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Conserved domains on  [gi|530414001|ref|XP_005258428|]
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haloacid dehalogenase-like hydrolase domain-containing protein 2 isoform X2 [Homo sapiens]

Protein Classification

HAD-IIA family hydrolase( domain architecture ID 11576289)

HAD (haloacid dehalogenase)-IIA family hydrolase such as vertebrate haloacid dehalogenase-like hydrolase domain-containing protein 2 and phospholysine phosphohistidine inorganic pyrophosphate phosphatase, which hydrolyzes imidodiphosphate, 3-phosphohistidine and 6-phospholysine, as well as inorganic diphosphate with lower efficiency

CATH:  3.30.1240.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  16889794|15337123|33940035|37786806

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 8-225 2.87e-140

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: 392.80  E-value: 2.87e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001   8 KAVLVDLSGTLHIEDAAVPGAQEALKRLRGASVIIRFVTNTTKESKQDLLERLRKLEFDISEDEIFTSLTAARSLLERKQ 87
Cdd:cd07509    1 KAVLLDLSGTLYISGAAIPGAAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQRLGFDVSEEEIFTSLTAARQYLEEKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001  88 VRPMLLVDDRALPDFKGIQTSDPNAVVMGLAPEHFHYQILNQAFRLLLDGAPLIAIHKARYYKRKDGLALGPGPFVTALE 167
Cdd:cd07509   81 LRPHLLVDDDALEDFIGIDTSDPNAVVIGDAGEHFNYQTLNRAFRLLLDGAPLIALHKGRYYKRKDGLALDPGAFVTGLE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530414001 168 YATDTKATVVGKPEKTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQDVGMLGILVKT 225
Cdd:cd07509  161 YATGIKATVVGKPSPEFFLSALRSLGVDPEEAVMIGDDLRDDVGGAQACGMRGILVRT 218
 
Name Accession Description Interval E-value
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 8-225 2.87e-140

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: 392.80  E-value: 2.87e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001   8 KAVLVDLSGTLHIEDAAVPGAQEALKRLRGASVIIRFVTNTTKESKQDLLERLRKLEFDISEDEIFTSLTAARSLLERKQ 87
Cdd:cd07509    1 KAVLLDLSGTLYISGAAIPGAAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQRLGFDVSEEEIFTSLTAARQYLEEKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001  88 VRPMLLVDDRALPDFKGIQTSDPNAVVMGLAPEHFHYQILNQAFRLLLDGAPLIAIHKARYYKRKDGLALGPGPFVTALE 167
Cdd:cd07509   81 LRPHLLVDDDALEDFIGIDTSDPNAVVIGDAGEHFNYQTLNRAFRLLLDGAPLIALHKGRYYKRKDGLALDPGAFVTGLE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530414001 168 YATDTKATVVGKPEKTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQDVGMLGILVKT 225
Cdd:cd07509  161 YATGIKATVVGKPSPEFFLSALRSLGVDPEEAVMIGDDLRDDVGGAQACGMRGILVRT 218
HAD-SF-IIA-hyp3 TIGR01458
HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of ...
 7-225 1.30e-132

HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of the IIA subfamily (TIGR01460) of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. One sequence (GP|10716807) has been annotated as a "phospholysine phosphohistidine inorganic pyrophosphatase," probably in reference to studies on similarly described (but unsequenced) enzymes from bovine and rat tissues. However, the supporting information for this annotation has never been published. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 162372 [Multi-domain]  Cd Length: 257  Bit Score: 373.81  E-value: 1.30e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001    7 LKAVLVDLSGTLHIEDA----AVPGAQEALKRLRGASVIIRFVTNTTKESKQDLLERLRKLEFDISEDEIFTSLTAARSL 82
Cdd:TIGR01458   1 VKGVLLDISGVLYISDAgggtAVPGSQEAVKRLRGASVKVRFVTNTTKESKQDLLERLQRLGFDISEDEVFTPAPAARQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001   83 LERKQVRPMLLVDDRALPDFKGIQTSDPNAVVMGLAPEHFHYQILNQAFRLLLDGAP--LIAIHKARYYKRKDGLALGPG 160
Cdd:TIGR01458  81 LEEKQLRPMLLVDDRVLPDFDGIDTSDPNCVVMGLAPEHFSYQILNQAFRLLLDGAKpvLIAIGKGRYYKRKDGLALDVG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530414001  161 PFVTALEYATDTKATVVGKPEKTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQDVGMLGILVKT 225
Cdd:TIGR01458 161 PFVTALEYATDTKATVVGKPSKTFFLEALRATGCEPEEAVMIGDDCRDDVGGAQDCGMRGIQVRT 225
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
8-225 4.28e-70

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 215.36  E-value: 4.28e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001   8 KAVLVDLSGTLHIEDAAVPGAQEALKRLRGASVIIRFVTNTTKESKQDLLERLRKLEFDISEDEIFTSLTAARSLLERKQ 87
Cdd:COG0647    9 DAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATAAYLAERH 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001  88 V--RPMLLVDDRALPDFKGI-----QTSDPNAVVMGLAPEhFHYQILNQAFRLLLDGAPLIAIHKARYYKRKDGLALGPG 160
Cdd:COG0647   89 PgaRVYVIGEEGLREELEEAgltlvDDEEPDAVVVGLDRT-FTYEKLAEALRAIRRGAPFIATNPDRTVPTEDGLIPGAG 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530414001 161 PFVTALEYATDTKATVVGKPEKTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQDVGMLGILVKT 225
Cdd:COG0647  168 ALAAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAGLDTLLVLT 232
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 10-86 1.24e-20

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 83.28  E-value: 1.24e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530414001   10 VLVDLSGTLHIEDAAVPGAQEALKRLRGASVIIRFVTNTTKESKQDLLERLRKLEFDISEDEIFTSLTAARSLLERK 86
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGFDIDEDEIITSGTAAADYLKER 77
PRK10444 PRK10444
HAD-IIA family hydrolase;
7-223 7.77e-15

HAD-IIA family hydrolase;


Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 71.36  E-value: 7.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001   7 LKAVLVDLSGTLHIEDAAVPGAQEALKRLRGASVIIRFVTNTTKESKQDLLERLRKLEFDISEDEIFTSLTAARSLLERK 86
Cdd:PRK10444   1 IKNVICDIDGVLMHDNVAVPGAAEFLHRILDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFLRRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001  87 QVRPMLLVDDRALPD--FKG---IQTSDPNAVVMGlAPEHFHYQILNQAFRLLLDGAPLIAIHKARYykrkdGLALGP-- 159
Cdd:PRK10444  81 EGKKAYVIGEGALIHelYKAgftITDINPDFVIVG-ETRSYNWDMMHKAAYFVANGARFIATNPDTH-----GRGFYPac 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530414001 160 GPFVTALEYATDTKATVVGKPEKTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQDVGMLGILV 223
Cdd:PRK10444 155 GALCAGIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILV 218
 
Name Accession Description Interval E-value
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 8-225 2.87e-140

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: 392.80  E-value: 2.87e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001   8 KAVLVDLSGTLHIEDAAVPGAQEALKRLRGASVIIRFVTNTTKESKQDLLERLRKLEFDISEDEIFTSLTAARSLLERKQ 87
Cdd:cd07509    1 KAVLLDLSGTLYISGAAIPGAAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQRLGFDVSEEEIFTSLTAARQYLEEKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001  88 VRPMLLVDDRALPDFKGIQTSDPNAVVMGLAPEHFHYQILNQAFRLLLDGAPLIAIHKARYYKRKDGLALGPGPFVTALE 167
Cdd:cd07509   81 LRPHLLVDDDALEDFIGIDTSDPNAVVIGDAGEHFNYQTLNRAFRLLLDGAPLIALHKGRYYKRKDGLALDPGAFVTGLE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530414001 168 YATDTKATVVGKPEKTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQDVGMLGILVKT 225
Cdd:cd07509  161 YATGIKATVVGKPSPEFFLSALRSLGVDPEEAVMIGDDLRDDVGGAQACGMRGILVRT 218
HAD-SF-IIA-hyp3 TIGR01458
HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of ...
 7-225 1.30e-132

HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of the IIA subfamily (TIGR01460) of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. One sequence (GP|10716807) has been annotated as a "phospholysine phosphohistidine inorganic pyrophosphatase," probably in reference to studies on similarly described (but unsequenced) enzymes from bovine and rat tissues. However, the supporting information for this annotation has never been published. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 162372 [Multi-domain]  Cd Length: 257  Bit Score: 373.81  E-value: 1.30e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001    7 LKAVLVDLSGTLHIEDA----AVPGAQEALKRLRGASVIIRFVTNTTKESKQDLLERLRKLEFDISEDEIFTSLTAARSL 82
Cdd:TIGR01458   1 VKGVLLDISGVLYISDAgggtAVPGSQEAVKRLRGASVKVRFVTNTTKESKQDLLERLQRLGFDISEDEVFTPAPAARQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001   83 LERKQVRPMLLVDDRALPDFKGIQTSDPNAVVMGLAPEHFHYQILNQAFRLLLDGAP--LIAIHKARYYKRKDGLALGPG 160
Cdd:TIGR01458  81 LEEKQLRPMLLVDDRVLPDFDGIDTSDPNCVVMGLAPEHFSYQILNQAFRLLLDGAKpvLIAIGKGRYYKRKDGLALDVG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530414001  161 PFVTALEYATDTKATVVGKPEKTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQDVGMLGILVKT 225
Cdd:TIGR01458 161 PFVTALEYATDTKATVVGKPSKTFFLEALRATGCEPEEAVMIGDDCRDDVGGAQDCGMRGIQVRT 225
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
8-225 4.28e-70

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 215.36  E-value: 4.28e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001   8 KAVLVDLSGTLHIEDAAVPGAQEALKRLRGASVIIRFVTNTTKESKQDLLERLRKLEFDISEDEIFTSLTAARSLLERKQ 87
Cdd:COG0647    9 DAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATAAYLAERH 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001  88 V--RPMLLVDDRALPDFKGI-----QTSDPNAVVMGLAPEhFHYQILNQAFRLLLDGAPLIAIHKARYYKRKDGLALGPG 160
Cdd:COG0647   89 PgaRVYVIGEEGLREELEEAgltlvDDEEPDAVVVGLDRT-FTYEKLAEALRAIRRGAPFIATNPDRTVPTEDGLIPGAG 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530414001 161 PFVTALEYATDTKATVVGKPEKTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQDVGMLGILVKT 225
Cdd:COG0647  168 ALAAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAGLDTLLVLT 232
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 8-225 4.98e-36

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: 127.32  E-value: 4.98e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001   8 KAVLVDLSGTLHIEDAAVPGAQEALKRLRGASVIIRFVTNTTKESKQDLLERLRKLEFDISEDEIFTS-LTAARSLLERK 86
Cdd:cd07530    1 KGYLIDLDGTVYRGGTAIPGAVEFIERLREKGIPFLFLTNNSTRTPEDVAAKLAEMGIDVPEEDVYTSaLATAQYLAEQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001  87 QVRPMLLVDDRALPD------FKGIQTsDPNAVVMGLAPeHFHYQILNQAFRLLLDGAPLIAIHKARYYKRKDGLALGPG 160
Cdd:cd07530   81 PGAKVYVIGEEGLRTalheagLTLTDE-NPDYVVVGLDR-DLTYEKLAEATLAIRNGAKFIATNPDLTLPTERGLLPGNG 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530414001 161 PFVTALEYATDTKATVVGKPEKTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQDVGMLGILVKT 225
Cdd:cd07530  159 SVVAALEAATGVKPLFIGKPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAAGIAAGIDTLLVLT 223
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 10-225 1.11e-30

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: 113.19  E-value: 1.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001   10 VLVDLSGTLHIEDAAVPGAQEALKRLRGASVIIRFVTNTTKESKQDLLERLRKLEF-DISEDEIFTSLTAARSLLERKQV 88
Cdd:TIGR01460   1 FLFDIDGVLWLGHKPIPGAAEALNRLRAKGKPVVFLTNNSSRSEEDYAEKLSSLLGvDVSPDQIITSGSVTKDLLRQRFE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001   89 R-PMLLV--------------DDRALPDFKGIQTSDPNAVVMGLAPEHFHYQILNQAFRLLLDG-APLIAIHKARYYKRK 152
Cdd:TIGR01460  81 GeKVYVIgvgelresleglgfRNDFFDDIDHLAIEKIPAAVIVGEPSDFSYDELAKAAYLLAEGdVPFIAANRDDLVRLG 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530414001  153 DG-LALGPGPFVTALEYATDTKATVVGKPEKTFFLEALRGTGCEPEE-AVMIGDDCRDDVGGAQDVGMLGILVKT 225
Cdd:TIGR01460 161 DGrFRPGAGAIAAGIKELSGREPTVVGKPSPAIYRAALNLLQARPERrDVMVGDNLRTDILGAKNAGFDTLLVLT 235
HAD_Pase_UmpH-like cd07531
UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar ...
 8-225 4.92e-29

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: 109.58  E-value: 4.92e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001   8 KAVLVDLSGTLHIEDAAVPGAQEALKRLRGASVIIRFVTNTTKESKQDLLERLRKLEFDISEDEIFTSLTA-ARSLLERK 86
Cdd:cd07531    1 KGYIIDLDGTIGKGVTLIPGAVEGVKTLRRLGKKIIFLSNNSTRSRRILLERLRSFGIEVGEDEILVSSYVtARFLAREK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001  87 QVRPMLLVDDRALPD---FKGIQTSDP---NAVVMGLAPEHFHYQILNQAFRLLLDGAPLIAIHKARYYKRKDGLALGPG 160
Cdd:cd07531   81 PNAKVFVTGEEGLIEelrLAGLEIVDKydeAEYVVVGSNRKITYELLTKAFRACLRGARYIATNPDRIFPAEDGPIPDTA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530414001 161 PFVTALEYATDTKA-TVVGKPEKTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQDVGMLGILVKT 225
Cdd:cd07531  161 AIIGAIEWCTGREPeVVVGKPSEVMAREALDILGLDAKDCAIVGDQIDVDIAMGKAIGMETALVLT 226
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
 10-225 1.73e-22

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: 92.43  E-value: 1.73e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001  10 VLVDLSGTLHIEDAAVPGAQEALKRLRGASVIIRFVTNTTKESKQDLLERLRKLEFDISEDEIFTS-LTAARSLLERK-- 86
Cdd:cd07508    2 VISDCDGVLWHDERAIPGAAEFLEALKEAGKKIVFVSNNSSRSRQDYAEKFRKFGVDVPEDQIVTSaKATARFLRSRKfg 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001  87 --------------------QVRPMLLVDDRALPDFKGIQTSDPN--AVVMGLApEHFHYQILNQAFRLLLD-GAPLIAI 143
Cdd:cd07508   82 kkvyvlgeeglkeelraagfRIAGGPSKGIETYAELVEHLEDDENvdAVIVGSD-FKLNFAKLRKACRYLRNpGCLFIAT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001 144 HKARYYK-RKDGLALGPGPFVTALEYATDTKATVVGKPEKTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQDVGMLGIL 222
Cdd:cd07508  161 APDRIHPlKDGGPIPGTGAFAAAVEAATGRQPLVLGKPSPWLGELALEKFGIDPERVLFVGDRLATDVLFGKACGFQTLL 240


                 ...
gi 530414001 223 VKT 225
Cdd:cd07508  241 VLT 243
HAD_Pase_UmpH-like cd16422
uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid ...
 11-228 2.70e-22

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: 91.34  E-value: 2.70e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001  11 LVDLSGTLHIEDAAVPGAQEALKRLRGASVIIRFVTNTTKESKQDLLERLRKLEFDISEDEIFTSLTAARSLLERKQVRP 90
Cdd:cd16422    3 IFDMDGTIYLGDDLIPGTLEFLERLHEKKRRYIFLTNNSSKNLADYVEKLNRLGIDAGLDRVFTSGEATIDHLKKEFIKP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001  91 MLLVddRALPDFKG--------IQTSDPNAVVMGLAPEhFHYQILNQAFRLLLDGAPLIAIHKARYYKRKDGLALGPGPF 162
Cdd:cd16422   83 KIFL--LGTKSLREefekagftLDGDDIDVVVLGFDTE-LTYEKLRTACLLLRRGIPYIATHPDINCPSEEGPIPDAGSI 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530414001 163 VTALEYATDTKA-TVVGKPEKTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQDVGMLGILVKT-ETR 228
Cdd:cd16422  160 IALIETSTGRRPdLVIGKPNPIILDPVLEKFDYSKEETVMVGDRLYTDIVLGINAGVDSILVLSgETT 227
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 10-86 1.24e-20

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 83.28  E-value: 1.24e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530414001   10 VLVDLSGTLHIEDAAVPGAQEALKRLRGASVIIRFVTNTTKESKQDLLERLRKLEFDISEDEIFTSLTAARSLLERK 86
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGFDIDEDEIITSGTAAADYLKER 77
PGP_euk TIGR01452
phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the ...
 10-225 1.25e-19

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: 84.92  E-value: 1.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001   10 VLVDLSGTLHIEDAAVPGAQEALKRLRGASVIIRFVTNTTKESKQDLLERLRKLEFDISEDEIFTSLTAARSLLER---- 85
Cdd:TIGR01452   5 FIFDCDGVLWLGERVVPGAPELLDRLARAGKQILFVTNNSTKSRAEYALKFARLGFNGLAEQLFSSALCAARLLRQppda 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001   86 -KQVRPMLLVDDRALPDFKGIQ--------------------TSDPN--AVVMGLaPEHFHYQILNQAFRLLLD-GAPLI 141
Cdd:TIGR01452  85 gKAVYVIGEEGLRAELDAAGIRlagdpgekkqdeadgfmydiKLDERvgAVVVGY-DEHFSYVKLMEACAHLREpGCLFV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001  142 AIHKARYYKRKDGLAL-GPGPFVTALEYATDTKATVVGKPEKTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQDVGMLG 220
Cdd:TIGR01452 164 ATNRDPWHPLSDGSRTpGTGSLVAAIETASGRQPLVVGKPSPYMFNCITEKFSIDPARTLMVGDRLETDILFGHRCGMTT 243


                  ....*
gi 530414001  221 ILVKT 225
Cdd:TIGR01452 244 VLVLS 248
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
 10-225 1.81e-18

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: 81.66  E-value: 1.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001  10 VLVDLSGTLHIEDAAVPGAQEALKRLRGASVIIRFVTNTTKESKQDLLERLRKLEFD-ISEDEIFTS-LTAARSL----- 82
Cdd:cd07510    4 FLFDCDGVLWNGEKAIPGAPETLNLLRSLGKRLVFVTNNSTKSREAYAKKFARLGFTgLKEEEIFSSaYCAARYLrqrlp 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001  83 ------------------LERKQVRPMLLVDDR-----ALPDFKGIQTSDPNAVVMGLAPeHFHYQILNQAFRLLLD-GA 138
Cdd:cd07510   84 gpadgkvyvlggeglraeLEAAGVAHLGGPDDGlrraaPKDWLLAGLDPDVGAVLVGLDE-HVNYLKLAKATQYLRDpGC 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001 139 PLIAIHKARYYKRKDGLAL-GPGPFVTALEYATDTKATVVGKPEKTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQDVG 217
Cdd:cd07510  163 LFVATNRDPWHPLSDGSFIpGTGSLVAALETASGRQAIVVGKPSRFMFDCISSKFSIDPARTCMVGDRLDTDILFGQNCG 242


                 ....*...
gi 530414001 218 MLGILVKT 225
Cdd:cd07510  243 LKTLLVLT 250
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
 10-226 3.78e-18

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: 81.20  E-value: 3.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001  10 VLVDLSGTLHIEDAAVPGAQEALKRLRGASVIIRFVTNTTKESKQDLLERLRKLEFDISEDEIFTSLTAARSLLERKQVR 89
Cdd:cd07532    9 VIFDADGVLWTGDKPIPGAVEVFNALLDKGKKVFIVTNNSTKTREELAKKAKKLGFNVKENNILSSAAVIADYLKEKGFK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001  90 PMLLV-------------------------DDRALPDFKGIQTSDPN--AVVMGLaPEHFHYQILNQAFRLLLDgaPLI- 141
Cdd:cd07532   89 KKVYVigeegirkeleeagivscggdgedeKDDSMGDFAHNLELDPDvgAVVVGR-DEHFSYPKLMKACNYLRN--PDVl 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001 142 -------AIHKARYYKRkdglALGPGPFVTALEYATDTKATVVGKPEKTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQ 214
Cdd:cd07532  166 flatnmdATFPGPVGRV----IPGAGAMVAAIEAVSGRKPLVLGKPNPQILNFLMKSGVIKPERTLMIGDRLKTDILFAN 241

                        250
                 ....*....|..
gi 530414001 215 DVGMLGILVKTE 226
Cdd:cd07532  242 NCGFQSLLVGTG 253
Hydrolase_like pfam13242
HAD-hyrolase-like;
176-225 7.66e-15

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 67.26  E-value: 7.66e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 530414001  176 VVGKPEKTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQDVGMLGILVKT 225
Cdd:pfam13242   1 VCGKPNPGMLERALARLGLDPERTVMIGDRLDTDILGAREAGARTILVLT 50
PRK10444 PRK10444
HAD-IIA family hydrolase;
7-223 7.77e-15

HAD-IIA family hydrolase;


Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 71.36  E-value: 7.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001   7 LKAVLVDLSGTLHIEDAAVPGAQEALKRLRGASVIIRFVTNTTKESKQDLLERLRKLEFDISEDEIFTSLTAARSLLERK 86
Cdd:PRK10444   1 IKNVICDIDGVLMHDNVAVPGAAEFLHRILDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFLRRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001  87 QVRPMLLVDDRALPD--FKG---IQTSDPNAVVMGlAPEHFHYQILNQAFRLLLDGAPLIAIHKARYykrkdGLALGP-- 159
Cdd:PRK10444  81 EGKKAYVIGEGALIHelYKAgftITDINPDFVIVG-ETRSYNWDMMHKAAYFVANGARFIATNPDTH-----GRGFYPac 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530414001 160 GPFVTALEYATDTKATVVGKPEKTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQDVGMLGILV 223
Cdd:PRK10444 155 GALCAGIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILV 218
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 177-233 5.10e-10

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: 57.35  E-value: 5.10e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530414001 177 VGKPEKTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQDVGMLGILVKTETRNVDGA 233
Cdd:COG1011  147 VRKPDPEIFELALERLGVPPEEALFVGDSPETDVAGARAAGMRTVWVNRSGEPAPAE 203
HAD_like cd07525
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 8-225 5.39e-10

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: 57.72  E-value: 5.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001   8 KAVLVDLSGTLHIEDAAVPGAQEALKRLRGASVIIRFVTNTTKeSKQDLLERLRKLEF-DISEDEIFTSLTAARSLLERK 86
Cdd:cd07525    1 DAFLLDLWGVLHDGNEPYPGAVEALAALRAAGKTVVLVTNAPR-PAESVVRQLAKLGVpPSTYDAIITSGEVTRELLARE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001  87 QVRP---MLLVDDRALPDFKGIQ---TSDPNA----VVMGLAPEHF----HYQ-ILNQAFRlllDGAPLIAIHKARYYKR 151
Cdd:cd07525   80 AGLGrkvYHLGPERDANVLEGLDvvaTDDAEKaefiLCTGLYDDETetpeDYRkLLKAAAA---RGLPLICANPDLVVPR 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530414001 152 KDGLALGPGPFVTALEyATDTKATVVGKPEKTFFLEALRGTGCEP-EEAVMIGDDCRDDVGGAQDVGMLGILVKT 225
Cdd:cd07525  157 GGKLIYCAGALAELYE-ELGGEVIYFGKPHPPIYDLALARLGRPAkARILAVGDGLHTDILGANAAGLDSLFVTG 230
PLN02645 PLN02645
phosphoglycolate phosphatase
 9-223 4.84e-09

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 55.49  E-value: 4.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001   9 AVLVDLSGTLHIEDAAVPGAQEALKRLRGASVIIRFVTNTTKESKQDLLERLRKLEFDISEDEIFTSLTAARSLLE---- 84
Cdd:PLN02645  30 TFIFDCDGVIWKGDKLIEGVPETLDMLRSMGKKLVFVTNNSTKSRAQYGKKFESLGLNVTEEEIFSSSFAAAAYLKsinf 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001  85 --RKQVRPM---LLVDDRALPDFKGI-------------------QTSDPNAVVMGLAPEHFHYQIlnQAFRLLL---DG 137
Cdd:PLN02645 110 pkDKKVYVIgeeGILEELELAGFQYLggpedgdkkielkpgflmeHDKDVGAVVVGFDRYINYYKI--QYATLCIrenPG 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001 138 APLIAIHK-ARYYKRKDGLALGPGPFVTALEYATDTKATVVGKPEkTFFLEALRGT-GCEPEEAVMIGDDCRDDVGGAQD 215
Cdd:PLN02645 188 CLFIATNRdAVTHLTDAQEWAGAGSMVGAIKGSTEREPLVVGKPS-TFMMDYLANKfGIEKSQICMVGDRLDTDILFGQN 266


                 ....*...
gi 530414001 216 VGMLGILV 223
Cdd:PLN02645 267 GGCKTLLV 274
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 179-223 7.32e-09

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: 52.29  E-value: 7.32e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 530414001 179 KPEKTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQDVGMLGILV 223
Cdd:cd16415   62 KPDPRIFQKALERLGVSPEEALHVGDDLKNDYLGARAVGWHALLV 106
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 177-221 2.93e-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: 50.23  E-value: 2.93e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 530414001 177 VGKPEKTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQDVGMLGI 221
Cdd:cd04305   62 VQKPNPEIFDYALNQLGVKPEETLMVGDSLESDILGAKNAGIKTV 106
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 175-223 7.66e-05

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: 40.84  E-value: 7.66e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530414001 175 TVVGKPEKTFFLEALRGTGCEPEEAVMIGDDcRDDVGGAQDVGMLGILV 223
Cdd:cd01427   59 GGTPKPKPKPLLLLLLKLGVDPEEVLFVGDS-ENDIEAARAAGGRTVAV 106
YqeG_hyp_ppase TIGR01668
HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins ...
 177-224 8.62e-05

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: 41.62  E-value: 8.62e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 530414001  177 VGKPEKTFFlEALRGTGCEPEEAVMIGDDCRDDVGGAQDVGMLGILVK 224
Cdd:TIGR01668  90 VKPPGCAFR-RAHPEMGLTSEQVAVVGDRLFTDVMGGNRNGSYTILVE 136
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
156-225 1.05e-04

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 41.84  E-value: 1.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001 156 ALGPGPFVTALEYATDTKAtvvGKPEKTFFLEALRGTGCEPEEAVMIGDDcRDDVGGAQDVGMLGILVKT 225
Cdd:COG0546  120 ALGLDDYFDAIVGGDDVPP---AKPKPEPLLEALERLGLDPEEVLMVGDS-PHDIEAARAAGVPFIGVTW 185
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 177-224 1.12e-04

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: 41.56  E-value: 1.12e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530414001 177 VGKPEKTFFLEALRGTGCEPEEAVMIgDDCRDDVGGAQDVGMLGILVK 224
Cdd:cd02603  139 VRKPDPEIYQLALERLGVKPEEVLFI-DDREENVEAARALGIHAILVT 185
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 117-223 1.78e-04

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: 40.87  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001  117 LAPEHFHY-QILNQAFRLLLDGA-PLIAIHKARYYK--------RKDGLALGPGPFVTALEYATDTKATVVGKPEKTFFL 186
Cdd:TIGR01509  63 LLYKQLFYeQIEEEAKLKPLPGVrALLEALRARGKKlalltnspRAHKLVLALLGLRDLFDVVIDSSDVGLGKPDPDIYL 142

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 530414001  187 EALRGTGCEPEEAVMIgDDCRDDVGGAQDVGMLGILV 223
Cdd:TIGR01509 143 QALKALGLEPSECVFV-DDSPAGIEAAKAAGMHTVGV 178
COG2503 COG2503
Predicted secreted acid phosphatase [General function prediction only];
23-121 1.91e-04

Predicted secreted acid phosphatase [General function prediction only];


Pssm-ID: 441997 [Multi-domain]  Cd Length: 269  Bit Score: 41.49  E-value: 1.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001  23 AAVPGAQEALKRLRGASVIIRFVTNTTKESKQDLLERLRKLEF-DISEDEIF-----TSLTAARSLLERKQvRPMLLVDD 96
Cdd:COG2503  123 TAVPGAVEFLNYANSKGVTVFYISNRKAEEKAATLANLKALGFpVVDEDHLLlktdgSDKEARRQAVAKRY-RIVMLVGD 201

                         90       100
                 ....*....|....*....|....*
gi 530414001  97 RaLPDFKGIQTSDPNAVVMGLAPEH 121
Cdd:COG2503  202 N-LGDFADAFDKKSNAERRALVEQN 225
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 178-223 2.30e-04

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: 39.56  E-value: 2.30e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 530414001 178 GKPEKTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQDVGMLGILV 223
Cdd:cd16416   63 GKPRPRAFRRALKEMDLPPEQVAMVGDQLFTDILGGNRAGLYTILV 108
YqeG COG2179
Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];
178-224 5.74e-04

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


Pssm-ID: 441782  Cd Length: 164  Bit Score: 39.34  E-value: 5.74e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 530414001 178 GKPEKTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQDVGMLGILVK 224
Cdd:COG2179   90 KKPLPRGFRKALKLMGLPPEETAVVGDQLFTDVLGGNRAGLYTILVK 136
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 7-217 1.60e-03

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: 38.34  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001    7 LKAVLVDLSGTLHIedaAVPGAQEALKRLRgasviirfvtnTTKESKQDLLERLRKLEFDISEDEIfTSLTAARSLLERK 86
Cdd:pfam00702   1 IKAVVFDLDGTLTD---GEPVVTEAIAELA-----------SEHPLAKAIVAAAEDLPIPVEDFTA-RLLLGKRDWLEEL 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001   87 qvrPMLLVDDRALPDFKGIQTSDPNAVVMGLAPEHFHYQILNQAFRLLLD-GAPLIAI-HKARYYKRKDGLALGPGPFVT 164
Cdd:pfam00702  66 ---DILRGLVETLEAEGLTVVLVELLGVIALADELKLYPGAAEALKALKErGIKVAILtGDNPEAAEALLRLLGLDDYFD 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530414001  165 ALEYATDTKatvVGKPEKTFFLEALRGTGCEPEEAVMIGDDcRDDVGGAQDVG 217
Cdd:pfam00702 143 VVISGDDVG---VGKPKPEIYLAALERLGVKPEEVLMVGDG-VNDIPAAKAAG 191
HAD_CAP cd07534
molecular class C acid phosphatases, similar to Haemophilus influenzae e (P4) acid phosphatase; ...
 23-102 5.46e-03

molecular class C acid phosphatases, similar to Haemophilus influenzae e (P4) acid phosphatase; belongs to the haloacid dehalogenase-like hydrolase superfamily; Molecular class C acid phosphatases (CAPs) are nonspecific acid phosphatases with generally broad substrate specificity and optimum activity at neutral to acidic pH. Members include Haemophilus influenzae lipoprotein e (P4), Elizabethkingia meningosepticum OlpA, Helicobacter pylori HppA, Enterobacter sp. 4 acid phosphatase PhoI, and Streptococcus pyogenes M1 GAS LppC. Lipoprotein e (P4) exhibits phosphomonoesterase activity with aryl phosphate substrates including nicotinamide mononucleotide (NMN), tyrosine phosphate, phenyl phosphate, p-nitrophenyl phosphate, and 4-methylumbelliferyl phosphate. The role of P4 in NAD+ uptake appears to be the dephosphorylation of NMN to nicotinamide riboside, which is then taken up by the organism. Elizabethkingia meningosepticum OlpA is a broad-spectrum nucleotidase with preference for 5'-nucleotides, it efficiently hydrolyzes nucleotide monophosphates, with a strong preference for 5'-nucleotides and for 3'-AMP; OlpA can also hydrolyze sugar phosphates and beta-glycerol phosphate, although with a lower efficiency. Helicobacter pylori HppA is also a 5' nucleotidase. 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: 319836 [Multi-domain]  Cd Length: 196  Bit Score: 36.93  E-value: 5.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414001  23 AAVPGAQEALKRLRGASVIIRFVTNTTKESKQDLLERLRKLEFDISEDEIF-----TSLTAARSLLERKQVRPMLLVDDR 97
Cdd:cd07534   74 KPIPGAVDFLNYANAKGVTIFYVSNRDQKLKAATLKNLKRLGFPQASDDHLllktdKSSKESRRQLVKEKYNIVLLFGDN 153


                 ....*
gi 530414001  98 aLPDF 102
Cdd:cd07534  154 -LGDF 157
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 179-226 6.73e-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: 36.23  E-value: 6.73e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530414001 179 KPEKTFFLEALRGTGCEPEEAVMIGDDCRdDVGGAQDVGMLGILVKTE 226
Cdd:COG0241  102 KPKPGMLLQAAERLGIDLSNSYMIGDRLS-DLQAAKAAGCKGILVLTG 148
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 9-75 8.05e-03

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: 35.06  E-value: 8.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530414001   9 AVLVDLSGTLHiedaavpgAQEALKRLRGASVIIRFVTNTTKESkqdLLERLRKLEFDISEDEIFTS 75
Cdd:cd01427    1 AVLFDLDGTLL--------AVELLKRLRAAGIKLAIVTNRSREA---LRALLEKLGLGDLFDGIIGS 56
 
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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