKYGKQWDG-REAQKIVGKTPLEAAATVVEDYGLPCSTDEFNSEITPLLSEQW 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  87 PSVKALPGADRLLKHLYSHKVPFGLASNSSSEFIHAKISCMKGWKDWFSVILGSDQVIEGKPAPYLFEEAAKRMGVDASH 166
Cdd:PLN02940   90 CNIKALPGANRLIKHLKSHGVPMALASNSPRANIEAKISCHQGWKESFSVIVGGDEVEKGKPSPDIFLEAAKRLNVEPSN 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279 167 CLVIEDSLIGVKAAKAAKMKVIAVPS--RGEIECSSlADKVLNSLLEFEPELWGLPPFEDWVDRTLPIDPIYLSSHYVNG 244
Cdd:PLN02940  170 CLVIEDSLPGVMAGKAAGMEVIAVPSipKQTHLYSS-ADEVINSLLDLQPEKWGLPPFNDWIEGTLPIEPWHIGGPVIKG 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279 245 -------------SMSEISEDASLPDQVFGTFFGWGGTVMAWTIKVVVNIGWNCSSCTKRNRIwKLWSVDGCDSKVFEQQ 311
Cdd:PLN02940  249 fgrgskvlgiptaNLSTENYSDVLSEHPSGVYFGWAGLSTRGVYKMVMSIGWNPYFNNTEKTI-EPWLLHDFGEDFYGEE 327

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1955861279 312 MQFMLVGYIR-RLNSTDLENIdVREIEEFKYIANTSLDRPMFVDH 355
Cdd:PLN02940  328 LRLVIVGYIRpEANFPSLESL-IAKIHEDRRIAEKALDLPLYAKY 371
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
9-212 5.07e-54

Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 176.94  E-value: 5.07e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   9 AVILDLDGTLLDTERATKDVLKDFLAKYGKVWDkkREEEKRL-GMTQKESAAAIVRDYGLPLTPDQFIQEITPMYRE--K 85
Cdd:COG0637     4 AVIFDMDGTLVDSEPLHARAWREAFAELGIDLT--EEEYRRLmGRSREDILRYLLEEYGLDLPEEELAARKEELYREllA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  86 WPSVKALPGADRLLKHLYSHKVPFGLASNSSSEFIHAKISCMkGWKDWFSVILGSDQVIEGKPAPYLFEEAAKRMGVDAS 165
Cdd:COG0637    82 EEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAA-GLLDYFDVIVTGDDVARGKPDPDIYLLAAERLGVDPE 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1955861279 166 HCLVIEDSLIGVKAAKAAKMKVIAVPSRGEIECS-SLADKVLNSLLEF 212
Cdd:COG0637   161 ECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEElAGADLVVDDLAEL 208
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 7-191 6.85e-41

subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and Gpp2; This subfamily includes Arabidopsis thaliana AtGpp1 and AtGpp2, and Drosophila GS1-like protein (Dmel\Gs1l) of unknown function. AtGpp1 and AtGpp2 are constitutively expressed in all the Arabidopsis tissues and unaffected under abiotic stress. Overexpression of AtGpp2 in transgenic Arabidopsis plants increases the specific DL-glycerol-3-phosphatase activity and improves the plants tolerance to salt, osmotic and oxidative stress. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319831 [Multi-domain]  Cd Length: 192  Bit Score: 142.49  E-value: 6.85e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   7 VSAVILDLDGTLLDTERATKDVLKDFLAKYGKV--WDKKReeeKRLGMTQKESAAAIVRDYGLPLTPDQ-FIQEITPMYR 83
Cdd:cd07529     1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTytWDVKA---KMMGRPASEAARIIVDELKLPMSLEEeFDEQQEALAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  84 EKWPSVKALPGADRLLKHLYSHKVPFGLASNSssefiHAKISCMKG--WKDWFS----VILGSD--QVIEGKPAPYLFEE 155
Cdd:cd07529    78 LFMGTAKLMPGAERLLRHLHAHNIPIALATSS-----CTRHFKLKTsrHKELFSlfhhVVTGDDpeVKGRGKPAPDIFLV 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1955861279 156 AAKRMG---VDASHCLVIEDSLIGVKAAKAAKMKVIAVP 191
Cdd:cd07529   153 AAKRFNeppKDPSKCLVFEDSPNGVKAAKAAGMQVVMVP 191
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 7-177 1.04e-26

beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: the characterized beta-phosphoglucomutases (including those from E.coli, B.subtilus and L.lactis, TIGR01990), a clade of putative bPGM's from mycobacteria and a clade including the uncharacterized E.coli and H.influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the "variant 3" glu-asp version of the third conserved HAD domain (TIGR01509).


Pssm-ID: 213673 [Multi-domain]  Cd Length: 185  Bit Score: 104.73  E-value: 1.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   7 VSAVILDLDGTLLDTERATKDVLKDFLAKYGKVWDKKREEEKRlGMTQKESAAAIVRDYGLPLTPDQFIQ---EITPMYR 83
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLK-GLSREDILRAILKLRGDGLSLEEIHQlaeRKNELYR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  84 EKWP--SVKALPGADRLLKHLYSHKVPFGLASNS-SSEFIHAKIscmkGWKDWFSVILGSDQVIEGKPAPYLFEEAAKRM 160
Cdd:TIGR02009  80 ELLRltGVAVLPGIRNLLKRLKAKGIAVGLGSSSkNAPRILAKL----GLRDYFDAIVDASEVKNGKPHPETFLLAAELL 155

                         170
                  ....*....|....*..
gi 1955861279 161 GVDASHCLVIEDSLIGV 177
Cdd:TIGR02009 156 GVPPNECIVFEDALAGV 172
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 7-177 3.23e-20

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 87.26  E-value: 3.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   7 VSAVILDLDGTLLDTERATKDVLKD----------FLAKYGKVWDKKREEEKRLGMTQKE--SAAAIVRDYGLPLTPDQF 74
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAElasehplakaIVAAAEDLPIPVEDFTARLLLGKRDwlEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  75 IQEITPMYREKW--PSVKALPGADRLLKHLYSHKVPFGLASNSSSEFIHAKISCMkGWKDWFSVILGSDQVIEGKPAPYL 152
Cdd:pfam00702  81 TVVLVELLGVIAlaDELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLL-GLDDYFDVVISGDDVGVGKPKPEI 159

                         170       180
                  ....*....|....*....|....*
gi 1955861279 153 FEEAAKRMGVDASHCLVIEDSLIGV 177
Cdd:pfam00702 160 YLAALERLGVKPEEVLMVGDGVNDI 184
 
Name Accession Description Interval E-value
PLN02940 PLN02940
riboflavin kinase
 7-355 1.54e-114

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 338.35  E-value: 1.54e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   7 VSAVILDLDGTLLDTERATKDVLKDFLAKYGKVWDKkREEEKRLGMTQKESAAAIVRDYGLPLTPDQFIQEITPMYREKW 86
Cdd:PLN02940   11 VSHVILDLDGTLLNTDGIVSDVLKAFLVKYGKQWDG-REAQKIVGKTPLEAAATVVEDYGLPCSTDEFNSEITPLLSEQW 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  87 PSVKALPGADRLLKHLYSHKVPFGLASNSSSEFIHAKISCMKGWKDWFSVILGSDQVIEGKPAPYLFEEAAKRMGVDASH 166
Cdd:PLN02940   90 CNIKALPGANRLIKHLKSHGVPMALASNSPRANIEAKISCHQGWKESFSVIVGGDEVEKGKPSPDIFLEAAKRLNVEPSN 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279 167 CLVIEDSLIGVKAAKAAKMKVIAVPS--RGEIECSSlADKVLNSLLEFEPELWGLPPFEDWVDRTLPIDPIYLSSHYVNG 244
Cdd:PLN02940  170 CLVIEDSLPGVMAGKAAGMEVIAVPSipKQTHLYSS-ADEVINSLLDLQPEKWGLPPFNDWIEGTLPIEPWHIGGPVIKG 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279 245 -------------SMSEISEDASLPDQVFGTFFGWGGTVMAWTIKVVVNIGWNCSSCTKRNRIwKLWSVDGCDSKVFEQQ 311
Cdd:PLN02940  249 fgrgskvlgiptaNLSTENYSDVLSEHPSGVYFGWAGLSTRGVYKMVMSIGWNPYFNNTEKTI-EPWLLHDFGEDFYGEE 327

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1955861279 312 MQFMLVGYIR-RLNSTDLENIdVREIEEFKYIANTSLDRPMFVDH 355
Cdd:PLN02940  328 LRLVIVGYIRpEANFPSLESL-IAKIHEDRRIAEKALDLPLYAKY 371
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
9-212 5.07e-54

Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 176.94  E-value: 5.07e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   9 AVILDLDGTLLDTERATKDVLKDFLAKYGKVWDkkREEEKRL-GMTQKESAAAIVRDYGLPLTPDQFIQEITPMYRE--K 85
Cdd:COG0637     4 AVIFDMDGTLVDSEPLHARAWREAFAELGIDLT--EEEYRRLmGRSREDILRYLLEEYGLDLPEEELAARKEELYREllA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  86 WPSVKALPGADRLLKHLYSHKVPFGLASNSSSEFIHAKISCMkGWKDWFSVILGSDQVIEGKPAPYLFEEAAKRMGVDAS 165
Cdd:COG0637    82 EEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAA-GLLDYFDVIVTGDDVARGKPDPDIYLLAAERLGVDPE 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1955861279 166 HCLVIEDSLIGVKAAKAAKMKVIAVPSRGEIECS-SLADKVLNSLLEF 212
Cdd:COG0637   161 ECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEElAGADLVVDDLAEL 208
PLN02811 PLN02811
hydrolase
 14-224 5.09e-44

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 151.45  E-value: 5.09e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  14 LDGTLLDTERATKDVLKDFLAKYGKV--WDKKreeEKRLGMTQKESAAAIVRDYGLP--LTPDQFIQEITPMYREKWPSV 89
Cdd:PLN02811    1 MDGLLLDTEKFYTEVQEKILARYGKTfdWSLK---AKMMGKKAIEAARIFVEESGLSdsLSPEDFLVEREAMLQDLFPTS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  90 KALPGADRLLKHLYSHKVPFGLASNSSSEFIHAKIScmkGWKDWFS----VILGSD-QVIEGKPAPYLFEEAAKRM---G 161
Cdd:PLN02811   78 DLMPGAERLVRHLHAKGIPIAIATGSHKRHFDLKTQ---RHGELFSlmhhVVTGDDpEVKQGKPAPDIFLAAARRFedgP 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1955861279 162 VDASHCLVIEDSLIGVKAAKAAKMKVIAVP-SRGEIECSSLADKVLNSLLEFEPELWGLPPFED 224
Cdd:PLN02811  155 VDPGKVLVFEDAPSGVEAAKNAGMSVVMVPdPRLDKSYCKGADQVLSSLLDFKPEEWGLPPFPD 218
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 7-191 6.85e-41

subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and Gpp2; This subfamily includes Arabidopsis thaliana AtGpp1 and AtGpp2, and Drosophila GS1-like protein (Dmel\Gs1l) of unknown function. AtGpp1 and AtGpp2 are constitutively expressed in all the Arabidopsis tissues and unaffected under abiotic stress. Overexpression of AtGpp2 in transgenic Arabidopsis plants increases the specific DL-glycerol-3-phosphatase activity and improves the plants tolerance to salt, osmotic and oxidative stress. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319831 [Multi-domain]  Cd Length: 192  Bit Score: 142.49  E-value: 6.85e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   7 VSAVILDLDGTLLDTERATKDVLKDFLAKYGKV--WDKKReeeKRLGMTQKESAAAIVRDYGLPLTPDQ-FIQEITPMYR 83
Cdd:cd07529     1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTytWDVKA---KMMGRPASEAARIIVDELKLPMSLEEeFDEQQEALAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  84 EKWPSVKALPGADRLLKHLYSHKVPFGLASNSssefiHAKISCMKG--WKDWFS----VILGSD--QVIEGKPAPYLFEE 155
Cdd:cd07529    78 LFMGTAKLMPGAERLLRHLHAHNIPIALATSS-----CTRHFKLKTsrHKELFSlfhhVVTGDDpeVKGRGKPAPDIFLV 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1955861279 156 AAKRMG---VDASHCLVIEDSLIGVKAAKAAKMKVIAVP 191
Cdd:cd07529   153 AAKRFNeppKDPSKCLVFEDSPNGVKAAKAAGMQVVMVP 191
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 9-192 1.57e-32

beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; This family represents the beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. Family members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. It belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319808 [Multi-domain]  Cd Length: 143  Bit Score: 118.87  E-value: 1.57e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   9 AVILDLDGTLLDTERAtkdvlkdflakYGKVWdkkreeekrlgmtqkesaaaivrdyglpltpdQFIQEITPMYREKWPS 88
Cdd:cd07505     1 AVIFDMDGVLIDTEPL-----------HRQAW--------------------------------QLLERKNALLLELIAS 37

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  89 --VKALPGADRLLKHLYSHKVPFGLASNSSSEFIHAKISCMKGWKDWFSVILGSDQVIEGKPAPYLFEEAAKRMGVDASH 166
Cdd:cd07505    38 egLKLKPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLLRGYFDVIVSGDDVERGKPAPDIYLLAAERLGVDPER 117

                         170       180
                  ....*....|....*....|....*.
gi 1955861279 167 CLVIEDSLIGVKAAKAAKMKVIAVPS 192
Cdd:cd07505   118 CLVFEDSLAGIEAAKAAGMTVVAVPD 143
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
9-216 6.67e-28

Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 108.86  E-value: 6.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   9 AVILDLDGTLLDTERATKDVLKDFLAKYGKvwdkKREEEKRLGMTQKESAAAIVRDYgLPLTPDQFIQEITPMYREKW-- 86
Cdd:COG0546     3 LVLFDLDGTLVDSAPDIAAALNEALAELGL----PPLDLEELRALIGLGLRELLRRL-LGEDPDEELEELLARFRELYee 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  87 ---PSVKALPGADRLLKHLYSHKVPFGLASNSSSEFIHAKISCMkGWKDWFSVILGSDQVIEGKPAPYLFEEAAKRMGVD 163
Cdd:COG0546    78 ellDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEAL-GLDDYFDAIVGGDDVPPAKPKPEPLLEALERLGLD 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955861279 164 ASHCLVIEDSLI--------GVkaakaakmKVIAVP----SRGEIEcSSLADKVLNSLLEFEPEL 216
Cdd:COG0546   157 PEEVLMVGDSPHdieaaraaGV--------PFIGVTwgygSAEELE-AAGADYVIDSLAELLALL 212
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 7-177 1.04e-26

beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: the characterized beta-phosphoglucomutases (including those from E.coli, B.subtilus and L.lactis, TIGR01990), a clade of putative bPGM's from mycobacteria and a clade including the uncharacterized E.coli and H.influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the "variant 3" glu-asp version of the third conserved HAD domain (TIGR01509).


Pssm-ID: 213673 [Multi-domain]  Cd Length: 185  Bit Score: 104.73  E-value: 1.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   7 VSAVILDLDGTLLDTERATKDVLKDFLAKYGKVWDKKREEEKRlGMTQKESAAAIVRDYGLPLTPDQFIQ---EITPMYR 83
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLK-GLSREDILRAILKLRGDGLSLEEIHQlaeRKNELYR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  84 EKWP--SVKALPGADRLLKHLYSHKVPFGLASNS-SSEFIHAKIscmkGWKDWFSVILGSDQVIEGKPAPYLFEEAAKRM 160
Cdd:TIGR02009  80 ELLRltGVAVLPGIRNLLKRLKAKGIAVGLGSSSkNAPRILAKL----GLRDYFDAIVDASEVKNGKPHPETFLLAAELL 155

                         170
                  ....*....|....*..
gi 1955861279 161 GVDASHCLVIEDSLIGV 177
Cdd:TIGR02009 156 GVPPNECIVFEDALAGV 172
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 7-174 1.22e-24

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 100.10  E-value: 1.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   7 VSAVILDLDGTLLDTER-------------ATKDVLKDFLAKYGKVWDKKREEEKRLGMTQKESAAAIVRDYGLPLTPDQ 73
Cdd:COG1011     1 IKAVLFDLDGTLLDFDPviaealralaerlGLLDEAEELAEAYRAIEYALWRRYERGEITFAELLRRLLEELGLDLAEEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  74 FIQeitpmYREKWPS-VKALPGADRLLKHLYSHKVPFGLASNSSSEFIHAKISCMkGWKDWFSVILGSDQVIEGKPAPYL 152
Cdd:COG1011    81 AEA-----FLAALPElVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRL-GLDDLFDAVVSSEEVGVRKPDPEI 154

                         170       180
                  ....*....|....*....|..
gi 1955861279 153 FEEAAKRMGVDASHCLVIEDSL 174
Cdd:COG1011   155 FELALERLGVPPEEALFVGDSP 176
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 9-211 4.14e-21

uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized Bacillus subtilis YhcW; This subfamily includes the uncharacterized Bacillus subtilis YhcW. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319859 [Multi-domain]  Cd Length: 169  Bit Score: 88.85  E-value: 4.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   9 AVILDLDGTLLDTERATKDVLKDFLAKygkvwdKKREEEKRLGmtqkesaaaivrdyglpltpdqfiqeitpmyrEKWPS 88
Cdd:cd16423     1 AVIFDFDGVIVDTEPLWYEAWQELLNE------RRNELIKRQF--------------------------------SEKTD 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  89 VKALPGADRLLKHLYSHKVPFGLASNSSSEFIhakISCMK--GWKDWFSVILGSDQVIEGKPAPYLFEEAAKRMGVDASH 166
Cdd:cd16423    43 LPPIEGVKELLEFLKEKGIKLAVASSSPRRWI---EPHLErlGLLDYFEVIVTGDDVEKSKPDPDLYLEAAERLGVNPEE 119

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1955861279 167 CLVIEDSLIGVKAAKAAKMKVIAVPSR--GEIECSSlADKVLNSLLE 211
Cdd:cd16423   120 CVVIEDSRNGVLAAKAAGMKCVGVPNPvtGSQDFSK-ADLVLSSFAE 165
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 9-176 5.46e-21

subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides xylulose-1,5-bisphosphate phosphatase CbbY; This family includes Rhodobacter sphaeroides and Arabidopsis thaliana xylulose-1,5-bisphosphate phosphatase CbbY which convert xylulose-1,5-bisphosphate (a potent inhibitor of Ribulose-1,5-bisphosphate carboxylase/oxygenase, Rubisco), to the non-inhibitory compound xylulose-5-phosphate. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319830 [Multi-domain]  Cd Length: 199  Bit Score: 89.75  E-value: 5.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   9 AVILDLDGTLLDTERATKDVLKD-FLAKYGKVWDKKREEEKRLGMTQ--KESAAAIVRDYG----LPLTPDQFIQEI--- 78
Cdd:cd07528     1 ALIFDVDGTLAETEELHRRAFNNaFFAERGLDWYWDRELYGELLRVGggKERIAAYFEKVGwpesAPKDLKELIADLhka 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  79 -TPMYRE--KWPSVKALPGADRLLKHLYSHKVPFGLASNSSSEFIHAKISCMKG--WKDWFSVILGSDQVIEGKPAPYLF 153
Cdd:cd07528    81 kTERYAEliAAGLLPLRPGVARLIDEAKAAGVRLAIATTTSPANVDALLSALLGpeRRAIFDAIAAGDDVAEKKPDPDIY 160

                         170       180
                  ....*....|....*....|...
gi 1955861279 154 EEAAKRMGVDASHCLVIEDSLIG 176
Cdd:cd07528   161 LLALERLGVSPSDCLAIEDSAIG 183
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 9-177 2.29e-20

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 87.48  E-value: 2.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   9 AVILDLDGTLLDTERATKDVLKDFLAKYGKVWDKKREEEKRLGMTQKESAaaivrDYG---LPLTPDQFIQEITPMYREK 85
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAIAKLINREELGLVPDELGVSAVGRLELALRRFKA-----QYGrtiSPEDAQLLYKQLFYEQIEE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  86 WPSVKALPGADRLLKHLYSHKVPFGLASNSssEFIHAKISCMKGWKDWFSVILGSDQVIEGKPAPYLFEEAAKRMGVDAS 165
Cdd:TIGR01509  76 EAKLKPLPGVRALLEALRARGKKLALLTNS--PRAHKLVLALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGLEPS 153

                         170
                  ....*....|..
gi 1955861279 166 HCLVIEDSLIGV 177
Cdd:TIGR01509 154 ECVFVDDSPAGI 165
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 7-177 3.23e-20

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 87.26  E-value: 3.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   7 VSAVILDLDGTLLDTERATKDVLKD----------FLAKYGKVWDKKREEEKRLGMTQKE--SAAAIVRDYGLPLTPDQF 74
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAElasehplakaIVAAAEDLPIPVEDFTARLLLGKRDwlEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  75 IQEITPMYREKW--PSVKALPGADRLLKHLYSHKVPFGLASNSSSEFIHAKISCMkGWKDWFSVILGSDQVIEGKPAPYL 152
Cdd:pfam00702  81 TVVLVELLGVIAlaDELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLL-GLDDYFDVVISGDDVGVGKPKPEI 159

                         170       180
                  ....*....|....*....|....*
gi 1955861279 153 FEEAAKRMGVDASHCLVIEDSLIGV 177
Cdd:pfam00702 160 YLAALERLGVKPEEVLMVGDGVNDI 184
bPGM TIGR01990
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 9-190 2.67e-19

beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which catalyzes the interconverison of beta-D-glucose-1-phosphate and beta-D-glucose-6-phosphate. The 6-phosphate is capable of non-enzymatic anomerization (alpha <-> beta) while the 1-phosphate is not. A separate enzyme is responsible for the isomerization of the alpha anomers. Beta-D-glucose-1-phosphate results from the phosphorylysis of maltose (2.4.1.8), trehalose (2.4.1.64) or trehalose-6-phosphate (2.4.1.216). Alternatively, these reactions can be run in the synthetic direction to create the disaccharides. All sequenced genomes which contain a member of this family also appear to contain at least one putative maltose or trehalose phosphorylase. Three species, Lactococcus, Enterococcus and Neisseria appear to contain a pair of paralogous beta-PGM's. Beta-phosphoglucomutase is a member of the haloacid dehalogenase superfamily of hydrolase enzymes. These enzymes are characterized by a series of three catalytic motifs positioned within an alpha-beta (Rossman) fold. beta-PGM contains an inserted alpha helical domain in between the first and second conserved motifs and thus is a member of subfamily IA of the superfamily. The third catalytic motif comes in three variants, the third of which, containing a conserved DD or ED, is the only one found here as well as in several other related enzymes (TIGR01509). The enzyme from L. lactis has been extensively characterized including a remarkable crystal structure which traps the pentacoordinate transition state. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 213672 [Multi-domain]  Cd Length: 185  Bit Score: 84.67  E-value: 2.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   9 AVILDLDGTLLDTERATKDVLKDFLAKYGKVWDKKREEEKRlGMTQKESAAAIVRDYGLPLTPDQF-------------- 74
Cdd:TIGR01990   1 AVIFDLDGVITDTAEYHYLAWKHLADELGIPFDEEFNESLK-GVSREESLERILDLGGKKYSEEEKeelaerkndyyvel 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  75 IQEITPmyrekwpsVKALPGADRLLKHLYSHKVPFGLASNS-SSEFIHAKIscmkGWKDWFSVILGSDQVIEGKPAPYLF 153
Cdd:TIGR01990  80 LKELTP--------ADVLPGIKSLLADLKKNNIKIALASASkNAPTILEKL----ELIDYFDAIVDPAELKKGKPDPEIF 147

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1955861279 154 EEAAKRMGVDASHCLVIEDSLIGVKAAKAAKMKVIAV 190
Cdd:TIGR01990 148 LAAAEGLGVSPSECIGIEDAQAGIEAIKAAGMFAVGV 184
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
10-190 5.87e-19

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 83.40  E-value: 5.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  10 VILDLDGTLLDTERATKDVLKDFLAKYGKVwDKKREE-EKRLGMTQKESAAAivrdyglpLTPDQFIQEITPMYREKW-- 86
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYG-ELSEEEiLKFIGLPLREIFRY--------LGVSEDEEEKIEFYLRKYne 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  87 ----PSVKALPGADRLLKHLYSHKVPFGLASNSSSEFIhakISCMK--GWKDWFSVILGSDQVIEGKPAPYLFEEAAKRM 160
Cdd:pfam13419  72 elhdKLVKPYPGIKELLEELKEQGYKLGIVTSKSRENV---EEFLKqlGLEDYFDVIVGGDDVEGKKPDPDPILKALEQL 148

                         170       180       190
                  ....*....|....*....|....*....|
gi 1955861279 161 GVDASHCLVIEDSLIGVKAAKAAKMKVIAV 190
Cdd:pfam13419 149 GLKPEEVIYVGDSPRDIEAAKNAGIKVIAV 178
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 9-177 3.55e-18

subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli 6-phosphogluconate phosphatase YieH; This subfamily includes Escherichia coli YieH/HAD3 an 6-phosphogluconate phosphatase, which can hydrolyzed purines and pyrimidines as secondary substrates. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate, and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319828 [Multi-domain]  Cd Length: 141  Bit Score: 80.06  E-value: 3.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   9 AVILDLDGTLLDTERATKDVLKDFLAKYGKvwdkkreeekrlgmtqkESAAAIVRDyglpltpdqfiqeitpmyrekwps 88
Cdd:cd07526     2 LVIFDCDGVLVDSEVIAARVLVEVLAELGA-----------------RVLAAFEAE------------------------ 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  89 VKALPGADRLLKHLyshKVPFGLASNSSSEFIHAKISCMkGWKDWF-SVILGSDQVIEGKPAPYLFEEAAKRMGVDASHC 167
Cdd:cd07526    41 LQPIPGAAAALSAL---TLPFCVASNSSRERLTHSLGLA-GLLAYFeGRIFSASDVGRGKPAPDLFLHAAAQMGVAPERC 116

                         170
                  ....*....|
gi 1955861279 168 LVIEDSLIGV 177
Cdd:cd07526   117 LVIEDSPTGV 126
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
9-177 3.86e-15

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 72.80  E-value: 3.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   9 AVILDLDGTLLDTERATKDVLKDFLAKYGKVWDkkreeEKRL----GMTQKESAAAIVRDYGLPLTPDQFIQEITPMYRE 84
Cdd:PRK10725    7 GLIFDMDGTILDTEPTHRKAWREVLGRYGLQFD-----EQAMvalnGSPTWRIAQAIIELNQADLDPHALAREKTEAVKS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  85 K-WPSVKALPGADrLLKHLYSHKvPFGLASNSSSEFIHAKISCMkGWKDWFSVILGSDQVIEGKPAPYLFEEAAKRMGVD 163
Cdd:PRK10725   82 MlLDSVEPLPLIE-VVKAWHGRR-PMAVGTGSESAIAEALLAHL-GLRRYFDAVVAADDVQHHKPAPDTFLRCAQLMGVQ 158

                         170
                  ....*....|....
gi 1955861279 164 ASHCLVIEDSLIGV 177
Cdd:PRK10725  159 PTQCVVFEDADFGI 172
PRK10826 PRK10826
hexitol phosphatase HxpB;
1-216 5.62e-15

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 73.44  E-value: 5.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   1 MNFVGGVSAVILDLDGTLLDTE----RATKDVLK--------------------DFLAKYgkvWDKKREEEkrlGMTQKE 56
Cdd:PRK10826    1 MSTPRQILAAIFDMDGLLIDSEplwdRAELDVMAslgvdisrreelpdtlglriDQVVDL---WYARQPWN---GPSRQE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  57 SAAAIVrdyglpltpDQFIQEItpmyREKWPsvkALPGADRLLKHLYSHKVPFGLASNSSSEFIHAKIScMKGWKDWFSV 136
Cdd:PRK10826   75 VVQRII---------ARVISLI----EETRP---LLPGVREALALCKAQGLKIGLASASPLHMLEAVLT-MFDLRDYFDA 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279 137 ILGSDQVIEGKPAPYLFEEAAKRMGVDASHCLVIEDSLIGVKAAKAAKMKVIAVPS---RGEiECSSLADKVLNSLLEFE 213
Cdd:PRK10826  138 LASAEKLPYSKPHPEVYLNCAAKLGVDPLTCVALEDSFNGMIAAKAARMRSIVVPApeqQND-PRWALADVKLESLTELT 216


                  ...
gi 1955861279 214 PEL 216
Cdd:PRK10826  217 AAD 219
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 9-211 6.99e-14

beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); Lactococcus lactis beta-PGM catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate as an intermediate. In the forward G6P-forming direction, this reaction links polysaccharide phosphorolysis to glycolysis, in the reverse direction, the reaction provides G1P for the biosynthesis of exo-polysaccharides. This subfamily belongs to the beta-phosphoglucomutase-like family whose other members include Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319788 [Multi-domain]  Cd Length: 174  Bit Score: 68.86  E-value: 6.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   9 AVILDLDGTLLDTeratkdvlkdflAKYgKVWDKKREEEKrlgmtqKESAAAIVRDYglpltpDQFIQEITPmyrekwps 88
Cdd:cd02598     1 GVIFDLDGVITDT------------AEY-HYRAWKKLADK------EELAARKNRIY------VELIEELTP-------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  89 VKALPGADRLLKHLYSHKVPFGLASNS-SSEFIHAKIscmkGWKDWFSVILGSDQVIEGKPAPYLFEEAAKRMGVDASHC 167
Cdd:cd02598    48 VDVLPGIASLLVDLKAKGIKIALASASkNAPKILEKL----GLAEYFDAIVDGAVLAKGKPDPDIFLAAAEGLGLNPKDC 123

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1955861279 168 LVIEDSLIGVKAAKAAKMKVIAVpsrGEIECSSLADKVLNSLLE 211
Cdd:cd02598   124 IGVEDAQAGIRAIKAAGFLVVGV---GREEDLLGADIVVPDTTA 164
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 8-177 8.97e-13

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 67.81  E-value: 8.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   8 SAVILDLDGTLLDTER-----ATKDVLKDF--------LAKYGKVWDKKREEEKrlgMTQ--KESAAAIVRDYGLPLTPD 72
Cdd:PLN02779   41 EALLFDCDGVLVETERdghrvAFNDAFKEFglrpvewdVELYDELLNIGGGKER---MTWyfNENGWPTSTIEKAPKDEE 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  73 Q---FIQEI----TPMYRE--KWPSVKALPGADRLLKHLYSHKVPFGLASNSSSEFIHAKISCMKGWK--DWFSVILGsD 141
Cdd:PLN02779  118 ErkeLVDSLhdrkTELFKEliESGALPLRPGVLRLMDEALAAGIKVAVCSTSNEKAVSKIVNTLLGPEraQGLDVFAG-D 196

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1955861279 142 QVIEGKPAPYLFEEAAKRMGVDASHCLVIEDSLIGV 177
Cdd:PLN02779  197 DVPKKKPDPDIYNLAAETLGVDPSRCVVVEDSVIGL 232
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 9-190 1.01e-12

subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p); This subfamily includes Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p). GPP1p and GPP2p are involved in glycerol biosynthesis, GPP1 is induced in response to both anaerobic and hyperosmotic stress, GPP2 is induced in response to hyperosmotic or oxidative stress, and during diauxic shift; overexpression of DOG1 or DOG2 confers 2-deoxyglucose resistance. These belong to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319829 [Multi-domain]  Cd Length: 205  Bit Score: 66.60  E-value: 1.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   9 AVILDLDGTLLDTERATKDVLKDFLAKYGkvwDKKREEEKRL-GMTqkesAAAIVRDYGLPLTPDQFI----QEITPMYR 83
Cdd:cd07527     1 ALLFDMDGTLVDSTPAVERAWHKWAKEHG---VDPEEVLKVShGRR----AIDVIRKLAPDDADIELVlaleTEEPESYP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  84 EKwpsVKALPGADRLLKHLYSHKVPFGLASNSSSEFIHAKISCMKGWKDwfSVILGSDQVIEGKPAPYLFEEAAKRMGVD 163
Cdd:cd07527    74 EG---VIAIPGAVDLLASLPAAGDRWAIVTSGTRALAEARLEAAGLPHP--EVLVTADDVKNGKPDPEPYLLGAKLLGLD 148

                         170       180
                  ....*....|....*....|....*..
gi 1955861279 164 ASHCLVIEDSLIGVKAAKAAKMKVIAV 190
Cdd:cd07527   149 PSDCVVFEDAPAGIKAGKAAGARVVAV 175
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 7-173 2.12e-12

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 65.38  E-value: 2.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   7 VSAVILDLDGTLLDTeraTKDVLKDF---LAKYG-KVWdkKREEEKR-LGMTQKESAAAIvrdygLPLTPDQFIQEITPM 81
Cdd:cd02616     1 ITTILFDLDGTLIDT---NELIIKSFnhtLKEYGlEGY--TREEVLPfIGPPLRETFEKI-----DPDKLEDMVEEFRKY 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  82 YREKWPS-VKALPGADRLLKHLYSHKVPFGLASNSSSEFIHAKISCMkGWKDWFSVILGSDQVIEGKPAPYLFEEAAKRM 160
Cdd:cd02616    71 YREHNDDlTKEYPGVYETLARLKSQGIKLGVVTTKLRETALKGLKLL-GLDKYFDVIVGGDDVTHHKPDPEPVLKALELL 149

                         170
                  ....*....|...
gi 1955861279 161 GVDASHCLVIEDS 173
Cdd:cd02616   150 GAEPEEALMVGDS 162
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 9-175 8.98e-11

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions.The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)(D/E), (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 60.10  E-value: 8.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   9 AVILDLDGTLLDTERATKDVLKDFLAKYGKVwdkkREEEKRLGMTQKESAAAIVRDygLPLTPDQFIQEITPMYREKWps 88
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFGLD----PASFKALKQAGGLAEEEWYRI--ATSALEELQGRFWSEYDAEE-- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  89 vKALPGADRLLKHLYSHKVPFGLASNSSSEFIHAKISCMKGwKDWFSVILGSDqVIEGKPAPYLFEEAAKRMGVDaSHCL 168
Cdd:TIGR01549  73 -AYIRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGL-GDYFELILVSD-EPGSKPEPEIFLAALESLGVP-PEVL 148


                  ....*..
gi 1955861279 169 VIEDSLI 175
Cdd:TIGR01549 149 HVGDNLN 155
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 5-190 4.38e-10

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 61.41  E-value: 4.38e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279    5 GGVSAVILDLDGTLLDTERATKDVLKDFLAKYGKvwdKKREEE--KRLGMTQKESAAAIVRDYGLP-LTPDQFIQEITPM 81
Cdd:PLN02919    73 GKVSAVLFDMDGVLCNSEEPSRRAAVDVFAEMGV---EVTVEDfvPFMGTGEANFLGGVASVKGVKgFDPDAAKKRFFEI 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   82 YREKWP---SVKALPGADRLLKHLYSHKVPFGLASNSSSEFIHAKISCMKGWKDWFSVILGSDQVIEGKPAPYLFEEAAK 158
Cdd:PLN02919   150 YLEKYAkpnSGIGFPGALELITQCKNKGLKVAVASSADRIKVDANLAAAGLPLSMFDAIVSADAFENLKPAPDIFLAAAK 229

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1955861279  159 RMGVDASHCLVIEDSLIGVKAAKAAKMKVIAV 190
Cdd:PLN02919   230 ILGVPTSECVVIEDALAGVQAARAAGMRCIAV 261
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 90-212 1.92e-09

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 57.73  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  90 KALPGADRLLKHLYSHKVPFGLASNSSSEFIHAKISCMkGWKDWFSVILGSDQVIEGKPAPYLFEEAAKRMGVDASHCLV 169
Cdd:PLN03243  109 RLRPGSREFVQALKKHEIPIAVASTRPRRYLERAIEAV-GMEGFFSVVLAAEDVYRGKPDPEMFMYAAERLGFIPERCIV 187

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1955861279 170 IEDSLIGVKAAKAAKMKVIAVPSRGEIECSSLADKVLNSLLEF 212
Cdd:PLN03243  188 FGNSNSSVEAAHDGCMKCVAVAGKHPVYELSAGDLVVRRLDDL 230
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 92-174 4.49e-09

human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases; N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 53.70  E-value: 4.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  92 LPGADRLLKHLySHKVPFGLASNSSSEFIHAKISCMkGWKDWFSVILGSDQVIEGKPAPYLFEEAAKRMGVDASHCLVIE 171
Cdd:cd04305    11 LPGAKELLEEL-KKGYKLGIITNGPTEVQWEKLEQL-GIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETLMVG 88


                  ...
gi 1955861279 172 DSL 174
Cdd:cd04305    89 DSL 91
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 9-174 4.64e-09

Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGP; EC 3.1.3.18) catalyzes the conversion of 2-phosphoglycolate into glycolate and phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319854 [Multi-domain]  Cd Length: 212  Bit Score: 55.70  E-value: 4.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   9 AVILDLDGTLLDT----ERATKDVLKDF-LAKYGK-------------------VWDKKREEEKRLgmtQKESAAAIVRD 64
Cdd:cd16417     1 LVAFDLDGTLVDSapdlAEAANAMLAALgLPPLPEetvrtwigngadvlveralTGAREAEPDEEL---FKEARALFDRH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  65 YGLPLTpdqfiqEITPMYrekwpsvkalPGADRLLKHLYSHKVPFGLASNSSSEFIhAKISCMKGWKDWFSVILGSDQVI 144
Cdd:cd16417    78 YAETLS------VHSHLY----------PGVKEGLAALKAQGYPLACVTNKPERFV-APLLEALGISDYFSLVLGGDSLP 140

                         170       180       190
                  ....*....|....*....|....*....|
gi 1955861279 145 EGKPAPYLFEEAAKRMGVDASHCLVIEDSL 174
Cdd:cd16417   141 EKKPDPAPLLHACEKLGIAPAQMLMVGDSR 170
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 7-177 9.70e-09

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 55.09  E-value: 9.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   7 VSAVILDLDGTLLDTERATKDVLKDFLAKYGKVWDKKREEEKRLGMTQKESAAAIVRDYGLPLTpdqfIQEITPMYREKW 86
Cdd:PRK10563    4 IEAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLSLEEVFKRFKGVKLYEIIDIISKEHGVTLA----KAELEPVYRAEV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  87 P-----SVKALPGADRLLKHLyshKVPFGLASNSSsefihakISCMK------GWKDWFSVILGSDQVIEG-KPAPYLFE 154
Cdd:PRK10563   80 ArlfdsELEPIAGANALLESI---TVPMCVVSNGP-------VSKMQhslgktGMLHYFPDKLFSGYDIQRwKPDPALMF 149

                         170       180
                  ....*....|....*....|...
gi 1955861279 155 EAAKRMGVDASHCLVIEDSLIGV 177
Cdd:PRK10563  150 HAAEAMNVNVENCILVDDSSAGA 172
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 95-190 2.54e-08

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 51.24  E-value: 2.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  95 ADRLLKHLYSHKVPFGLASNSSSEFIHAKIScMKGWKDWFSVILGSDQVIEGKPAPYLFEEAAKRMGVDASHCLVIEDSL 174
Cdd:cd01427    12 AVELLKRLRAAGIKLAIVTNRSREALRALLE-KLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSE 90

                          90
                  ....*....|....*.
gi 1955861279 175 IGVKAAKAAKMKVIAV 190
Cdd:cd01427    91 NDIEAARAAGGRTVAV 106
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 9-177 1.24e-07

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 51.58  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   9 AVILDLDGTLLDTERA------TKDVLKDFLAKYGKVWDKKREEEKRLG-MTQKESAAAIVRDYGLPLTPDQFIQEITPM 81
Cdd:cd02603     3 AVLFDFGGVLIDPDPAaavarfEALTGEPSEFVLDTEGLAGAFLELERGrITEEEFWEELREELGRPLSAELFEELVLAA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  82 YrekwpsvKALPGADRLLKHLYSHKVPFGLASNSSSEFIHAKISCMKGWKDWFSVILGSDQVIEGKPAPYLFEEAAKRMG 161
Cdd:cd02603    83 V-------DPNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLPRRGDLFDGVVESCRLGVRKPDPEIYQLALERLG 155

                         170
                  ....*....|....*.
gi 1955861279 162 VDASHCLVIEDSLIGV 177
Cdd:cd02603   156 VKPEEVLFIDDREENV 171
PRK11587 PRK11587
putative phosphatase; Provisional
 13-209 1.33e-07

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 51.53  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  13 DLDGTLLDT----ERATKDvlkdflakygkvWDKKR--EEEKRLGMTQKESAAAIVRDYgLPLTPDQFIQEiTPMYREKW 86
Cdd:PRK11587    9 DLDGTLVDSlpavERAWSN------------WADRHgiAPDEVLNFIHGKQAITSLRHF-MAGASEAEIQA-EFTRLEQI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  87 PS-----VKALPGADRLLKHLYSHKVPFGLASNSSSEFIHA--KISCMKGWKDWFSvilgSDQVIEGKPAP--YLFeeAA 157
Cdd:PRK11587   75 EAtdtegITALPGAIALLNHLNKLGIPWAIVTSGSVPVASArhKAAGLPAPEVFVT----AERVKRGKPEPdaYLL--GA 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1955861279 158 KRMGVDASHCLVIEDSLIGVKAAKAAKMKVIAVPSRGEIECSSLADKVLNSL 209
Cdd:PRK11587  149 QLLGLAPQECVVVEDAPAGVLSGLAAGCHVIAVNAPADTPRLDEVDLVLHSL 200
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
9-216 4.09e-07

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 50.19  E-value: 4.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   9 AVILDLDGTLLDT-----------------ERATKDVLKDFLakyGKVWDK--KREEEKRLGMTQKESAAAIVRDYglpl 69
Cdd:PRK13222    8 AVAFDLDGTLVDSapdlaaavnaalaalglPPAGEERVRTWV---GNGADVlvERALTWAGREPDEELLEKLRELF---- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  70 tpDQFIQEITPMYREKWPSVKALpgadrlLKHLYSHKVPFGLASNSSSEFIhAKISCMKGWKDWFSVILGSDQVIEGKPA 149
Cdd:PRK13222   81 --DRHYAENVAGGSRLYPGVKET------LAALKAAGYPLAVVTNKPTPFV-APLLEALGIADYFSVVIGGDSLPNKKPD 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955861279 150 PYLFEEAAKRMGVDASHCLVIEDSLIGVKAAKAAKMKVIAVP---SRGE-IEcSSLADKVLNSLLEFEPEL 216
Cdd:PRK13222  152 PAPLLLACEKLGLDPEEMLFVGDSRNDIQAARAAGCPSVGVTygyNYGEpIA-LSEPDVVIDHFAELLPLL 221
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 9-173 1.75e-06

haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter sphaeroides CbbZ; Phosphoglycolate phosphatase catalyzes the dephosphorylation of phosphoglycolate; its activity requires divalent cations, especially Mg++. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319815 [Multi-domain]  Cd Length: 214  Bit Score: 48.47  E-value: 1.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   9 AVILDLDGTLLDTERATKDVLKDFLAKYGK-----------VWDKKREEEKRLGMTQKESAAAIVRDYGLPLtpdqFIQE 77
Cdd:cd07512     1 AVIFDLDGTLIDSAPDLHAALNAVLAAEGLaplslaevrsfVGHGAPALIRRAFAAAGEDLDGPLHDALLAR----FLDH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  78 itpmYREKWPSVKAL-PGADRLLKHLYSHKVPFGLASNSSSEFIHAKISCMkGWKDWFSVILGSDQVIEGKPAPYLFEEA 156
Cdd:cd07512    77 ----YEADPPGLTRPyPGVIEALERLRAAGWRLAICTNKPEAPARALLSAL-GLADLFAAVVGGDTLPQRKPDPAPLRAA 151

                         170
                  ....*....|....*..
gi 1955861279 157 AKRMGVDASHCLVIEDS 173
Cdd:cd07512   152 IRRLGGDVSRALMVGDS 168
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 9-169 3.25e-06

L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 47.65  E-value: 3.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   9 AVILDLDGTLLDTERATKDVLKDFLAKYGKV---W-DKKREEEKRLGMTQ---------KESAAAIVRDYGLPLTPDQFI 75
Cdd:cd02588     2 ALVFDVYGTLIDWHSGLAAAERAFPGRGEELsrlWrQKQLEYTWLVTLMGpyvdfdeltRDALRATAAELGLELDESDLD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  76 QEITPMYREK-WPSVKalPGADRLlkhlysHKVPFGLA--SNSSSEFI-----HAKIScmkgwkDWFSVILGSDQVIEGK 147
Cdd:cd02588    82 ELGDAYLRLPpFPDVV--AGLRRL------REAGYRLAilSNGSPDLIedvvaNAGLR------DLFDAVLSAEDVRAYK 147

                         170       180
                  ....*....|....*....|...
gi 1955861279 148 PAPYLFEEAAKRMGVDAS-HCLV 169
Cdd:cd02588   148 PAPAVYELAAERLGVPPDeILHV 170
Hydrolase_like pfam13242
HAD-hyrolase-like;
144-174 8.52e-06

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 43.37  E-value: 8.52e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1955861279 144 IEGKPAPYLFEEAAKRMGVDASHCLVIEDSL 174
Cdd:pfam13242   1 VCGKPNPGMLERALARLGLDPERTVMIGDRL 31
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 7-173 1.38e-05

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 45.79  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   7 VSAVILDLDGTLLDTERAtkdVLKDFLAKYGKVWDK--KREEekrlgmtqkesaaaIVRDYGLPLTpDQF-------IQE 77
Cdd:PRK13288    3 INTVLFDLDGTLINTNEL---IISSFLHTLKTYYPNqyKRED--------------VLPFIGPSLH-DTFskideskVEE 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  78 ITPMYRE-----KWPSVKALPGADRLLKHLYSHKVPFGLASNSSSEFIHAKISCMkGWKDWFSVILGSDQVIEGKPAPYL 152
Cdd:PRK13288   65 MITTYREfnhehHDELVTEYETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLT-GLDEFFDVVITLDDVEHAKPDPEP 143

                         170       180
                  ....*....|....*....|.
gi 1955861279 153 FEEAAKRMGVDASHCLVIEDS 173
Cdd:PRK13288  144 VLKALELLGAKPEEALMVGDN 164
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 9-172 3.46e-05

phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase PGP/CbbZ; Phosphoglycolate phosphatase catalyzes the dephosphorylation of phosphoglycolate; its activity requires divalent cations, especially Mg++. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319799 [Multi-domain]  Cd Length: 201  Bit Score: 44.27  E-value: 3.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   9 AVILDLDGTLLDTERATKDVLKDFLAKYGkvWDKKREEEkrLGMTQKESAAAIVRDYGLPLTPDQFI-QEITPMYREKWP 87
Cdd:cd04303     1 LIIFDFDGTLADSFPWFLSILNQLAARHG--FKTVDEEE--IEQLRQLSSREILKQLGVPLWKLPLIaKDFRRLMAEAAP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  88 SVKALPGADRLLKHLYSHKVPFGLASNSSSEFIHAKIScMKGWKDWFSVILGSDqvIEGKPApyLFEEAAKRMGVDASHC 167
Cdd:cd04303    77 ELALFPGVEDMLRALHARGVRLAVVSSNSEENIRRVLG-PEELISLFAVIEGSS--LFGKAK--KIRRVLRRTKITAAQV 151


                  ....*
gi 1955861279 168 LVIED 172
Cdd:cd04303   152 IYVGD 156
PRK13225 PRK13225
phosphoglycolate phosphatase; Provisional
 7-149 4.04e-05

phosphoglycolate phosphatase; Provisional


Pssm-ID: 106187 [Multi-domain]  Cd Length: 273  Bit Score: 44.70  E-value: 4.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   7 VSAVILDLDGTLLDTERATKDVLKDFLAKYGkvWDKKreEEKRLGMTQKESAAAIVRDYGL-PLTPDQFIQEITPMYREK 85
Cdd:PRK13225   62 LQAIIFDFDGTLVDSLPTVVAIANAHAPDFG--YDPI--DERDYAQLRQWSSRTIVRRAGLsPWQQARLLQRVQRQLGDC 137

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1955861279  86 WPSVKALPGADRLLKHLYSHKVPFGLASNSSSEFIHAKIScMKGWKDWFSVILGSDQVIEGKPA 149
Cdd:PRK13225  138 LPALQLFPGVADLLAQLRSRSLCLGILSSNSRQNIEAFLQ-RQGLRSLFSVVQAGTPILSKRRA 200
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 94-211 5.72e-05

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 44.86  E-value: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  94 GADRLLKHLYSHKVPFGLASNSSSEFIHAKISCMkGWKDWFSVILGSDQVIEGKPAPYLFEEAAKRMGVDASHCLVIEDS 173
Cdd:PLN02575  220 GSQEFVNVLMNYKIPMALVSTRPRKTLENAIGSI-GIRGFFSVIVAAEDVYRGKPDPEMFIYAAQLLNFIPERCIVFGNS 298

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1955861279 174 LIGVKAAKAAKMKVIAVPSRGEIECSSLADKVLNSLLE 211
Cdd:PLN02575  299 NQTVEAAHDARMKCVAVASKHPIYELGAADLVVRRLDE 336
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 10-190 1.99e-04

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to Parvibaculum lavamentivorans HAD-superfamily hydrolase, subfamily IA, variant 1; This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319835 [Multi-domain]  Cd Length: 207  Bit Score: 42.00  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  10 VILDLDGTLLDTERATKDVLKDFLAKYGKVwDKKREEEKRL-GMTQKEsaaAIVRDYGLPlTPD------QFIQEITPMY 82
Cdd:cd07533     2 VIFDWDGTLADSQHNIVAAMTAAFADLGLP-VPSAAEVRSIiGLSLDE---AIARLLPMA-TPAlvavaeRYKEAFDILR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  83 REKWPSVKALPGADRLLKHLYSHKVPFGLASNSSSEFIHAKIScMKGWKDWFSVILGSDQViEGKPAPYLFEEAAKRMGV 162
Cdd:cd07533    77 LLPEHAEPLFPGVREALDALAAQGVLLAVATGKSRRGLDRVLE-QHGLGGYFDATRTADDT-PSKPHPEMLREILAELGV 154

                         170       180
                  ....*....|....*....|....*...
gi 1955861279 163 DASHCLVIEDSLIGVKAAKAAKMKVIAV 190
Cdd:cd07533   155 DPSRAVMVGDTAYDMQMAANAGAHAVGV 182
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 146-174 2.24e-04

inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP); LHPP hydrolyzes nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate as well as oxygen-phosphorus bonds in inorganic pyrophosphate in vitro. This family also includes human haloacid dehalogenase like hydrolase domain containing 2 protine (HDHD2) a phosphatase which may be involved in polygenic hypertension. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319812 [Multi-domain]  Cd Length: 248  Bit Score: 42.27  E-value: 2.24e-04
                          10        20
                  ....*....|....*....|....*....
gi 1955861279 146 GKPAPYLFEEAAKRMGVDASHCLVIEDSL 174
Cdd:cd07509   171 GKPSPEFFLSALRSLGVDPEEAVMIGDDL 199
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 9-193 6.58e-04

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 40.98  E-value: 6.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279   9 AVILDLDGTLLDTE----RATKDVLKDFLAKYGKVWDKKREEEKRLGMTQKESAaaivrdygLPLTPD------QFIQEI 78
Cdd:PLN02770   24 AVLFDVDGTLCDSDplhyYAFREMLQEINFNGGVPITEEFFVENIAGKHNEDIA--------LGLFPDdlerglKFTDDK 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  79 TPMYREKWPS-VKALPGADRLLKHLYSHKVPFGLASNSSSEFIHAKISCMkGWKDWF-SVILGSD-QVIEGKPAPYLfeE 155
Cdd:PLN02770   96 EALFRKLASEqLKPLNGLYKLKKWIEDRGLKRAAVTNAPRENAELMISLL-GLSDFFqAVIIGSEcEHAKPHPDPYL--K 172

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1955861279 156 AAKRMGVDASHCLVIEDSLIGVKAAKAAKMKVIAVPSR 193
Cdd:PLN02770  173 ALEVLKVSKDHTFVFEDSVSGIKAGVAAGMPVVGLTTR 210
HAD_Pase_UmpH-like cd07531
UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar ...
 142-211 1.83e-03

UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar phosphatase; Bacillus subtilis AraL is a phosphatase displaying activity towards different sugar phosphate substrates; it is encoded by the arabinose metabolic operon araABDLMNPQ-abfA and may play a role in the dephosphorylation of substrates related to l-arabinose metabolism. This subfamily belongs to the UmpH/NagD phosphatase family, and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319833 [Multi-domain]  Cd Length: 252  Bit Score: 39.48  E-value: 1.83e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1955861279 142 QVIEGKPAPYLFEEAAKRMGVDASHCLVIEDSL-----IGVKAAKAAKMKVIAVPSRGEIECSSLA-DKVLNSLLE 211
Cdd:cd07531   175 EVVVGKPSEVMAREALDILGLDAKDCAIVGDQIdvdiaMGKAIGMETALVLTGVTTRENLDRHGYKpDYVLNSIKD 250
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 11-154 1.96e-03

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the uncharacterized Lactococcus lactis YsbA; The specific function of Lactococcus lactis YsbA is unknown. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases


Pssm-ID: 319825 [Multi-domain]  Cd Length: 173  Bit Score: 38.51  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  11 ILDLDGTLLDTERATKDVLKDFLAKYGKVWDKKREEEkrlgmTQKESAAAIVRDYGLPLtPDQFiQEITPMYREKWPSVK 90
Cdd:cd07523     3 IWDLDGTLLDSYPAMTKALSETLADFGIPQDLETVYK-----IIKESSVQFAIQYYAEV-PDLE-EEYKELEAEYLAKPI 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1955861279  91 ALPGADRLLK---------HLYSHKvpfglasNSSSEFIHAKIscmkGWKDWFSVILGSDQVIEGKPAP----YLFE 154
Cdd:cd07523    76 LFPGAKAVLRwikeqggknFLMTHR-------DHSALTILKKD----GIASYFTEIVTSDNGFPRKPNPeainYLLN 141
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 147-174 2.30e-03

Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino acid transport and metabolism]; Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 440011 [Multi-domain]  Cd Length: 176  Bit Score: 38.54  E-value: 2.30e-03
                          10        20
                  ....*....|....*....|....*...
gi 1955861279 147 KPAPYLFEEAAKRMGVDASHCLVIEDSL 174
Cdd:COG0241   102 KPKPGMLLQAAERLGIDLSNSYMIGDRL 129
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
 139-174 2.67e-03

haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this UmpH/NagD family include Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase , Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase, human PGP phosphoglycolate phosphatase, Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase, Bacillus AraL a putative sugar phosphatase, and Plasmodium falciparum para nitrophenyl phosphate phosphatase PNPase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319811 [Multi-domain]  Cd Length: 270  Bit Score: 39.27  E-value: 2.67e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1955861279 139 GSDQVIEGKPAPYLFEEAAKRMGVDASHCLVIEDSL 174
Cdd:cd07508   189 GRQPLVLGKPSPWLGELALEKFGIDPERVLFVGDRL 224
PRK09449 PRK09449
dUMP phosphatase; Provisional
 90-174 4.25e-03

dUMP phosphatase; Provisional


Pssm-ID: 181865 [Multi-domain]  Cd Length: 224  Bit Score: 38.34  E-value: 4.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  90 KALPGADRLLKHLYShKVPFGLASNSSSEFIHAKIScMKGWKDWFSVILGSDQVIEGKPAPYLFEEAAKRMG-VDASHCL 168
Cdd:PRK09449   95 TPLPGAVELLNALRG-KVKMGIITNGFTELQQVRLE-RTGLRDYFDLLVISEQVGVAKPDVAIFDYALEQMGnPDRSRVL 172


                  ....*.
gi 1955861279 169 VIEDSL 174
Cdd:PRK09449  173 MVGDNL 178
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 129-175 5.12e-03

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to uncharacterized Drosophila melanogaster rhythmically expressed gene 2 protein and human haloacid dehalogenase-like hydrolase domain-containing protein 3; The haloacid dehalogenase-like (HAD) hydrolases are a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319852 [Multi-domain]  Cd Length: 128  Bit Score: 36.89  E-value: 5.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1955861279 129 GWKDWFSVILGSDQVIEGKPAPYLFEEAAKRMGVDASHCLVIEDSLI 175
Cdd:cd16415    44 GLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSPEEALHVGDDLK 90
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 82-175 8.26e-03

histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal domain of the Escherichia coli bifunctional enzyme histidinol-phosphate phosphatase/imidazole-glycerol-phosphate dehydratase, HisB. The N-terminal histidinol-phosphate phosphatase domain catalyzes the dephosphorylation of histidinol phosphate, the eight step of L-histidine biosynthesis. This family also includes Escherichia coli GmhB phosphatase which is highly specific for D-glycero-D-manno-heptose-1,7-bisphosphate, it removes the C(7)phosphate and not the C(1)phosphate, and this is the third essential step of lipopolysaccharide heptose biosynthesis. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319806 [Multi-domain]  Cd Length: 142  Bit Score: 36.36  E-value: 8.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955861279  82 YREKWPSVKALPGADRLLKHLYSHKVPFGLASNSS-------SEFIHAKIScmkgwkDWFSVILGSDQV-IEG------- 146
Cdd:cd07503    17 YVHKPEDLEFLPGVIEALKKLKDAGYLVVVVTNQSgiargyfSEADFEALH------DKMRELLASQGVeIDDiyycphh 90

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1955861279 147 --------KPAPYLFEEAAKRMGVDASHCLVIEDSLI 175
Cdd:cd07503    91 pddgcpcrKPKPGMLLDAAKELGIDLARSFVIGDRLS 127
 
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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