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Conserved domains on  [gi|755398009|gb|AJJ15215|]
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HAD hydrolase, IA, variant 1 family protein [Yersinia pestis]

Protein Classification

HAD-IIA family hydrolase( domain architecture ID 11484729)

HAD-IIA family hydrolase similar to Escherichia coli ribonucleotide monophosphatase NagD, which catalyzes the dephosphorylation of an unusually broad range of substrate including deoxyribo- and ribonucleoside tri-, di-, and monophosphates, as well as polyphosphate and glucose-1-P (Glu1P)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10444 PRK10444
HAD-IIA family hydrolase;
3-250 0e+00

HAD-IIA family hydrolase;


:

Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 520.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009   3 IKSVICDIDGVLLHDNTAIKGANDFLARIQDAGMPLVILTNYPSQTAQDLTNRFITAGLDVPESAFYTSAMATADFLRRQ 82
Cdd:PRK10444   1 IKNVICDIDGVLMHDNVAVPGAAEFLHRILDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFLRRQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009  83 DGKKAYVIGEGALVHELYKAGFTITDINPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDSHGHGFAPACGALCAP 162
Cdd:PRK10444  81 EGKKAYVIGEGALIHELYKAGFTITDINPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDTHGRGFYPACGALCAG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009 163 IEKISGRKPFYVGKPSPWIIRAALNKMQAHSESTVIVGDNLRTDILAGFQAGLETILVLSGVSTLTDIDAMPFRPSYVYP 242
Cdd:PRK10444 161 IEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILVLSGVSTLDDIDSMPFRPSWIYP 240

                 ....*...
gi 755398009 243 SVADIDII 250
Cdd:PRK10444 241 SVADIDVI 248
 
Name Accession Description Interval E-value
PRK10444 PRK10444
HAD-IIA family hydrolase;
3-250 0e+00

HAD-IIA family hydrolase;


Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 520.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009   3 IKSVICDIDGVLLHDNTAIKGANDFLARIQDAGMPLVILTNYPSQTAQDLTNRFITAGLDVPESAFYTSAMATADFLRRQ 82
Cdd:PRK10444   1 IKNVICDIDGVLMHDNVAVPGAAEFLHRILDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFLRRQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009  83 DGKKAYVIGEGALVHELYKAGFTITDINPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDSHGHGFAPACGALCAP 162
Cdd:PRK10444  81 EGKKAYVIGEGALIHELYKAGFTITDINPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDTHGRGFYPACGALCAG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009 163 IEKISGRKPFYVGKPSPWIIRAALNKMQAHSESTVIVGDNLRTDILAGFQAGLETILVLSGVSTLTDIDAMPFRPSYVYP 242
Cdd:PRK10444 161 IEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILVLSGVSTLDDIDSMPFRPSWIYP 240

                 ....*...
gi 755398009 243 SVADIDII 250
Cdd:PRK10444 241 SVADIDVI 248
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
4-246 8.27e-122

UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase and Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase; Escherichia coli UmpH/NagD is a ribonucleoside tri-, di-, and monophosphatase with a preference for purines, it shows peak activity with UMP and functions in UMP-degradation. It is also an effective phosphatase with AMP, GMP and CMP. Mycobacterium tuberculosis phosphatase, Rv1692 is a glycerol 3-phosphate phosphatase. Rv1692 is the final enzyme involved in glycerophospholipid recycling/catabolism. 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: 319832 [Multi-domain]  Cd Length: 247  Bit Score: 346.50  E-value: 8.27e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009   4 KSVICDIDGVLLHDNTAIKGANDFLARIQDAGMPLVILTNYPSQTAQDLTNRFITAGLDVPESAFYTSAMATADFLRRQ- 82
Cdd:cd07530    1 KGYLIDLDGTVYRGGTAIPGAVEFIERLREKGIPFLFLTNNSTRTPEDVAAKLAEMGIDVPEEDVYTSALATAQYLAEQl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009  83 DGKKAYVIGEGALVHELYKAGFTITDINPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDSHG---HGFAPACGAL 159
Cdd:cd07530   81 PGAKVYVIGEEGLRTALHEAGLTLTDENPDYVVVGLDRDLTYEKLAEATLAIRNGAKFIATNPDLTLpteRGLLPGNGSV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009 160 CAPIEKISGRKPFYVGKPSPWIIRAALNKMQAHSESTVIVGDNLRTDILAGFQAGLETILVLSGVSTLTDIDAMPFRPSY 239
Cdd:cd07530  161 VAALEAATGVKPLFIGKPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAAGIAAGIDTLLVLTGVTTREDLAKPPYRPTY 240

                 ....*..
gi 755398009 240 VYPSVAD 246
Cdd:cd07530  241 IVPSLRE 247
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
1-249 3.70e-105

Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 304.72  E-value: 3.70e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009   1 MTIKSVICDIDGVLLHDNTAIKGANDFLARIQDAGMPLVILTNYPSQTAQDLTNRFITAGLDVPESAFYTSAMATADFLR 80
Cdd:COG0647    6 DRYDAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATAAYLA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009  81 RQ-DGKKAYVIGEGALVHELYKAGFTIT-DINPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDS---HGHGFAPA 155
Cdd:COG0647   86 ERhPGARVYVIGEEGLREELEEAGLTLVdDEEPDAVVVGLDRTFTYEKLAEALRAIRRGAPFIATNPDRtvpTEDGLIPG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009 156 CGALCAPIEKISGRKPFYVGKPSPWIIRAALNKMQAHSESTVIVGDNLRTDILAGFQAGLETILVLSGVSTLTDIDAMPF 235
Cdd:COG0647  166 AGALAAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAGLDTLLVLTGVTTAEDLEAAPI 245
                        250
                 ....*....|....
gi 755398009 236 RPSYVYPSVADIDI 249
Cdd:COG0647  246 RPDYVLDSLAELLL 259
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
6-223 6.70e-73

Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural subclass of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The classes 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. Class I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Class II consists of sequences in which the capping domain is found between the second and third motifs. Class III sequences have no capping domain in iether of these positions. The Class IIA capping domain is predicted by PSI-PRED to consist of a mixed alpha-beta fold with the basic pattern: Helix-Helix-Helix-Sheet-Helix-Loop-Sheet-Helix-Sheet-Helix. Presently, this subfamily encompasses a single equivalog model (TIGR01452) for the eukaryotic phosphoglycolate phosphatase, as well as four hypothetical equivalogs covering closely related sequences (TIGR01456 and TIGR01458 in eukaryotes, TIGR01457 in gram positive bacteria and TIGR01459 in gram negative bacteria). The Escherishia coli NagD gene and the Bacillus subtilus AraL gene are members of this subfamily but are not members of the any of the presently defined equivalogs within it. NagD is part of the NAG operon responsible for N-acetylglucosamine metabolism. The function of this gene is unknown. Genes from several organisms have been annotated as NagD, or NagD-like. However, without data on the presence of other members of this pathway, (such as in the case of Yersinia pestis) these assignments should not be given great weight. The AraL gene is similar: it is part of the L-arabinose operon, but the function is unknown. A gene from Halobacterium has been annotated as AraL, but no other Ara operon genes have been annotated. Many of the genes in this subfamily have been annotated as "pNPPase" "4-nitrophenyl phosphatase" or "NPPase". These all refer to the same activity versus a common lab test compound used to determine phosphatase activity. There is no evidence that this activity is physiologically relevant. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273637 [Multi-domain]  Cd Length: 236  Bit Score: 222.20  E-value: 6.70e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009    6 VICDIDGVLLHDNTAIKGANDFLARIQDAGMPLVILTNYPSQTAQDLTNRFIT-AGLDVPESAFYTSAMATADFLR-RQD 83
Cdd:TIGR01460   1 FLFDIDGVLWLGHKPIPGAAEALNRLRAKGKPVVFLTNNSSRSEEDYAEKLSSlLGVDVSPDQIITSGSVTKDLLRqRFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009   84 GKKAYVIGEGALVHELYKAGF---TITDIN-------PDFVIVGETRSYNWDMMHKAAYFVANG-ARFIATNPDS---HG 149
Cdd:TIGR01460  81 GEKVYVIGVGELRESLEGLGFrndFFDDIDhlaiekiPAAVIVGEPSDFSYDELAKAAYLLAEGdVPFIAANRDDlvrLG 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755398009  150 HG-FAPACGALCAPIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEST-VIVGDNLRTDILAGFQAGLETILVLSG 223
Cdd:TIGR01460 161 DGrFRPGAGAIAAGIKELSGREPTVVGKPSPAIYRAALNLLQARPERRdVMVGDNLRTDILGAKNAGFDTLLVLTG 236
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
6-105 7.17e-29

Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.


Pssm-ID: 433132  Cd Length: 101  Bit Score: 104.85  E-value: 7.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009    6 VICDIDGVLLHDNTAIKGANDFLARIQDAGMPLVILTNYPSQTAQDLTNRFITAGLDVPESAFYTSAMATADFLRRQD-G 84
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGFDIDEDEIITSGTAAADYLKERKfG 80
                          90       100
                  ....*....|....*....|.
gi 755398009   85 KKAYVIGEGALVHELYKAGFT 105
Cdd:pfam13344  81 KKVLVIGSEGLREELEEAGFE 101
 
Name Accession Description Interval E-value
PRK10444 PRK10444
HAD-IIA family hydrolase;
3-250 0e+00

HAD-IIA family hydrolase;


Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 520.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009   3 IKSVICDIDGVLLHDNTAIKGANDFLARIQDAGMPLVILTNYPSQTAQDLTNRFITAGLDVPESAFYTSAMATADFLRRQ 82
Cdd:PRK10444   1 IKNVICDIDGVLMHDNVAVPGAAEFLHRILDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFLRRQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009  83 DGKKAYVIGEGALVHELYKAGFTITDINPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDSHGHGFAPACGALCAP 162
Cdd:PRK10444  81 EGKKAYVIGEGALIHELYKAGFTITDINPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDTHGRGFYPACGALCAG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009 163 IEKISGRKPFYVGKPSPWIIRAALNKMQAHSESTVIVGDNLRTDILAGFQAGLETILVLSGVSTLTDIDAMPFRPSYVYP 242
Cdd:PRK10444 161 IEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILVLSGVSTLDDIDSMPFRPSWIYP 240

                 ....*...
gi 755398009 243 SVADIDII 250
Cdd:PRK10444 241 SVADIDVI 248
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
4-246 8.27e-122

UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase and Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase; Escherichia coli UmpH/NagD is a ribonucleoside tri-, di-, and monophosphatase with a preference for purines, it shows peak activity with UMP and functions in UMP-degradation. It is also an effective phosphatase with AMP, GMP and CMP. Mycobacterium tuberculosis phosphatase, Rv1692 is a glycerol 3-phosphate phosphatase. Rv1692 is the final enzyme involved in glycerophospholipid recycling/catabolism. 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: 319832 [Multi-domain]  Cd Length: 247  Bit Score: 346.50  E-value: 8.27e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009   4 KSVICDIDGVLLHDNTAIKGANDFLARIQDAGMPLVILTNYPSQTAQDLTNRFITAGLDVPESAFYTSAMATADFLRRQ- 82
Cdd:cd07530    1 KGYLIDLDGTVYRGGTAIPGAVEFIERLREKGIPFLFLTNNSTRTPEDVAAKLAEMGIDVPEEDVYTSALATAQYLAEQl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009  83 DGKKAYVIGEGALVHELYKAGFTITDINPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDSHG---HGFAPACGAL 159
Cdd:cd07530   81 PGAKVYVIGEEGLRTALHEAGLTLTDENPDYVVVGLDRDLTYEKLAEATLAIRNGAKFIATNPDLTLpteRGLLPGNGSV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009 160 CAPIEKISGRKPFYVGKPSPWIIRAALNKMQAHSESTVIVGDNLRTDILAGFQAGLETILVLSGVSTLTDIDAMPFRPSY 239
Cdd:cd07530  161 VAALEAATGVKPLFIGKPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAAGIAAGIDTLLVLTGVTTREDLAKPPYRPTY 240

                 ....*..
gi 755398009 240 VYPSVAD 246
Cdd:cd07530  241 IVPSLRE 247
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
1-249 3.70e-105

Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 304.72  E-value: 3.70e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009   1 MTIKSVICDIDGVLLHDNTAIKGANDFLARIQDAGMPLVILTNYPSQTAQDLTNRFITAGLDVPESAFYTSAMATADFLR 80
Cdd:COG0647    6 DRYDAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATAAYLA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009  81 RQ-DGKKAYVIGEGALVHELYKAGFTIT-DINPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDS---HGHGFAPA 155
Cdd:COG0647   86 ERhPGARVYVIGEEGLREELEEAGLTLVdDEEPDAVVVGLDRTFTYEKLAEALRAIRRGAPFIATNPDRtvpTEDGLIPG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009 156 CGALCAPIEKISGRKPFYVGKPSPWIIRAALNKMQAHSESTVIVGDNLRTDILAGFQAGLETILVLSGVSTLTDIDAMPF 235
Cdd:COG0647  166 AGALAAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAGLDTLLVLTGVTTAEDLEAAPI 245
                        250
                 ....*....|....
gi 755398009 236 RPSYVYPSVADIDI 249
Cdd:COG0647  246 RPDYVLDSLAELLL 259
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
5-246 1.02e-100

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: 294.27  E-value: 1.02e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009   5 SVICDIDGVLLHDNTAIKGANDFLARIQDAGMPLVILTNYPSQTAQDLTNRFITAGLDVPESAFYTSAMATADFLRRQD- 83
Cdd:cd07508    1 LVISDCDGVLWHDERAIPGAAEFLEALKEAGKKIVFVSNNSSRSRQDYAEKFRKFGVDVPEDQIVTSAKATARFLRSRKf 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009  84 GKKAYVIGEGALVHELYKAGFTI-------------------TDINPDFVIVGETRSYNWDMMHKAAYFVAN-GARFIAT 143
Cdd:cd07508   81 GKKVYVLGEEGLKEELRAAGFRIaggpskgietyaelvehleDDENVDAVIVGSDFKLNFAKLRKACRYLRNpGCLFIAT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009 144 NPDSHG----HGFAPACGALCAPIEKISGRKPFYVGKPSPWIIRAALNKMQAHSESTVIVGDNLRTDILAGFQAGLETIL 219
Cdd:cd07508  161 APDRIHplkdGGPIPGTGAFAAAVEAATGRQPLVLGKPSPWLGELALEKFGIDPERVLFVGDRLATDVLFGKACGFQTLL 240
                        250       260       270
                 ....*....|....*....|....*....|
gi 755398009 220 VLSGVSTLTDIDA---MPFRPSYVYPSVAD 246
Cdd:cd07508  241 VLTGVTTLEDLQAyidHELVPDYYADSLAD 270
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
6-223 6.70e-73

Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural subclass of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The classes 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. Class I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Class II consists of sequences in which the capping domain is found between the second and third motifs. Class III sequences have no capping domain in iether of these positions. The Class IIA capping domain is predicted by PSI-PRED to consist of a mixed alpha-beta fold with the basic pattern: Helix-Helix-Helix-Sheet-Helix-Loop-Sheet-Helix-Sheet-Helix. Presently, this subfamily encompasses a single equivalog model (TIGR01452) for the eukaryotic phosphoglycolate phosphatase, as well as four hypothetical equivalogs covering closely related sequences (TIGR01456 and TIGR01458 in eukaryotes, TIGR01457 in gram positive bacteria and TIGR01459 in gram negative bacteria). The Escherishia coli NagD gene and the Bacillus subtilus AraL gene are members of this subfamily but are not members of the any of the presently defined equivalogs within it. NagD is part of the NAG operon responsible for N-acetylglucosamine metabolism. The function of this gene is unknown. Genes from several organisms have been annotated as NagD, or NagD-like. However, without data on the presence of other members of this pathway, (such as in the case of Yersinia pestis) these assignments should not be given great weight. The AraL gene is similar: it is part of the L-arabinose operon, but the function is unknown. A gene from Halobacterium has been annotated as AraL, but no other Ara operon genes have been annotated. Many of the genes in this subfamily have been annotated as "pNPPase" "4-nitrophenyl phosphatase" or "NPPase". These all refer to the same activity versus a common lab test compound used to determine phosphatase activity. There is no evidence that this activity is physiologically relevant. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273637 [Multi-domain]  Cd Length: 236  Bit Score: 222.20  E-value: 6.70e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009    6 VICDIDGVLLHDNTAIKGANDFLARIQDAGMPLVILTNYPSQTAQDLTNRFIT-AGLDVPESAFYTSAMATADFLR-RQD 83
Cdd:TIGR01460   1 FLFDIDGVLWLGHKPIPGAAEALNRLRAKGKPVVFLTNNSSRSEEDYAEKLSSlLGVDVSPDQIITSGSVTKDLLRqRFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009   84 GKKAYVIGEGALVHELYKAGF---TITDIN-------PDFVIVGETRSYNWDMMHKAAYFVANG-ARFIATNPDS---HG 149
Cdd:TIGR01460  81 GEKVYVIGVGELRESLEGLGFrndFFDDIDhlaiekiPAAVIVGEPSDFSYDELAKAAYLLAEGdVPFIAANRDDlvrLG 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755398009  150 HG-FAPACGALCAPIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEST-VIVGDNLRTDILAGFQAGLETILVLSG 223
Cdd:TIGR01460 161 DGrFRPGAGAIAAGIKELSGREPTVVGKPSPAIYRAALNLLQARPERRdVMVGDNLRTDILGAKNAGFDTLLVLTG 236
HAD_Pase_UmpH-like cd16422
uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid ...
7-244 3.78e-55

uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid dehalogenase-like superfamily; This uncharacterized 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: 319858 [Multi-domain]  Cd Length: 247  Bit Score: 177.24  E-value: 3.78e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009   7 ICDIDGVLLHDNTAIKGANDFLARIQDAGMPLVILTNYPSQTAQDLTNRFITAGLDVPESAFYTSAMATADFLRRQDGK- 85
Cdd:cd16422    3 IFDMDGTIYLGDDLIPGTLEFLERLHEKKRRYIFLTNNSSKNLADYVEKLNRLGIDAGLDRVFTSGEATIDHLKKEFIKp 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009  86 KAYVIGEGALVHELYKAGFTITDINPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDSH---GHGFAPACGALCAP 162
Cdd:cd16422   83 KIFLLGTKSLREEFEKAGFTLDGDDIDVVVLGFDTELTYEKLRTACLLLRRGIPYIATHPDINcpsEEGPIPDAGSIIAL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009 163 IEKISGRKP-FYVGKPSPWIIRAALNKMQAHSESTVIVGDNLRTDILAGFQAGLETILVLSGVSTLTDIDAMPFRPSYVY 241
Cdd:cd16422  163 IETSTGRRPdLVIGKPNPIILDPVLEKFDYSKEETVMVGDRLYTDIVLGINAGVDSILVLSGETTREDLEDLERKPTYVF 242

                 ...
gi 755398009 242 PSV 244
Cdd:cd16422  243 DNV 245
HAD-SF-IIA-hyp2 TIGR01457
HAD-superfamily subfamily IIA hydrolase, TIGR01457; This hypothetical equivalog is a member of ...
4-246 4.10e-52

HAD-superfamily subfamily IIA hydrolase, TIGR01457; This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all gram positive (low-GC) bacteria. Sequences found in this model are annotated variously as related to NagD or 4-nitrophenyl phosphatase, and this hypothetical equivalog, of all of those within the Class IIA subfamily, is most closely related to the E. coli NagD enzyme and the PGP_euk equivalog (TIGR01452). However, there is presently no evidence that this hypothetical equivalog has the same function of either those. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 130524  Cd Length: 249  Bit Score: 169.65  E-value: 4.10e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009    4 KSVICDIDGVLLHDNTAIKGANDFLARIQDAGMPLVILTNYPSQTAQDLTNRFITAGLDVPESAFYTSAMATADFLRRQ- 82
Cdd:TIGR01457   2 KGYLIDLDGTMYNGTEKIEEACEFVRTLKKRGVPYLFVTNNSTRTPEQVADKLVSFDIPATEEQVFTTSMATAQYIAQQk 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009   83 DGKKAYVIGEGALVHELYKAGFTITDINPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDSH---GHGFAPACGAL 159
Cdd:TIGR01457  82 KDASVYVIGEEGLREAIKENGLTFGGENPDYVVVGLDRSITYEKFAVACLAIRNGARFISTNGDIAiptERGLLPGNGSL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009  160 CAPIEKISGRKPFYVGKPSPWIIRAALNKMQAHSESTVIVGDNLRTDILAGFQAGLETILVLSGVSTLTDIDAMPFRPSY 239
Cdd:TIGR01457 162 TSVLTVSTGVKPVFIGKPESIIMEQAMRVLGTDVEETLMVGDNYATDIMAGINAGIDTLLVHTGVTKREHMTDDMEKPTH 241

                  ....*..
gi 755398009  240 VYPSVAD 246
Cdd:TIGR01457 242 AIDSLAE 248
HAD_Pase_UmpH-like cd07531
UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar ...
4-247 3.96e-49

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: 161.97  E-value: 3.96e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009   4 KSVICDIDGVLLHDNTAIKGANDFLARIQDAGMPLVILTNYPSQTAQDLTNRFITAGLDVPESAFYTSAMATADFLRRQ- 82
Cdd:cd07531    1 KGYIIDLDGTIGKGVTLIPGAVEGVKTLRRLGKKIIFLSNNSTRSRRILLERLRSFGIEVGEDEILVSSYVTARFLAREk 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009  83 DGKKAYVIGEGALVHELYKAGFTITDiNPD---FVIVGETRSYNWDMMHKAAYFVANGARFIATNPDS---HGHGFAPAC 156
Cdd:cd07531   81 PNAKVFVTGEEGLIEELRLAGLEIVD-KYDeaeYVVVGSNRKITYELLTKAFRACLRGARYIATNPDRifpAEDGPIPDT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009 157 GALCAPIEKISGRKP-FYVGKPSPWIIRAALNKMQAHSESTVIVGDNLRTDILAGFQAGLETILVLSGVSTLTDIDAMPF 235
Cdd:cd07531  160 AAIIGAIEWCTGREPeVVVGKPSEVMAREALDILGLDAKDCAIVGDQIDVDIAMGKAIGMETALVLTGVTTRENLDRHGY 239
                        250
                 ....*....|..
gi 755398009 236 RPSYVYPSVADI 247
Cdd:cd07531  240 KPDYVLNSIKDL 251
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
2-247 1.90e-48

UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium falciparum PNPase; Plasmodium falciparum para nitrophenyl phosphate phosphatase (PNPase) catalyzes the dephosphorylation of thiamine monophosphate to thiamine, other substrates on which its active are nucleotides, phosphorylated sugars, pyridoxal-5-phosphate, and paranitrophenyl phosphate. 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: 319834 [Multi-domain]  Cd Length: 286  Bit Score: 161.32  E-value: 1.90e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009   2 TIKSVICDIDGVLLHDNTAIKGANDFLARIQDAGMPLVILTNYPSQTAQDLTNRFITAGLDVPESAFYTSAMATADFL-R 80
Cdd:cd07532    5 NIDTVIFDADGVLWTGDKPIPGAVEVFNALLDKGKKVFIVTNNSTKTREELAKKAKKLGFNVKENNILSSAAVIADYLkE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009  81 RQDGKKAYVIGEGALVHELYKAGF---------------------TITDINPDFVIVGETRSYNWDMMHKAAYFVAN-GA 138
Cdd:cd07532   85 KGFKKKVYVIGEEGIRKELEEAGIvscggdgedekddsmgdfahnLELDPDVGAVVVGRDEHFSYPKLMKACNYLRNpDV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009 139 RFIATNPDShghgFAPAC--------GALCAPIEKISGRKPFYVGKPSPWIIRAALNKMQAHSESTVIVGDNLRTDILAG 210
Cdd:cd07532  165 LFLATNMDA----TFPGPvgrvipgaGAMVAAIEAVSGRKPLVLGKPNPQILNFLMKSGVIKPERTLMIGDRLKTDILFA 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 755398009 211 FQAGLETILVLSGVSTLTDI---------DAMPFRPSYVYPSVADI 247
Cdd:cd07532  241 NNCGFQSLLVGTGVNSLEDAekikkegdpKKKDLVPDTYLPSLGHL 286
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
9-247 2.47e-44

UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase; This subfamily includes the phosphoglycolate phosphatases (human PGP and Arabidopsis thaliana PGLP2) and p-nitrophenylphosphatases (Schizosaccharomyces pombe PHO2 and Saccharomyces PHO13p). It 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: 319813 [Multi-domain]  Cd Length: 282  Bit Score: 150.62  E-value: 2.47e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009   9 DIDGVLLHDNTAIKGANDFLARIQDAGMPLVILTNYPSQTAQDLTNRFITAGLDVPES-AFYTSAMATADFLRRQD---- 83
Cdd:cd07510    7 DCDGVLWNGEKAIPGAPETLNLLRSLGKRLVFVTNNSTKSREAYAKKFARLGFTGLKEeEIFSSAYCAARYLRQRLpgpa 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009  84 GKKAYVIGEGALVHELYKAGFTITDINPDF--------------------VIVGETRSYNWDMMHKAAYFVAN-GARFIA 142
Cdd:cd07510   87 DGKVYVLGGEGLRAELEAAGVAHLGGPDDGlrraapkdwllagldpdvgaVLVGLDEHVNYLKLAKATQYLRDpGCLFVA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009 143 TNPDSHGH----GFAPACGALCAPIEKISGRKPFYVGKPSPWIIRAALNKMQAHSESTVIVGDNLRTDILAGFQAGLETI 218
Cdd:cd07510  167 TNRDPWHPlsdgSFIPGTGSLVAALETASGRQAIVVGKPSRFMFDCISSKFSIDPARTCMVGDRLDTDILFGQNCGLKTL 246
                        250       260       270
                 ....*....|....*....|....*....|..
gi 755398009 219 LVLSGVSTLTDIDAM---PFRPSYVYPSVADI 247
Cdd:cd07510  247 LVLTGVSTLEEALAKlsnDLVPDYYVESLADL 278
PLN02645 PLN02645
phosphoglycolate phosphatase
3-247 6.10e-40

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 139.85  E-value: 6.10e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009   3 IKSV---ICDIDGVLLHDNTAIKGANDFLARIQDAGMPLVILTNYPSQTAQDLTNRFITAGLDVPESAFYTSAMATADFL 79
Cdd:PLN02645  25 IDSVetfIFDCDGVIWKGDKLIEGVPETLDMLRSMGKKLVFVTNNSTKSRAQYGKKFESLGLNVTEEEIFSSSFAAAAYL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009  80 RRQD---GKKAYVIGEGALVHELYKAGFTI----------TDINPDF----------VIVGETRSYNWDMMHKAAYFVAN 136
Cdd:PLN02645 105 KSINfpkDKKVYVIGEEGILEELELAGFQYlggpedgdkkIELKPGFlmehdkdvgaVVVGFDRYINYYKIQYATLCIRE 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009 137 --GARFIATNPDSHGHGFA----PACGALCAPIEKISGRKPFYVGKPSPWIIRAALNKMQAHSESTVIVGDNLRTDILAG 210
Cdd:PLN02645 185 npGCLFIATNRDAVTHLTDaqewAGAGSMVGAIKGSTEREPLVVGKPSTFMMDYLANKFGIEKSQICMVGDRLDTDILFG 264
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 755398009 211 FQAGLETILVLSGVSTLTDIDAM--PFRPSYVYPSVADI 247
Cdd:PLN02645 265 QNGGCKTLLVLSGVTSESMLLSPenKIQPDFYTSKISDF 303
PGP_euk TIGR01452
phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the ...
2-247 9.19e-40

phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the glycolate salvage pathway in higher organisms (photorespiration in plants). Phosphoglycolate results from the oxidase activity of RubisCO in the Calvin cycle when concentrations of carbon dioxide are low relative to oxygen. In mammals, PGP is found in many tissues, notably in red blood cells where P-glycolate is and important activator of the hydrolysis of 2,3-bisphosphoglycerate, a major modifier of the oxygen affinity of hemoglobin. Pyridoxal phosphate (PLP, Vitamin B6) phosphatase is involved in the degradation of PLP in mammals and is widely distributed in human tissues including erythrocyes. The enzymes described here are members of the Haloacid dehalogenase superfamily of hydrolase enzymes (pfam00702). Unlike the bacterial PGP equivalog (TIGR01449), which is a member of class (subfamily) I, these enzymes are members of class (subfamily) II. These two families have almost certainly arisen from convergent evolution (although these two ancestors may themselves have diverged from a more distant HAD superfamily progenitor). The primary seed sequence for this model comes from Chlamydomonas reinhardtii, a photosynthetic alga. The enzyme has been purified and characterized and these data are fully consistent with the assignment of function as a PGPase involved in photorespiration. The second seed, from Homo sapiens chromosome 22 has been characterized as a pyridoxal phosphatase. Biochemical characterization of partially purified PGP's from various tissues including red blood cells have been performed while one gene for PGP has been localized to chromosome 16p13.3. The sequence used here maps to chromosome 22. There is indeed a related gene on chromosome 16 (and it is expressed, since EST's are found) which shows 46% identity. The chromosome 16 gene is not in evidence in nraa but translated from the genomic sequence. The third seed, from C. elegans, is only supported by sequence similarity. This model is limited to eukaryotic species including S. pombe and S. cerevisiae, although several archaea score between the trusted and noise cutoffs. This model is closely related to a family of bacterial sequences including the E. coli NagD and B. subtilus AraL genes which are characterized by the ability to hydrolyze para-nitrophenylphosphate (pNPPases or NPPases). The chlamydomonas PGPase d


Pssm-ID: 273635 [Multi-domain]  Cd Length: 279  Bit Score: 138.46  E-value: 9.19e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009    2 TIKSVICDIDGVLLHDNTAIKGANDFLARIQDAGMPLVILTNYPSQTAQDLTNRFITAGLDVPESAFYTSAMATADFLRR 81
Cdd:TIGR01452   1 TAQGFIFDCDGVLWLGERVVPGAPELLDRLARAGKQILFVTNNSTKSRAEYALKFARLGFNGLAEQLFSSALCAARLLRQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009   82 Q--DGKKAYVIGEGALVHELYKAG--------------------FTITDINPDFVIVGETRSYNWDMMHKA-AYFVANGA 138
Cdd:TIGR01452  81 PpdAGKAVYVIGEEGLRAELDAAGirlagdpgekkqdeadgfmyDIKLDERVGAVVVGYDEHFSYVKLMEAcAHLREPGC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009  139 RFIATNPDSHGHG----FAPACGALCAPIEKISGRKPFYVGKPSPWIIRAALNKMQAHSESTVIVGDNLRTDILAGFQAG 214
Cdd:TIGR01452 161 LFVATNRDPWHPLsdgsRTPGTGSLVAAIETASGRQPLVVGKPSPYMFNCITEKFSIDPARTLMVGDRLETDILFGHRCG 240
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 755398009  215 LETILVLSGVSTLTDIDAM------PFRPSYVYPSVADI 247
Cdd:TIGR01452 241 MTTVLVLSGVSQLEEAQEYlmagqdDLVPDYVVESLADL 279
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
4-250 2.14e-32

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: 118.54  E-value: 2.14e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009   4 KSVICDIDGVLLHDNTAIKGANDFLARIQDAGMPLVILTNYPSQTAQDLTNRFITAGLDVPESAFYTSAMATADFLRRQD 83
Cdd:cd07509    1 KAVLLDLSGTLYISGAAIPGAAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQRLGFDVSEEEIFTSLTAARQYLEEKG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009  84 GKKAYVIGEGALvhELYKAgftITDINPDFVIVGET-RSYNWDMMHKAAYFVANGARFIATN-------PDshghGFAPA 155
Cdd:cd07509   81 LRPHLLVDDDAL--EDFIG---IDTSDPNAVVIGDAgEHFNYQTLNRAFRLLLDGAPLIALHkgryykrKD----GLALD 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009 156 CGALCAPIEKISGRKPFYVGKPSPWIIRAALNKMQAHSESTVIVGDNLRTDILAGFQAGLETILVLSG---VSTLTDIDa 232
Cdd:cd07509  152 PGAFVTGLEYATGIKATVVGKPSPEFFLSALRSLGVDPEEAVMIGDDLRDDVGGAQACGMRGILVRTGkyrPSDEKKPN- 230
                        250
                 ....*....|....*...
gi 755398009 233 mPFRPSYVYPSVADIDII 250
Cdd:cd07509  231 -VPPDLTADSFADAVDHI 247
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
6-105 7.17e-29

Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.


Pssm-ID: 433132  Cd Length: 101  Bit Score: 104.85  E-value: 7.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009    6 VICDIDGVLLHDNTAIKGANDFLARIQDAGMPLVILTNYPSQTAQDLTNRFITAGLDVPESAFYTSAMATADFLRRQD-G 84
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGFDIDEDEIITSGTAAADYLKERKfG 80
                          90       100
                  ....*....|....*....|.
gi 755398009   85 KKAYVIGEGALVHELYKAGFT 105
Cdd:pfam13344  81 KKVLVIGSEGLREELEEAGFE 101
Hydrolase_like pfam13242
HAD-hyrolase-like;
175-246 3.08e-24

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 92.29  E-value: 3.08e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755398009  175 GKPSPWIIRAALNKMQAHSESTVIVGDNLRTDILAGFQAGLETILVLSGVSTLTDIDAMPFRPSYVYPSVAD 246
Cdd:pfam13242   3 GKPNPGMLERALARLGLDPERTVMIGDRLDTDILGAREAGARTILVLTGVTRPADLEKAPIRPDYVVDDLAE 74
HAD_like cd07525
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
4-232 3.16e-14

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; 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: 319827 [Multi-domain]  Cd Length: 253  Bit Score: 70.05  E-value: 3.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009   4 KSVICDIDGVLLHDNTAIKGANDFLARIQDAGMPLVILTNYPSQTAQdlTNRFItAGLDVPES---AFYTSAMATADFLR 80
Cdd:cd07525    1 DAFLLDLWGVLHDGNEPYPGAVEALAALRAAGKTVVLVTNAPRPAES--VVRQL-AKLGVPPStydAIITSGEVTRELLA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009  81 RQD--GKKAYVIG--------EG---ALVHELYKAGFTITDINPDFvivgETRS---YNwDMMHKAAyfvANGARFIATN 144
Cdd:cd07525   78 REAglGRKVYHLGperdanvlEGldvVATDDAEKAEFILCTGLYDD----ETETpedYR-KLLKAAA---ARGLPLICAN 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009 145 PD---SHGHGFAPACGALCAPIEKISGRKPFYvGKPSPWIIRAALNKMQAHSESTVI-VGDNLRTDILAGFQAGLETILV 220
Cdd:cd07525  150 PDlvvPRGGKLIYCAGALAELYEELGGEVIYF-GKPHPPIYDLALARLGRPAKARILaVGDGLHTDILGANAAGLDSLFV 228
                        250
                 ....*....|..
gi 755398009 221 LSGVSTLTDIDA 232
Cdd:cd07525  229 TGGIHRRLAAEA 240
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
175-220 2.14e-13

Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the uncharacterized protein Bacillus subtilis YqeG; 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: 319853 [Multi-domain]  Cd Length: 108  Bit Score: 64.60  E-value: 2.14e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 755398009 175 GKPSPWIIRAALNKMQAHSESTVIVGDNLRTDILAGFQAGLETILV 220
Cdd:cd16416   63 GKPRPRAFRRALKEMDLPPEQVAMVGDQLFTDILGGNRAGLYTILV 108
HAD-SF-IIA-hyp4 TIGR01459
HAD-superfamily class IIA hydrolase, TIGR01459; This hypothetical equivalog is a member of the ...
9-222 1.22e-11

HAD-superfamily class IIA hydrolase, TIGR01459; This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all gram negative and primarily alpha proteobacteria. Only one sequence hase been annotated as other than "hypothetical." That one, from Brucella, is annotated as related to NagD, but only by sequence similarity and should be treated with some skepticism. (See comments for Class IIA subfamily model)


Pssm-ID: 130526 [Multi-domain]  Cd Length: 242  Bit Score: 62.60  E-value: 1.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009    9 DIDGVLLHDNTAIKGANDFLARIQDAGMPLVILTNYPSQTAQ------------DLTNRFITAGlDVPESAFYTSAmATA 76
Cdd:TIGR01459  14 DLWGVIIDGNHTYPGAVQNLNKIIAQGKPVYFVSNSPRNIFSlhktlkslginaDLPEMIISSG-EIAVQMILESK-KRF 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009   77 DFlrRQDGKkaYVIGEG----ALVHELYKAgFTITDINPDFVIVGETRSYNWDMMHKAAYFVANGAR---FIATNPDS-- 147
Cdd:TIGR01459  92 DI--RNGII--YLLGHLendiINLMQCYTT-DDENKANASLITIYRSENEKLDLDEFDELFAPIVARkipNICANPDRgi 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755398009  148 HGHGFAPACGALCAPIEKISGRKPFYVGKPSPWIIRAALNKMQA-HSESTVIVGDNLRTDILAGFQAGLETILVLS 222
Cdd:TIGR01459 167 NQHGIYRYGAGYYAELIKQLGGKVIYSGKPYPAIFHKALKECSNiPKNRMLMVGDSFYTDILGANRLGIDTALVLT 242
YqeG COG2179
Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];
175-237 1.34e-11

Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];


Pssm-ID: 441782  Cd Length: 164  Bit Score: 60.91  E-value: 1.34e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755398009 175 GKPSPWIIRAALNKMQAHSESTVIVGDNLRTDILAGFQAGLETILVLSgvstLTDIDAMPFRP 237
Cdd:COG2179   90 KKPLPRGFRKALKLMGLPPEETAVVGDQLFTDVLGGNRAGLYTILVKP----LVDKEFWFTRI 148
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
3-214 4.99e-11

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: 59.91  E-value: 4.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009    3 IKSVICDIDGVLLHDNTAIKGANDFLARIQDAGMPLVILTNYPSQTAQDLTNRFItagldvpesafytsaMATADFLRRQ 82
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPLAKAIVAAAEDLPIPVEDFTARLL---------------LGKRDWLEEL 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009   83 DGKKAyvigegaLVHELYKAGFTITDINPDFVIVGETRSYNWDMMHKA-AYFVANGAR-FIATNPDSHG-HGFAPACGAL 159
Cdd:pfam00702  66 DILRG-------LVETLEAEGLTVVLVELLGVIALADELKLYPGAAEAlKALKERGIKvAILTGDNPEAaEALLRLLGLD 138
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755398009  160 CAPIEKISGRkPFYVGKPSPWIIRAALNKMQAHSESTVIVGDNLrTDILAGFQAG 214
Cdd:pfam00702 139 DYFDVVISGD-DVGVGKPKPEIYLAALERLGVKPEEVLMVGDGV-NDIPAAKAAG 191
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
3-247 6.61e-11

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 59.94  E-value: 6.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009   3 IKSVICDIDGVLLHDNTAIKGA-NDFLARIQDAGMPLVILTNYPSQTAQDLtnrfITAGLDVPESAFYTSAMAT-ADFLR 80
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAAAlNEALAELGLPPLDLEELRALIGLGLREL----LRRLLGEDPDEELEELLARfRELYE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009  81 RQDGKKAYVIgEGA--LVHELYKAGFTItdinpdfvivgetrsynwdmmhkaayfvangarFIATNPDSHG-------HG 151
Cdd:COG0546   77 EELLDETRLF-PGVreLLEALKARGIKL---------------------------------AVVTNKPREFaerlleaLG 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009 152 FAPacgalcaPIEKISGRKPFYVGKPSPWIIRAALNKMQAHSESTVIVGDNLRtDILAGFQAGLETILVLSGVSTLTDID 231
Cdd:COG0546  123 LDD-------YFDAIVGGDDVPPAKPKPEPLLEALERLGLDPEEVLMVGDSPH-DIEAARAAGVPFIGVTWGYGSAEELE 194
                        250
                 ....*....|....*.
gi 755398009 232 AmpFRPSYVYPSVADI 247
Cdd:COG0546  195 A--AGADYVIDSLAEL 208
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
174-218 2.87e-08

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: 50.62  E-value: 2.87e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 755398009 174 VGKPSPWIIRAALNKMQAHSESTVIVGDNLRTDILAGFQAGLETI 218
Cdd:cd04305   62 VQKPNPEIFDYALNQLGVKPEETLMVGDSLESDILGAKNAGIKTV 106
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
163-220 2.83e-07

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 49.12  E-value: 2.83e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 755398009  163 IEKISGRKPFYVGKPSPWIIRAALNKMQAHSESTVIVGDNLRtDILAGFQAGLETILV 220
Cdd:pfam13419 122 FDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVIYVGDSPR-DIEAAKNAGIKVIAV 178
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
3-220 2.23e-06

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: 47.33  E-value: 2.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009   3 IKSVICDIDGVLLHDNTAIKGAND-FLARIQDAGMPLVILTNYpSQTAQDLTNRFITAGLDVPEsafytsamATADFLRR 81
Cdd:COG1011    1 IKAVLFDLDGTLLDFDPVIAEALRaLAERLGLLDEAEELAEAY-RAIEYALWRRYERGEITFAE--------LLRRLLEE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755398009  82 QDgkkayVIGEGALVHELYKAGFTITDINPDFVivgetrsynwDMMHKAAyfvANGAR-FIATN-PDSHGHGFAPACGaL 159
Cdd:COG1011   72 LG-----LDLAEELAEAFLAALPELVEPYPDAL----------ELLEALK---ARGYRlALLTNgSAELQEAKLRRLG-L 132
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755398009 160 CAPIEKI--SGRKPFYvgKPSPWIIRAALNKMQAHSESTVIVGDNLRTDILAGFQAGLETILV 220
Cdd:COG1011  133 DDLFDAVvsSEEVGVR--KPDPEIFELALERLGVPPEEALFVGDSPETDVAGARAAGMRTVWV 193
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
176-247 3.98e-06

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: 45.86  E-value: 3.98e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755398009 176 KPSPWIIRAALNKMQAHSESTVIVGDNLRtDILAGFQAGLETILVLSGVSTLTDIDAmpfRPSYVYPSVADI 247
Cdd:COG0241  102 KPKPGMLLQAAERLGIDLSNSYMIGDRLS-DLQAAKAAGCKGILVLTGKGAEELAEA---LPDTVADDLAEA 169
YqeG_hyp_ppase TIGR01668
HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins ...
171-225 7.76e-06

HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins is a member of the IIIA subfamily of the haloacid dehalogenase (HAD) superfamily of hydrolases. All characterized members of this subfamily (TIGR01662) and most characterized members of the HAD superfamily are phosphatases. HAD superfamily phosphatases contain active site residues in several conserved catalytic motifs, all of which are found conserved here. This family consists of sequences from fungi, plants, cyanobacteria, gram-positive bacteria and Deinococcus. There is presently no characterization of any sequence in this family.


Pssm-ID: 273744  Cd Length: 170  Bit Score: 45.09  E-value: 7.76e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755398009  171 PFYVG--KPSPWIIRAALNKMQAHSESTVIVGDNLRTDILAGFQAGLETILVLSGVS 225
Cdd:TIGR01668  84 PVLPHavKPPGCAFRRAHPEMGLTSEQVAVVGDRLFTDVMGGNRNGSYTILVEPLVH 140
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
176-247 1.15e-05

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 45.02  E-value: 1.15e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755398009 176 KPSPWIIRAALNKMQAHSESTVIVGDNLRtDILAGFQAGLETILV---LSGVSTLTDidampFRPSYVYPSVADI 247
Cdd:PRK13288 138 KPDPEPVLKALELLGAKPEEALMVGDNHH-DILAGKNAGTKTAGVawtIKGREYLEQ-----YKPDFMLDKMSDL 206
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
176-247 1.65e-05

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: 44.58  E-value: 1.65e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755398009 176 KPSPWIIRAALNKMQAHSESTVIVGDNLRtDILAGFQAGLETILVLSGVSTLTDIDAmpFRPSYVYPSVADI 247
Cdd:cd02616  136 KPDPEPVLKALELLGAEPEEALMVGDSPH-DILAGKNAGVKTVGVTWGYKGREYLKA--FNPDFIIDKMSDL 204
PRK09449 PRK09449
dUMP phosphatase; Provisional
174-217 1.02e-04

dUMP phosphatase; Provisional


Pssm-ID: 181865 [Multi-domain]  Cd Length: 224  Bit Score: 42.20  E-value: 1.02e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 755398009 174 VGKPSPWIIRAALNKMQAHSESTVI-VGDNLRTDILAGFQAGLET 217
Cdd:PRK09449 148 VAKPDVAIFDYALEQMGNPDRSRVLmVGDNLHSDILGGINAGIDT 192
HAD_like cd07511
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
9-67 2.21e-04

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to the uncharacterized human CECR5 (cat eye syndrome critical region protein 5); 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: 319814  Cd Length: 136  Bit Score: 40.06  E-value: 2.21e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755398009   9 DIDGVLLHDNTAIKGANDFLARIQDAGMPLVILTNYPSQTAQDLTNrFITAGLDVPESA 67
Cdd:cd07511    6 DIDGVLVRGKKPIPGAPKALKFLNDNKIPFIFLTNGGGFPESKRAD-FLSKLLGVEVSP 63
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
175-247 2.66e-04

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 40.96  E-value: 2.66e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755398009 175 GKPSPWIIRAALNKMQAHSESTVIVGDNLrTDILAGFQAGLETIlvlsGVSTLTDIDAMPFRPSYVYPSVADI 247
Cdd:COG0637  141 GKPDPDIYLLAAERLGVDPEECVVFEDSP-AGIRAAKAAGMRVV----GVPDGGTAEEELAGADLVVDDLAEL 208
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
176-219 1.69e-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: 38.13  E-value: 1.69e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 755398009 176 KPSPWIIRAALNKMQAHSESTVIVGDnlRT-DILAGFQAGLETIL 219
Cdd:cd07523  130 KPNPEAINYLLNKYQLNPEETVMIGD--RElDIEAGHNAGISTIL 172
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
176-220 3.10e-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: 3.10e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 755398009 176 KPSPWIIRAALNKMQAHSESTVIVGDNLRTDILAGFQAGLETILV 220
Cdd:cd16415   62 KPDPRIFQKALERLGVSPEEALHVGDDLKNDYLGARAVGWHALLV 106
 
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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