NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|22026920|ref|NP_611656|]
View 

uncharacterized protein Dmel_CG11291 [Drosophila melanogaster]

Protein Classification

HAD family hydrolase( domain architecture ID 11576405)

HAD (haloacid dehalogenase) family hydrolase; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
19-302 2.59e-155

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: 435.58  E-value: 2.59e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920  19 EWLAGIDTIICSTDGVLWQENTPIEGSVEAFNAIISKGKRCLIATNECCLTNKDLFQKAKCLGFNVKEQDIFSSSGAIAS 98
Cdd:cd07532   1 EWLANIDTVIFDADGVLWTGDKPIPGAVEVFNALLDKGKKVFIVTNNSTKTREELAKKAKKLGFNVKENNILSSAAVIAD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920  99 YLSDRKFKKKILVLGGDGIRKDLKEAGFCSVVNDLQPNDQ-KKIDFVRSLVLDPDVGAVLVARDDNMIANELLVACNYLQ 177
Cdd:cd07532  81 YLKEKGFKKKVYVIGEEGIRKELEEAGIVSCGGDGEDEKDdSMGDFAHNLELDPDVGAVVVGRDEHFSYPKLMKACNYLR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920 178 NPKVLFLTTCIDGFQPFG-KKRIPDAGSLASAIEIIVQRKPIVLGKPNQRILGKLMKSGEIKPEKTLVIGNSLKSDILFA 256
Cdd:cd07532 161 NPDVLFLATNMDATFPGPvGRVIPGAGAMVAAIEAVSGRKPLVLGKPNPQILNFLMKSGVIKPERTLMIGDRLKTDILFA 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 22026920 257 SICGFQSLLVGCDNGAIEKAEKIKKEGDEKKMKLVPDAFLSGLASF 302
Cdd:cd07532 241 NNCGFQSLLVGTGVNSLEDAEKIKKEGDPKKKDLVPDTYLPSLGHL 286
 
Name Accession Description Interval E-value
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
19-302 2.59e-155

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: 435.58  E-value: 2.59e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920  19 EWLAGIDTIICSTDGVLWQENTPIEGSVEAFNAIISKGKRCLIATNECCLTNKDLFQKAKCLGFNVKEQDIFSSSGAIAS 98
Cdd:cd07532   1 EWLANIDTVIFDADGVLWTGDKPIPGAVEVFNALLDKGKKVFIVTNNSTKTREELAKKAKKLGFNVKENNILSSAAVIAD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920  99 YLSDRKFKKKILVLGGDGIRKDLKEAGFCSVVNDLQPNDQ-KKIDFVRSLVLDPDVGAVLVARDDNMIANELLVACNYLQ 177
Cdd:cd07532  81 YLKEKGFKKKVYVIGEEGIRKELEEAGIVSCGGDGEDEKDdSMGDFAHNLELDPDVGAVVVGRDEHFSYPKLMKACNYLR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920 178 NPKVLFLTTCIDGFQPFG-KKRIPDAGSLASAIEIIVQRKPIVLGKPNQRILGKLMKSGEIKPEKTLVIGNSLKSDILFA 256
Cdd:cd07532 161 NPDVLFLATNMDATFPGPvGRVIPGAGAMVAAIEAVSGRKPLVLGKPNPQILNFLMKSGVIKPERTLMIGDRLKTDILFA 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 22026920 257 SICGFQSLLVGCDNGAIEKAEKIKKEGDEKKMKLVPDAFLSGLASF 302
Cdd:cd07532 241 NNCGFQSLLVGTGVNSLEDAEKIKKEGDPKKKDLVPDTYLPSLGHL 286
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
18-300 1.76e-45

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 154.50  E-value: 1.76e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920  18 AEWLAGIDTIICSTDGVLWQENTPIEGSVEAFNAIISKGKRCLIATNECCLTNKDLFQKAKCLGFNVKEQDIFSSSGAIA 97
Cdd:COG0647   2 SELADRYDAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920  98 SYLSDRKFKKKILVLGGDGIRKDLKEAGFcsvvndlqpndqkkidfvrSLVLDPDVGAVLVARDDNMIANELLVACNYLQ 177
Cdd:COG0647  82 AYLAERHPGARVYVIGEEGLREELEEAGL-------------------TLVDDEEPDAVVVGLDRTFTYEKLAEALRAIR 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920 178 NPkVLFLTTCIDGFQPFGKKRIPDAGSLASAIEIIVQRKPIVLGKPNQRILGKLMKSGEIKPEKTLVIGNSLKSDILFAS 257
Cdd:COG0647 143 RG-APFIATNPDRTVPTEDGLIPGAGALAAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVGDRLDTDILGAN 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 22026920 258 ICGFQSLLV--GcdngaiekaekIKKEGDEKKMKLVPDAFLSGLA 300
Cdd:COG0647 222 AAGLDTLLVltG-----------VTTAEDLEAAPIRPDYVLDSLA 255
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
27-267 6.25e-38

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: 134.38  E-value: 6.25e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920    27 IICSTDGVLWQENTPIEGSVEAFNAIISKGKRCLIATNECCLTNKDLFQK-AKCLGFNVKEQDIFSSSGAIASYLSDRKF 105
Cdd:TIGR01460   1 FLFDIDGVLWLGHKPIPGAAEALNRLRAKGKPVVFLTNNSSRSEEDYAEKlSSLLGVDVSPDQIITSGSVTKDLLRQRFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920   106 KKKILVLGGDGIRKDLKEAGF-CSVVNDLQPNDQKKIdfvrslvldpdVGAVLVARDDNMIANELLVACNYLQNPKVLFL 184
Cdd:TIGR01460  81 GEKVYVIGVGELRESLEGLGFrNDFFDDIDHLAIEKI-----------PAAVIVGEPSDFSYDELAKAAYLLAEGDVPFI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920   185 TTCIDGFQPFGKKR-IPDAGSLASAIEIIVQRKPIVLGKPNQRILGKLMKSGEIKPEKTLV-IGNSLKSDILFASICGFQ 262
Cdd:TIGR01460 150 AANRDDLVRLGDGRfRPGAGAIAAGIKELSGREPTVVGKPSPAIYRAALNLLQARPERRDVmVGDNLRTDILGAKNAGFD 229

                  ....*
gi 22026920   263 SLLVG 267
Cdd:TIGR01460 230 TLLVL 234
PLN02645 PLN02645
phosphoglycolate phosphatase
19-266 1.46e-36

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 132.91  E-value: 1.46e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920   19 EWLAGIDTIICSTDGVLWQENTPIEGSVEAFNAIISKGKRCLIATNECCLTNKDLFQKAKCLGFNVKEQDIFSSSGAIAS 98
Cdd:PLN02645  23 ELIDSVETFIFDCDGVIWKGDKLIEGVPETLDMLRSMGKKLVFVTNNSTKSRAQYGKKFESLGLNVTEEEIFSSSFAAAA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920   99 YLSDRKF--KKKILVLGGDGIRKDLKEAGFCSVVNdlqPND-QKKIDFVRSLVL--DPDVGAVLVARDDNMianellvac 173
Cdd:PLN02645 103 YLKSINFpkDKKVYVIGEEGILEELELAGFQYLGG---PEDgDKKIELKPGFLMehDKDVGAVVVGFDRYI--------- 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920  174 NY--LQ--------NPKVLFLTTCIDGFQPFGK-KRIPDAGSLASAIEIIVQRKPIVLGKPNQRILGKLMKSGEIKPEKT 242
Cdd:PLN02645 171 NYykIQyatlcireNPGCLFIATNRDAVTHLTDaQEWAGAGSMVGAIKGSTEREPLVVGKPSTFMMDYLANKFGIEKSQI 250
                        250       260
                 ....*....|....*....|....
gi 22026920  243 LVIGNSLKSDILFASICGFQSLLV 266
Cdd:PLN02645 251 CMVGDRLDTDILFGQNGGCKTLLV 274
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
27-127 1.37e-34

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 121.42  E-value: 1.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920    27 IICSTDGVLWQENTPIEGSVEAFNAIISKGKRCLIATNECCLTNKDLFQKAKCLGFNVKEQDIFSSSGAIASYLSDRKFK 106
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGFDIDEDEIITSGTAAADYLKERKFG 80
                          90       100
                  ....*....|....*....|.
gi 22026920   107 KKILVLGGDGIRKDLKEAGFC 127
Cdd:pfam13344  81 KKVLVIGSEGLREELEEAGFE 101
 
Name Accession Description Interval E-value
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
19-302 2.59e-155

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: 435.58  E-value: 2.59e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920  19 EWLAGIDTIICSTDGVLWQENTPIEGSVEAFNAIISKGKRCLIATNECCLTNKDLFQKAKCLGFNVKEQDIFSSSGAIAS 98
Cdd:cd07532   1 EWLANIDTVIFDADGVLWTGDKPIPGAVEVFNALLDKGKKVFIVTNNSTKTREELAKKAKKLGFNVKENNILSSAAVIAD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920  99 YLSDRKFKKKILVLGGDGIRKDLKEAGFCSVVNDLQPNDQ-KKIDFVRSLVLDPDVGAVLVARDDNMIANELLVACNYLQ 177
Cdd:cd07532  81 YLKEKGFKKKVYVIGEEGIRKELEEAGIVSCGGDGEDEKDdSMGDFAHNLELDPDVGAVVVGRDEHFSYPKLMKACNYLR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920 178 NPKVLFLTTCIDGFQPFG-KKRIPDAGSLASAIEIIVQRKPIVLGKPNQRILGKLMKSGEIKPEKTLVIGNSLKSDILFA 256
Cdd:cd07532 161 NPDVLFLATNMDATFPGPvGRVIPGAGAMVAAIEAVSGRKPLVLGKPNPQILNFLMKSGVIKPERTLMIGDRLKTDILFA 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 22026920 257 SICGFQSLLVGCDNGAIEKAEKIKKEGDEKKMKLVPDAFLSGLASF 302
Cdd:cd07532 241 NNCGFQSLLVGTGVNSLEDAEKIKKEGDPKKKDLVPDTYLPSLGHL 286
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
27-301 4.94e-66

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: 207.99  E-value: 4.94e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920  27 IICSTDGVLWQENTPIEGSVEAFNAIISKGKRCLIATNECCLTNKDLFQKAKCLGFNVKEQDIFSSSGAIASYLSDRKFK 106
Cdd:cd07508   2 VISDCDGVLWHDERAIPGAAEFLEALKEAGKKIVFVSNNSSRSRQDYAEKFRKFGVDVPEDQIVTSAKATARFLRSRKFG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920 107 KKILVLGGDGIRKDLKEAGFCSvVNDLQPNDQKKIDFVRSLVLDPDVGAVLVARDDNMIANELLVACNYLQNPKVLFLTT 186
Cdd:cd07508  82 KKVYVLGEEGLKEELRAAGFRI-AGGPSKGIETYAELVEHLEDDENVDAVIVGSDFKLNFAKLRKACRYLRNPGCLFIAT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920 187 CIDGFQPFGKKR-IPDAGSLASAIEIIVQRKPIVLGKPNQRILGKLMKSGEIKPEKTLVIGNSLKSDILFASICGFQSLL 265
Cdd:cd07508 161 APDRIHPLKDGGpIPGTGAFAAAVEAATGRQPLVLGKPSPWLGELALEKFGIDPERVLFVGDRLATDVLFGKACGFQTLL 240
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 22026920 266 VGCDNGAIEKAEKIkkegdeKKMKLVPDAFLSGLAS 301
Cdd:cd07508 241 VLTGVTTLEDLQAY------IDHELVPDYYADSLAD 270
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
24-300 1.53e-59

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: 191.83  E-value: 1.53e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920  24 IDTIICSTDGVLWQENTPIEGSVEAFNAIISKGKRCLIATNECCLTNKDLFQKAKCLGFNV-KEQDIFSSSGAIASYLSD 102
Cdd:cd07510   1 VDTFLFDCDGVLWNGEKAIPGAPETLNLLRSLGKRLVFVTNNSTKSREAYAKKFARLGFTGlKEEEIFSSAYCAARYLRQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920 103 R---KFKKKILVLGGDGIRKDLKEAGFCSVVNDLQPNDQKKIDFVRSLVLDPDVGAVLVARDDNMIANELLVACNYLQNP 179
Cdd:cd07510  81 RlpgPADGKVYVLGGEGLRAELEAAGVAHLGGPDDGLRRAAPKDWLLAGLDPDVGAVLVGLDEHVNYLKLAKATQYLRDP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920 180 KVLFLTTCIDGFQPF-GKKRIPDAGSLASAIEIIVQRKPIVLGKPNQRILGKLMKSGEIKPEKTLVIGNSLKSDILFASI 258
Cdd:cd07510 161 GCLFVATNRDPWHPLsDGSFIPGTGSLVAALETASGRQAIVVGKPSRFMFDCISSKFSIDPARTCMVGDRLDTDILFGQN 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 22026920 259 CGFQSLLV--GcdngaIEKAEKIKKEGDEkkmKLVPDAFLSGLA 300
Cdd:cd07510 241 CGLKTLLVltG-----VSTLEEALAKLSN---DLVPDYYVESLA 276
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
18-300 1.76e-45

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 154.50  E-value: 1.76e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920  18 AEWLAGIDTIICSTDGVLWQENTPIEGSVEAFNAIISKGKRCLIATNECCLTNKDLFQKAKCLGFNVKEQDIFSSSGAIA 97
Cdd:COG0647   2 SELADRYDAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920  98 SYLSDRKFKKKILVLGGDGIRKDLKEAGFcsvvndlqpndqkkidfvrSLVLDPDVGAVLVARDDNMIANELLVACNYLQ 177
Cdd:COG0647  82 AYLAERHPGARVYVIGEEGLREELEEAGL-------------------TLVDDEEPDAVVVGLDRTFTYEKLAEALRAIR 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920 178 NPkVLFLTTCIDGFQPFGKKRIPDAGSLASAIEIIVQRKPIVLGKPNQRILGKLMKSGEIKPEKTLVIGNSLKSDILFAS 257
Cdd:COG0647 143 RG-APFIATNPDRTVPTEDGLIPGAGALAAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVGDRLDTDILGAN 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 22026920 258 ICGFQSLLV--GcdngaiekaekIKKEGDEKKMKLVPDAFLSGLA 300
Cdd:COG0647 222 AAGLDTLLVltG-----------VTTAEDLEAAPIRPDYVLDSLA 255
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
27-267 6.25e-38

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: 134.38  E-value: 6.25e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920    27 IICSTDGVLWQENTPIEGSVEAFNAIISKGKRCLIATNECCLTNKDLFQK-AKCLGFNVKEQDIFSSSGAIASYLSDRKF 105
Cdd:TIGR01460   1 FLFDIDGVLWLGHKPIPGAAEALNRLRAKGKPVVFLTNNSSRSEEDYAEKlSSLLGVDVSPDQIITSGSVTKDLLRQRFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920   106 KKKILVLGGDGIRKDLKEAGF-CSVVNDLQPNDQKKIdfvrslvldpdVGAVLVARDDNMIANELLVACNYLQNPKVLFL 184
Cdd:TIGR01460  81 GEKVYVIGVGELRESLEGLGFrNDFFDDIDHLAIEKI-----------PAAVIVGEPSDFSYDELAKAAYLLAEGDVPFI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920   185 TTCIDGFQPFGKKR-IPDAGSLASAIEIIVQRKPIVLGKPNQRILGKLMKSGEIKPEKTLV-IGNSLKSDILFASICGFQ 262
Cdd:TIGR01460 150 AANRDDLVRLGDGRfRPGAGAIAAGIKELSGREPTVVGKPSPAIYRAALNLLQARPERRDVmVGDNLRTDILGAKNAGFD 229

                  ....*
gi 22026920   263 SLLVG 267
Cdd:TIGR01460 230 TLLVL 234
PLN02645 PLN02645
phosphoglycolate phosphatase
19-266 1.46e-36

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 132.91  E-value: 1.46e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920   19 EWLAGIDTIICSTDGVLWQENTPIEGSVEAFNAIISKGKRCLIATNECCLTNKDLFQKAKCLGFNVKEQDIFSSSGAIAS 98
Cdd:PLN02645  23 ELIDSVETFIFDCDGVIWKGDKLIEGVPETLDMLRSMGKKLVFVTNNSTKSRAQYGKKFESLGLNVTEEEIFSSSFAAAA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920   99 YLSDRKF--KKKILVLGGDGIRKDLKEAGFCSVVNdlqPND-QKKIDFVRSLVL--DPDVGAVLVARDDNMianellvac 173
Cdd:PLN02645 103 YLKSINFpkDKKVYVIGEEGILEELELAGFQYLGG---PEDgDKKIELKPGFLMehDKDVGAVVVGFDRYI--------- 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920  174 NY--LQ--------NPKVLFLTTCIDGFQPFGK-KRIPDAGSLASAIEIIVQRKPIVLGKPNQRILGKLMKSGEIKPEKT 242
Cdd:PLN02645 171 NYykIQyatlcireNPGCLFIATNRDAVTHLTDaQEWAGAGSMVGAIKGSTEREPLVVGKPSTFMMDYLANKFGIEKSQI 250
                        250       260
                 ....*....|....*....|....
gi 22026920  243 LVIGNSLKSDILFASICGFQSLLV 266
Cdd:PLN02645 251 CMVGDRLDTDILFGQNGGCKTLLV 274
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
27-127 1.37e-34

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 121.42  E-value: 1.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920    27 IICSTDGVLWQENTPIEGSVEAFNAIISKGKRCLIATNECCLTNKDLFQKAKCLGFNVKEQDIFSSSGAIASYLSDRKFK 106
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGFDIDEDEIITSGTAAADYLKERKFG 80
                          90       100
                  ....*....|....*....|.
gi 22026920   107 KKILVLGGDGIRKDLKEAGFC 127
Cdd:pfam13344  81 KKVLVIGSEGLREELEEAGFE 101
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
25-266 2.50e-34

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: 125.40  E-value: 2.50e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920  25 DTIICSTDGVLWQENTPIEGSVEAFNAIISKGKRCLIATNECCLTNKDLFQKAKCLGFNVKEQDIFSSSGAIASYLSDRK 104
Cdd:cd07530   1 KGYLIDLDGTVYRGGTAIPGAVEFIERLREKGIPFLFLTNNSTRTPEDVAAKLAEMGIDVPEEDVYTSALATAQYLAEQL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920 105 FKKKILVLGGDGIRKDLKEAGFcsVVNDLQPndqkkiDFVrSLVLDPDVG------AVLvarddnMIAN-ELLVACnylq 177
Cdd:cd07530  81 PGAKVYVIGEEGLRTALHEAGL--TLTDENP------DYV-VVGLDRDLTyeklaeATL------AIRNgAKFIAT---- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920 178 NPKVLFLTTciDGFqpfgkkrIPDAGSLASAIEIIVQRKPIVLGKPNQRILGKLMKSGEIKPEKTLVIGNSLKSDILFAS 257
Cdd:cd07530 142 NPDLTLPTE--RGL-------LPGNGSVVAALEAATGVKPLFIGKPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAAGI 212

                ....*....
gi 22026920 258 ICGFQSLLV 266
Cdd:cd07530 213 AAGIDTLLV 221
HAD_Pase_UmpH-like cd16422
uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid ...
32-266 9.26e-32

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: 118.69  E-value: 9.26e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920  32 DGVLWQENTPIEGSVEAFNAIISKGKRCLIATNECCLTNKDLFQKAKCLGFNVKEQDIFSSSGAIASYLSDRKFKKKILV 111
Cdd:cd16422   7 DGTIYLGDDLIPGTLEFLERLHEKKRRYIFLTNNSSKNLADYVEKLNRLGIDAGLDRVFTSGEATIDHLKKEFIKPKIFL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920 112 LGGDGIRKDLKEAGFcSVVNDlqpndqkkidfvrslvlDPDVgaVLVARDDNMIANELLVACNYLQNPkVLFLTTCIDGF 191
Cdd:cd16422  87 LGTKSLREEFEKAGF-TLDGD-----------------DIDV--VVLGFDTELTYEKLRTACLLLRRG-IPYIATHPDIN 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22026920 192 QPFGKKRIPDAGSLASAIEIIVQRKP-IVLGKPNQRILGKLMKSGEIKPEKTLVIGNSLKSDILFASICGFQSLLV 266
Cdd:cd16422 146 CPSEEGPIPDAGSIIALIETSTGRRPdLVIGKPNPIILDPVLEKFDYSKEETVMVGDRLYTDIVLGINAGVDSILV 221
PRK10444 PRK10444
HAD-IIA family hydrolase;
24-266 2.51e-22

HAD-IIA family hydrolase;


Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 93.32  E-value: 2.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920   24 IDTIICSTDGVLWQENTPIEGSVEAFNAIISKGKRCLIATNECCLTNKDLFQKAKCLGFNVKEQDIFSSSGAIASYLSdR 103
Cdd:PRK10444   1 IKNVICDIDGVLMHDNVAVPGAAEFLHRILDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFLR-R 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920  104 KFKKKILVLGGDGIRKDLKEAGFcsVVNDLQPndqkkiDFV-----RSLVLDP-DVGAVLVARDDNMIANellvacnylq 177
Cdd:PRK10444  80 QEGKKAYVIGEGALIHELYKAGF--TITDINP------DFVivgetRSYNWDMmHKAAYFVANGARFIAT---------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920  178 NPKVlflttcidgfqpFGKKRIPDAGSLASAIEIIVQRKPIVLGKPNQRILGKLMKSGEIKPEKTLVIGNSLKSDILFAS 257
Cdd:PRK10444 142 NPDT------------HGRGFYPACGALCAGIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGF 209

                 ....*....
gi 22026920  258 ICGFQSLLV 266
Cdd:PRK10444 210 QAGLETILV 218
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
32-266 1.13e-20

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: 88.88  E-value: 1.13e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920  32 DGVLWQENTPIEGSVEAFNAIISKGKRCLIATNECCLTNKDLFQKAKCLGFNVKEQDIFSSSGAIASYLSDRKFKKKILV 111
Cdd:cd07509   8 SGTLYISGAAIPGAAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQRLGFDVSEEEIFTSLTAARQYLEEKGLRPHLLV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920 112 lgGDGIRKDLKE----AGFCSVVNDLQPN-DQKKIDFVRSLVLDpdvGAVLVARDDNMianellvacnYLQNPKVLFLtt 186
Cdd:cd07509  88 --DDDALEDFIGidtsDPNAVVIGDAGEHfNYQTLNRAFRLLLD---GAPLIALHKGR----------YYKRKDGLAL-- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920 187 cidgfqpfgkkripDAGSLASAIEIIVQRKPIVLGKPNQRILGKLMKSGEIKPEKTLVIGNSLKSDILFASICGFQSLLV 266
Cdd:cd07509 151 --------------DPGAFVTGLEYATGIKATVVGKPSPEFFLSALRSLGVDPEEAVMIGDDLRDDVGGAQACGMRGILV 216
HAD_Pase_UmpH-like cd07531
UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar ...
25-266 4.63e-19

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: 84.54  E-value: 4.63e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920  25 DTIICSTDGVLWQENTPIEGSVEAFNAIISKGKRCLIATNECCLTNKDLFQKAKCLGFNVKEQDIFSSSGAIASYLSDRK 104
Cdd:cd07531   1 KGYIIDLDGTIGKGVTLIPGAVEGVKTLRRLGKKIIFLSNNSTRSRRILLERLRSFGIEVGEDEILVSSYVTARFLAREK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920 105 FKKKILVLGGDGIRKDLKEAGFcsvvndlqpndqkkidfvrSLVLDPDVGAVLVARDDNMIANELLVACNYLQNPKVLFL 184
Cdd:cd07531  81 PNAKVFVTGEEGLIEELRLAGL-------------------EIVDKYDEAEYVVVGSNRKITYELLTKAFRACLRGARYI 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920 185 TTCIDGFQPFGKKRIPDAGSLASAIEIIVQRKP-IVLGKPNQRILGKLMKSGEIKPEKTLVIGNSLKSDILFASICGFQS 263
Cdd:cd07531 142 ATNPDRIFPAEDGPIPDTAAIIGAIEWCTGREPeVVVGKPSEVMAREALDILGLDAKDCAIVGDQIDVDIAMGKAIGMET 221

                ...
gi 22026920 264 LLV 266
Cdd:cd07531 222 ALV 224
HAD_like cd07525
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
25-266 1.98e-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: 60.03  E-value: 1.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920  25 DTIICSTDGVLWQENTPIEGSVEAFNAIISKGKRCLIATNECCLTNkDLFQKAKCLGFNVKEQDIFSSSGAIASYLSDRK 104
Cdd:cd07525   1 DAFLLDLWGVLHDGNEPYPGAVEALAALRAAGKTVVLVTNAPRPAE-SVVRQLAKLGVPPSTYDAIITSGEVTRELLARE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920 105 FK--KKILVLGGDGIRkdlkeagfcSVVNDLQpndqkkidfvRSLVLDPDVGAVLVA---RDDNMIANELLVA-CNYLQN 178
Cdd:cd07525  80 AGlgRKVYHLGPERDA---------NVLEGLD----------VVATDDAEKAEFILCtglYDDETETPEDYRKlLKAAAA 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026920 179 PKVLFLTTCIDGFQPFGKKRIPDAGSLASAIEIIVQrKPIVLGKPNQRILGKLMK-SGEIKPEKTLVIGNSLKSDILFAS 257
Cdd:cd07525 141 RGLPLICANPDLVVPRGGKLIYCAGALAELYEELGG-EVIYFGKPHPPIYDLALArLGRPAKARILAVGDGLHTDILGAN 219

                ....*....
gi 22026920 258 ICGFQSLLV 266
Cdd:cd07525 220 AAGLDSLFV 228
Hydrolase_like pfam13242
HAD-hyrolase-like;
219-284 7.71e-07

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 46.07  E-value: 7.71e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22026920   219 VLGKPNQRILGKLMKSGEIKPEKTLVIGNSLKSDILFASICGFQSLLVGCDNGAIEKAEKIKKEGD 284
Cdd:pfam13242   1 VCGKPNPGMLERALARLGLDPERTVMIGDRLDTDILGAREAGARTILVLTGVTRPADLEKAPIRPD 66
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
221-266 5.05e-03

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: 36.09  E-value: 5.05e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 22026920 221 GKPNQRILGKLMKSGEIKPEKTLVIGNSLKSDILFASICGFQSLLV 266
Cdd:cd16416  63 GKPRPRAFRRALKEMDLPPEQVAMVGDQLFTDILGGNRAGLYTILV 108
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH
HHS Vulnerability Disclosure