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Conserved domains on  [gi|939619903|ref|NP_001303369|]
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uncharacterized protein Dmel_CG5577, isoform B [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

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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 ...
 19-311 1.08e-144

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: 409.00  E-value: 1.08e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  19 EWLQSFDTVLCDGDGTIWQDDTAIAGAPDVVNALQDrFDKKVYLITNNGLKTRQELFERSQRLGFHLPSDrHIISPTAAI 98
Cdd:cd07532    1 EWLANIDTVIFDADGVLWTGDKPIPGAVEVFNALLD-KGKKVFIVTNNSTKTREELAKKAKKLGFNVKEN-NILSSAAVI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  99 ADYLVGSPKfdrtRHKVYVVGNAAIARELRQRGIDSYGAGGTDELPpgdkwpDFVTREFGNPEAAKDVGAVVVGWDEYFS 178
Cdd:cd07532   79 ADYLKEKGF----KKKVYVIGEEGIRKELEEAGIVSCGGDGEDEKD------DSMGDFAHNLELDPDVGAVVVGRDEHFS 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 179 YCKMARACHILCsNPDAAFLVTNRDAVHKYP-SFCIPGTGAFVAGIEACSEREALEMGKPNPLVLEPFIKAEGLRTERTL 257
Cdd:cd07532  149 YPKLMKACNYLR-NPDVLFLATNMDATFPGPvGRVIPGAGAMVAAIEAVSGRKPLVLGKPNPQILNFLMKSGVIKPERTL 227

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 939619903 258 MIGDCLKIDVGFASNCGMLSLLVGTGRYNNLSDVRL-----EKDRLPQPDFYLPRLGDL 311
Cdd:cd07532  228 MIGDRLKTDILFANNCGFQSLLVGTGVNSLEDAEKIkkegdPKKKDLVPDTYLPSLGHL 286
 
Name Accession Description Interval E-value
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
 19-311 1.08e-144

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: 409.00  E-value: 1.08e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  19 EWLQSFDTVLCDGDGTIWQDDTAIAGAPDVVNALQDrFDKKVYLITNNGLKTRQELFERSQRLGFHLPSDrHIISPTAAI 98
Cdd:cd07532    1 EWLANIDTVIFDADGVLWTGDKPIPGAVEVFNALLD-KGKKVFIVTNNSTKTREELAKKAKKLGFNVKEN-NILSSAAVI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  99 ADYLVGSPKfdrtRHKVYVVGNAAIARELRQRGIDSYGAGGTDELPpgdkwpDFVTREFGNPEAAKDVGAVVVGWDEYFS 178
Cdd:cd07532   79 ADYLKEKGF----KKKVYVIGEEGIRKELEEAGIVSCGGDGEDEKD------DSMGDFAHNLELDPDVGAVVVGRDEHFS 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 179 YCKMARACHILCsNPDAAFLVTNRDAVHKYP-SFCIPGTGAFVAGIEACSEREALEMGKPNPLVLEPFIKAEGLRTERTL 257
Cdd:cd07532  149 YPKLMKACNYLR-NPDVLFLATNMDATFPGPvGRVIPGAGAMVAAIEAVSGRKPLVLGKPNPQILNFLMKSGVIKPERTL 227

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 939619903 258 MIGDCLKIDVGFASNCGMLSLLVGTGRYNNLSDVRL-----EKDRLPQPDFYLPRLGDL 311
Cdd:cd07532  228 MIGDRLKTDILFANNCGFQSLLVGTGVNSLEDAEKIkkegdPKKKDLVPDTYLPSLGHL 286
PGP_euk TIGR01452
phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the ...
 25-311 1.02e-62

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: 200.09  E-value: 1.02e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903   25 DTVLCDGDGTIWQDDTAIAGAPDVVNALQdRFDKKVYLITNNGLKTRQELFERSQRLGFHLpSDRHIISPTAAIADYLVG 104
Cdd:TIGR01452   3 QGFIFDCDGVLWLGERVVPGAPELLDRLA-RAGKQILFVTNNSTKSRAEYALKFARLGFNG-LAEQLFSSALCAARLLRQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  105 SPKFDRtrhKVYVVGNAAIARELRQRGIDSYGAGGTDELPPGDKWPDFVTREfgnpeaaKDVGAVVVGWDEYFSYCKMAR 184
Cdd:TIGR01452  81 PPDAGK---AVYVIGEEGLRAELDAAGIRLAGDPGEKKQDEADGFMYDIKLD-------ERVGAVVVGYDEHFSYVKLME 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  185 ACHILcSNPDAAFLVTNRDAVHKYPSFC-IPGTGAFVAGIEACSEREALEMGKPNPLVLEPFIKAEGLRTERTLMIGDCL 263
Cdd:TIGR01452 151 ACAHL-REPGCLFVATNRDPWHPLSDGSrTPGTGSLVAAIETASGRQPLVVGKPSPYMFNCITEKFSIDPARTLMVGDRL 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 939619903  264 KIDVGFASNCGMLSLLVGTG--RYNNLSDVRLEKDRLPQPDFYLPRLGDL 311
Cdd:TIGR01452 230 ETDILFGHRCGMTTVLVLSGvsQLEEAQEYLMAGQDDLVPDYVVESLADL 279
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
18-312 1.04e-57

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 186.47  E-value: 1.04e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  18 SEWLQSFDTVLCDGDGTIWQDDTAIAGAPDVVNALQDRfDKKVYLITNNGLKTRQELFERSQRLGFHLPSDrHIISPTAA 97
Cdd:COG0647    2 SELADRYDAFLLDLDGVLYRGDEPIPGAVEALARLRAA-GKPVLFLTNNSSRTPEDVAEKLRRLGIPVAED-EIVTSGDA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  98 IADYLvgspkfdRTRH---KVYVVGNAAIARELRQRGIDsygaggtdelppgdkwpdfvtrefgnPEAAKDVGAVVVGWD 174
Cdd:COG0647   80 TAAYL-------AERHpgaRVYVIGEEGLREELEEAGLT--------------------------LVDDEEPDAVVVGLD 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 175 EYFSYCKMARACHILcsNPDAAFLVTNRDAVhkYPS---FcIPGTGAFVAGIEACSEREALEMGKPNPLVLEPFIKAEGL 251
Cdd:COG0647  127 RTFTYEKLAEALRAI--RRGAPFIATNPDRT--VPTedgL-IPGAGALAAALEAATGGEPLVVGKPSPPIYELALERLGV 201

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939619903 252 RTERTLMIGDCLKIDVGFASNCGMLSLLVGTGrynnLSDVRLEKDRLPQPDFYLPRLGDLL 312
Cdd:COG0647  202 DPERVLMVGDRLDTDILGANAAGLDTLLVLTG----VTTAEDLEAAPIRPDYVLDSLAELL 258
PLN02645 PLN02645
phosphoglycolate phosphatase
 1-315 2.58e-55

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 182.22  E-value: 2.58e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903   1 MSRGGAIDLTGLSEEQVSEWLQSFDTVLCDGDGTIWQDDTAIAGAPDVVNALQDRfDKKVYLITNNGLKTRQELFERSQR 80
Cdd:PLN02645   5 TPAAMAAAAQLLTLENADELIDSVETFIFDCDGVIWKGDKLIEGVPETLDMLRSM-GKKLVFVTNNSTKSRAQYGKKFES 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  81 LGFHLPSDRhIISPTAAIADYLvGSPKFDRTRhKVYVVGNAAIARELRQRGIDSYGaGGTDelppGDKWPDFVTREFgnP 160
Cdd:PLN02645  84 LGLNVTEEE-IFSSSFAAAAYL-KSINFPKDK-KVYVIGEEGILEELELAGFQYLG-GPED----GDKKIELKPGFL--M 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 161 EAAKDVGAVVVGWDEYFSYCKMARACHILCSNPDAAFLVTNRDAV-HKYPSFCIPGTGAFVAGIEACSEREALEMGKPNP 239
Cdd:PLN02645 154 EHDKDVGAVVVGFDRYINYYKIQYATLCIRENPGCLFIATNRDAVtHLTDAQEWAGAGSMVGAIKGSTEREPLVVGKPST 233

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939619903 240 LVLEPFIKAEGLRTERTLMIGDCLKIDVGFASNCGMLSLLVGTGrYNNLSDVRLEKDRLpQPDFYLPRLGDLLNIL 315
Cdd:PLN02645 234 FMMDYLANKFGIEKSQICMVGDRLDTDILFGQNGGCKTLLVLSG-VTSESMLLSPENKI-QPDFYTSKISDFLTLK 307
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 27-132 1.73e-26

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 100.23  E-value: 1.73e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903   27 VLCDGDGTIWQDDTAIAGAPDVVNALQDRfDKKVYLITNNGLKTRQELFERSQRLGFHLPSDrHIISPTAAIADYLvGSP 106
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAA-GKPVVFVTNNSSRSREEYAEKLRKLGFDIDED-EIITSGTAAADYL-KER 77

                          90       100
                  ....*....|....*....|....*.
gi 939619903  107 KFDRtrhKVYVVGNAAIARELRQRGI 132
Cdd:pfam13344  78 KFGK---KVLVIGSEGLREELEEAGF 100
 
Name Accession Description Interval E-value
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
 19-311 1.08e-144

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: 409.00  E-value: 1.08e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  19 EWLQSFDTVLCDGDGTIWQDDTAIAGAPDVVNALQDrFDKKVYLITNNGLKTRQELFERSQRLGFHLPSDrHIISPTAAI 98
Cdd:cd07532    1 EWLANIDTVIFDADGVLWTGDKPIPGAVEVFNALLD-KGKKVFIVTNNSTKTREELAKKAKKLGFNVKEN-NILSSAAVI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  99 ADYLVGSPKfdrtRHKVYVVGNAAIARELRQRGIDSYGAGGTDELPpgdkwpDFVTREFGNPEAAKDVGAVVVGWDEYFS 178
Cdd:cd07532   79 ADYLKEKGF----KKKVYVIGEEGIRKELEEAGIVSCGGDGEDEKD------DSMGDFAHNLELDPDVGAVVVGRDEHFS 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 179 YCKMARACHILCsNPDAAFLVTNRDAVHKYP-SFCIPGTGAFVAGIEACSEREALEMGKPNPLVLEPFIKAEGLRTERTL 257
Cdd:cd07532  149 YPKLMKACNYLR-NPDVLFLATNMDATFPGPvGRVIPGAGAMVAAIEAVSGRKPLVLGKPNPQILNFLMKSGVIKPERTL 227

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 939619903 258 MIGDCLKIDVGFASNCGMLSLLVGTGRYNNLSDVRL-----EKDRLPQPDFYLPRLGDL 311
Cdd:cd07532  228 MIGDRLKTDILFANNCGFQSLLVGTGVNSLEDAEKIkkegdPKKKDLVPDTYLPSLGHL 286
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
 24-315 2.59e-70

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: 219.57  E-value: 2.59e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  24 FDTVLCDGDGTIWQDDTAIAGAPDVVNALQdRFDKKVYLITNNGLKTRQELFERSQRLGFHLPSDRHIISPTAAIADYLV 103
Cdd:cd07510    1 VDTFLFDCDGVLWNGEKAIPGAPETLNLLR-SLGKRLVFVTNNSTKSREAYAKKFARLGFTGLKEEEIFSSAYCAARYLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 104 GSPKFDRTRhKVYVVGNAAIARELRQRGIDSygAGGTDELPPGDKWPDFVtrefgNPEAAKDVGAVVVGWDEYFSYCKMA 183
Cdd:cd07510   80 QRLPGPADG-KVYVLGGEGLRAELEAAGVAH--LGGPDDGLRRAAPKDWL-----LAGLDPDVGAVLVGLDEHVNYLKLA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 184 RACHILcSNPDAAFLVTNRDAVH--KYPSFcIPGTGAFVAGIEACSEREALEMGKPNPLVLEPFIKAEGLRTERTLMIGD 261
Cdd:cd07510  152 KATQYL-RDPGCLFVATNRDPWHplSDGSF-IPGTGSLVAALETASGRQAIVVGKPSRFMFDCISSKFSIDPARTCMVGD 229

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 939619903 262 CLKIDVGFASNCGMLSLLVGTGrYNNLSDVRLEKDRLPQPDFYLPRLGDLLNIL 315
Cdd:cd07510  230 RLDTDILFGQNCGLKTLLVLTG-VSTLEEALAKLSNDLVPDYYVESLADLLELL 282
PGP_euk TIGR01452
phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the ...
 25-311 1.02e-62

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: 200.09  E-value: 1.02e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903   25 DTVLCDGDGTIWQDDTAIAGAPDVVNALQdRFDKKVYLITNNGLKTRQELFERSQRLGFHLpSDRHIISPTAAIADYLVG 104
Cdd:TIGR01452   3 QGFIFDCDGVLWLGERVVPGAPELLDRLA-RAGKQILFVTNNSTKSRAEYALKFARLGFNG-LAEQLFSSALCAARLLRQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  105 SPKFDRtrhKVYVVGNAAIARELRQRGIDSYGAGGTDELPPGDKWPDFVTREfgnpeaaKDVGAVVVGWDEYFSYCKMAR 184
Cdd:TIGR01452  81 PPDAGK---AVYVIGEEGLRAELDAAGIRLAGDPGEKKQDEADGFMYDIKLD-------ERVGAVVVGYDEHFSYVKLME 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  185 ACHILcSNPDAAFLVTNRDAVHKYPSFC-IPGTGAFVAGIEACSEREALEMGKPNPLVLEPFIKAEGLRTERTLMIGDCL 263
Cdd:TIGR01452 151 ACAHL-REPGCLFVATNRDPWHPLSDGSrTPGTGSLVAAIETASGRQPLVVGKPSPYMFNCITEKFSIDPARTLMVGDRL 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 939619903  264 KIDVGFASNCGMLSLLVGTG--RYNNLSDVRLEKDRLPQPDFYLPRLGDL 311
Cdd:TIGR01452 230 ETDILFGHRCGMTTVLVLSGvsQLEEAQEYLMAGQDDLVPDYVVESLADL 279
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
 27-310 2.54e-61

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: 196.05  E-value: 2.54e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  27 VLCDGDGTIWQDDTAIAGAPDVVNALQDRfDKKVYLITNNGLKTRQELFERSQRLGFHLPSDRhIISPTAAIADYLVgSP 106
Cdd:cd07508    2 VISDCDGVLWHDERAIPGAAEFLEALKEA-GKKIVFVSNNSSRSRQDYAEKFRKFGVDVPEDQ-IVTSAKATARFLR-SR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 107 KFdrtRHKVYVVGNAAIARELRQRGIDSYGAGGTDELPPGDkwpdFVTREFGNPEaakdVGAVVVGWDEYFSYCKMARAC 186
Cdd:cd07508   79 KF---GKKVYVLGEEGLKEELRAAGFRIAGGPSKGIETYAE----LVEHLEDDEN----VDAVIVGSDFKLNFAKLRKAC 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 187 hILCSNPDAAFLVTNRDAVH--KYPSFcIPGTGAFVAGIEACSEREALEMGKPNPLVLEPFIKAEGLRTERTLMIGDCLK 264
Cdd:cd07508  148 -RYLRNPGCLFIATAPDRIHplKDGGP-IPGTGAFAAAVEAATGRQPLVLGKPSPWLGELALEKFGIDPERVLFVGDRLA 225

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 939619903 265 IDVGFASNCGMLSLLVGTGrYNNLSDVRLEKDRLPQPDFYLPRLGD 310
Cdd:cd07508  226 TDVLFGKACGFQTLLVLTG-VTTLEDLQAYIDHELVPDYYADSLAD 270
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
18-312 1.04e-57

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 186.47  E-value: 1.04e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  18 SEWLQSFDTVLCDGDGTIWQDDTAIAGAPDVVNALQDRfDKKVYLITNNGLKTRQELFERSQRLGFHLPSDrHIISPTAA 97
Cdd:COG0647    2 SELADRYDAFLLDLDGVLYRGDEPIPGAVEALARLRAA-GKPVLFLTNNSSRTPEDVAEKLRRLGIPVAED-EIVTSGDA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  98 IADYLvgspkfdRTRH---KVYVVGNAAIARELRQRGIDsygaggtdelppgdkwpdfvtrefgnPEAAKDVGAVVVGWD 174
Cdd:COG0647   80 TAAYL-------AERHpgaRVYVIGEEGLREELEEAGLT--------------------------LVDDEEPDAVVVGLD 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 175 EYFSYCKMARACHILcsNPDAAFLVTNRDAVhkYPS---FcIPGTGAFVAGIEACSEREALEMGKPNPLVLEPFIKAEGL 251
Cdd:COG0647  127 RTFTYEKLAEALRAI--RRGAPFIATNPDRT--VPTedgL-IPGAGALAAALEAATGGEPLVVGKPSPPIYELALERLGV 201

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939619903 252 RTERTLMIGDCLKIDVGFASNCGMLSLLVGTGrynnLSDVRLEKDRLPQPDFYLPRLGDLL 312
Cdd:COG0647  202 DPERVLMVGDRLDTDILGANAAGLDTLLVLTG----VTTAEDLEAAPIRPDYVLDSLAELL 258
PLN02645 PLN02645
phosphoglycolate phosphatase
 1-315 2.58e-55

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 182.22  E-value: 2.58e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903   1 MSRGGAIDLTGLSEEQVSEWLQSFDTVLCDGDGTIWQDDTAIAGAPDVVNALQDRfDKKVYLITNNGLKTRQELFERSQR 80
Cdd:PLN02645   5 TPAAMAAAAQLLTLENADELIDSVETFIFDCDGVIWKGDKLIEGVPETLDMLRSM-GKKLVFVTNNSTKSRAQYGKKFES 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  81 LGFHLPSDRhIISPTAAIADYLvGSPKFDRTRhKVYVVGNAAIARELRQRGIDSYGaGGTDelppGDKWPDFVTREFgnP 160
Cdd:PLN02645  84 LGLNVTEEE-IFSSSFAAAAYL-KSINFPKDK-KVYVIGEEGILEELELAGFQYLG-GPED----GDKKIELKPGFL--M 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 161 EAAKDVGAVVVGWDEYFSYCKMARACHILCSNPDAAFLVTNRDAV-HKYPSFCIPGTGAFVAGIEACSEREALEMGKPNP 239
Cdd:PLN02645 154 EHDKDVGAVVVGFDRYINYYKIQYATLCIRENPGCLFIATNRDAVtHLTDAQEWAGAGSMVGAIKGSTEREPLVVGKPST 233

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939619903 240 LVLEPFIKAEGLRTERTLMIGDCLKIDVGFASNCGMLSLLVGTGrYNNLSDVRLEKDRLpQPDFYLPRLGDLLNIL 315
Cdd:PLN02645 234 FMMDYLANKFGIEKSQICMVGDRLDTDILFGQNGGCKTLLVLSG-VTSESMLLSPENKI-QPDFYTSKISDFLTLK 307
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 25-310 1.46e-40

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: 141.96  E-value: 1.46e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  25 DTVLCDGDGTIWQDDTAIAGAPDVVNALQDRfDKKVYLITNNGLKTRQELFERSQRLGFHLPSDrHIISPTAAIADYLvg 104
Cdd:cd07530    1 KGYLIDLDGTVYRGGTAIPGAVEFIERLREK-GIPFLFLTNNSTRTPEDVAAKLAEMGIDVPEE-DVYTSALATAQYL-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 105 spkfdRTRH---KVYVVGNAAIARELRQRGIdsygaGGTDElppgdkwpdfvtrefgNPEAakdvgaVVVGWDEYFSYCK 181
Cdd:cd07530   77 -----AEQLpgaKVYVIGEEGLRTALHEAGL-----TLTDE----------------NPDY------VVVGLDRDLTYEK 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 182 MARACHILcsNPDAAFLVTNRDAVHKYPSFCIPGTGAFVAGIEACSEREALEMGKPNPLVLEPFIKAEGLRTERTLMIGD 261
Cdd:cd07530  125 LAEATLAI--RNGAKFIATNPDLTLPTERGLLPGNGSVVAALEAATGVKPLFIGKPEPIMMRAALEKLGLKSEETLMVGD 202

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 939619903 262 CLKIDVGFASNCGMLSLLVGTGrYNNLSDVRLEKDRlpqPDFYLPRLGD 310
Cdd:cd07530  203 RLDTDIAAGIAAGIDTLLVLTG-VTTREDLAKPPYR---PTYIVPSLRE 247
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 27-283 6.63e-39

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: 137.07  E-value: 6.63e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903   27 VLCDGDGTIWQDDTAIAGAPDVVNALQDRfDKKVYLITNNGLKTRQELFERSQRLGFHLPSDRHIISPTAAIADYLvgsp 106
Cdd:TIGR01460   1 FLFDIDGVLWLGHKPIPGAAEALNRLRAK-GKPVVFLTNNSSRSEEDYAEKLSSLLGVDVSPDQIITSGSVTKDLL---- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  107 kfdRTRH---KVYVVGNAAIARELRQRGIDsygaggtdelppgdkwpdFVTREFGNP-EAAKDVGAVVVGWDEYFSYCKM 182
Cdd:TIGR01460  76 ---RQRFegeKVYVIGVGELRESLEGLGFR------------------NDFFDDIDHlAIEKIPAAVIVGEPSDFSYDEL 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  183 ARACHILcSNPDAAFLVTNRDA-VHKYPSFCIPGTGAFVAGIEACSEREALEMGKPNPLVLEPFIKAEGLRTERT-LMIG 260
Cdd:TIGR01460 135 AKAAYLL-AEGDVPFIAANRDDlVRLGDGRFRPGAGAIAAGIKELSGREPTVVGKPSPAIYRAALNLLQARPERRdVMVG 213

                         250       260
                  ....*....|....*....|...
gi 939619903  261 DCLKIDVGFASNCGMLSLLVGTG 283
Cdd:TIGR01460 214 DNLRTDILGAKNAGFDTLLVLTG 236
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 27-315 3.02e-33

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: 122.77  E-value: 3.02e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  27 VLCDGDGTIWQDDTAIAGAPDVVNALQDRfDKKVYLITNNGLKTRQELFERSQRLGFHLPSDrHIISPTAAIADYLvgsp 106
Cdd:cd07509    3 VLLDLSGTLYISGAAIPGAAEALKRLRHA-GLKVRFLTNTTKESRRTLAERLQRLGFDVSEE-EIFTSLTAARQYL---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 107 kfdrtrhkvyvvgnaaiarelRQRGIDSYgaggtdELPPGDKWPDFVTREFGNPEAakdvgaVVVG-WDEYFSYCKMARA 185
Cdd:cd07509   77 ---------------------EEKGLRPH------LLVDDDALEDFIGIDTSDPNA------VVIGdAGEHFNYQTLNRA 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 186 CHILCsnpDAAFLVtnrdAVHKYPSF------CIpGTGAFVAGIEACSEREALEMGKPNPLVLEPFIKAEGLRTERTLMI 259
Cdd:cd07509  124 FRLLL---DGAPLI----ALHKGRYYkrkdglAL-DPGAFVTGLEYATGIKATVVGKPSPEFFLSALRSLGVDPEEAVMI 195

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 939619903 260 GDCLKIDVGFASNCGMLSLLVGTGRYnnlsDVRLEKDRLPQPDFYLPRLGDLLNIL 315
Cdd:cd07509  196 GDDLRDDVGGAQACGMRGILVRTGKY----RPSDEKKPNVPPDLTADSFADAVDHI 247
HAD_Pase_UmpH-like cd07531
UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar ...
 25-312 7.08e-30

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: 113.82  E-value: 7.08e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  25 DTVLCDGDGTIWQDDTAIAGAPDVVNALQdRFDKKVYLITNNGLKTRQELFERSQRLGFHLPSDRhIISPTAAIADYLVG 104
Cdd:cd07531    1 KGYIIDLDGTIGKGVTLIPGAVEGVKTLR-RLGKKIIFLSNNSTRSRRILLERLRSFGIEVGEDE-ILVSSYVTARFLAR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 105 SPKFDrtrhKVYVVGNAAIARELRQRGIDSYGAGGTDELppgdkwpdfvtrefgnpeaakdvgaVVVGWDEYFSYCKMAR 184
Cdd:cd07531   79 EKPNA----KVFVTGEEGLIEELRLAGLEIVDKYDEAEY-------------------------VVVGSNRKITYELLTK 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 185 ACHILCSNpdAAFLVTNRDAVHKYPSFCIPGTGAFVAGIEACSEREA-LEMGKPNPLVLEPFIKAEGLRTERTLMIGDCL 263
Cdd:cd07531  130 AFRACLRG--ARYIATNPDRIFPAEDGPIPDTAAIIGAIEWCTGREPeVVVGKPSEVMAREALDILGLDAKDCAIVGDQI 207

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 939619903 264 KIDVGFASNCGMLSLLVGTGrynnlSDVRLEKDRLP-QPDFYLPRLGDLL 312
Cdd:cd07531  208 DVDIAMGKAIGMETALVLTG-----VTTRENLDRHGyKPDYVLNSIKDLV 252
HAD_Pase_UmpH-like cd16422
uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid ...
 28-310 3.01e-28

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: 109.45  E-value: 3.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  28 LCDGDGTIWQDDTAIAGAPDVVNALQdRFDKKVYLITNNGLKTRQELFERSQRLGFHLPSDRhIISPTAAIADYLvgspK 107
Cdd:cd16422    3 IFDMDGTIYLGDDLIPGTLEFLERLH-EKKRRYIFLTNNSSKNLADYVEKLNRLGIDAGLDR-VFTSGEATIDHL----K 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 108 FDRTRHKVYVVGNAAIARELRQRGIDSYGaggtdelppgdkwpdfvtrefgnpeaaKDVGAVVVGWDEYFSYCKMARACH 187
Cdd:cd16422   77 KEFIKPKIFLLGTKSLREEFEKAGFTLDG---------------------------DDIDVVVLGFDTELTYEKLRTACL 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 188 ILcSNPdAAFLVTNRDAVHKYPSFCIPGTGAFVAGIEACSER-EALEMGKPNPLVLEPFIKAEGLRTERTLMIGDCLKID 266
Cdd:cd16422  130 LL-RRG-IPYIATHPDINCPSEEGPIPDAGSIIALIETSTGRrPDLVIGKPNPIILDPVLEKFDYSKEETVMVGDRLYTD 207

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 939619903 267 VGFASNCGMLSLLVGTGRynnlSDVRLEKDRLPQPDFYLPRLGD 310
Cdd:cd16422  208 IVLGINAGVDSILVLSGE----TTREDLEDLERKPTYVFDNVGE 247
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 27-132 1.73e-26

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 100.23  E-value: 1.73e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903   27 VLCDGDGTIWQDDTAIAGAPDVVNALQDRfDKKVYLITNNGLKTRQELFERSQRLGFHLPSDrHIISPTAAIADYLvGSP 106
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAA-GKPVVFVTNNSSRSREEYAEKLRKLGFDIDED-EIITSGTAAADYL-KER 77

                          90       100
                  ....*....|....*....|....*.
gi 939619903  107 KFDRtrhKVYVVGNAAIARELRQRGI 132
Cdd:pfam13344  78 KFGK---KVLVIGSEGLREELEEAGF 100
HAD-SF-IIA-hyp3 TIGR01458
HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of ...
 27-315 3.49e-24

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: 98.78  E-value: 3.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903   27 VLCDGDGTIWQDD----TAIAGAPDVVNALQdRFDKKVYLITNNGLKTRQELFERSQRLGFHLpSDRHIISPTAAIADYL 102
Cdd:TIGR01458   4 VLLDISGVLYISDagggTAVPGSQEAVKRLR-GASVKVRFVTNTTKESKQDLLERLQRLGFDI-SEDEVFTPAPAARQLL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  103 vgspkfdrtrhkvyvvgnaaiarelRQRGIDSYgaggtdELPPGDKWPDFVTREFGNPEAakdvgaVVVG-WDEYFSYCK 181
Cdd:TIGR01458  82 -------------------------EEKQLRPM------LLVDDRVLPDFDGIDTSDPNC------VVMGlAPEHFSYQI 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  182 MARACHILCSNPDAAFLVTNRDAVHKYPSFCIPGTGAFVAGIEACSEREALEMGKPNPLVLEPFIKAEGLRTERTLMIGD 261
Cdd:TIGR01458 125 LNQAFRLLLDGAKPVLIAIGKGRYYKRKDGLALDVGPFVTALEYATDTKATVVGKPSKTFFLEALRATGCEPEEAVMIGD 204

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 939619903  262 CLKIDVGFASNCGMLSLLVGTGRYNNLSDVRLEkdrlPQPDFYLPRLGDLLNIL 315
Cdd:TIGR01458 205 DCRDDVGGAQDCGMRGIQVRTGKYRPSDEEKIN----VPPDLTCDSLPHAVDLI 254
PRK10444 PRK10444
HAD-IIA family hydrolase;
27-311 6.29e-20

HAD-IIA family hydrolase;


Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 87.16  E-value: 6.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  27 VLCDGDGTIWQDDTAIAGAPDVVNALQDRFDKKVYLiTNNGLKTRQELFERSQRLGFHLPSDRHIISPTAAiADYLVgsp 106
Cdd:PRK10444   4 VICDIDGVLMHDNVAVPGAAEFLHRILDKGLPLVLL-TNYPSQTGQDLANRFATAGVDVPDSVFYTSAMAT-ADFLR--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 107 kfDRTRHKVYVVGNAAIARELrqrgidsYGAGGTDElppgDKWPDFVtrefgnpeaakdvgavVVGWDEYFSYCKMARAC 186
Cdd:PRK10444  79 --RQEGKKAYVIGEGALIHEL-------YKAGFTIT----DINPDFV----------------IVGETRSYNWDMMHKAA 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 187 HILCSNpdAAFLVTNRDAvHKyPSFcIPGTGAFVAGIEACSEREALEMGKPNPLVLEPFIKAEGLRTERTLMIGDCLKID 266
Cdd:PRK10444 130 YFVANG--ARFIATNPDT-HG-RGF-YPACGALCAGIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTD 204

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 939619903 267 VGFASNCGMLSLLVGTGrYNNLSDVrlekDRLP-QPDFYLPRLGDL 311
Cdd:PRK10444 205 ILAGFQAGLETILVLSG-VSTLDDI----DSMPfRPSWIYPSVADI 245
Hydrolase_like pfam13242
HAD-hyrolase-like;
234-311 1.72e-11

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 59.17  E-value: 1.72e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939619903  234 MGKPNPLVLEPFIKAEGLRTERTLMIGDCLKIDVGFASNCGMLSLLVGTGRYNNlSDVRLEKDRlpqPDFYLPRLGDL 311
Cdd:pfam13242   2 CGKPNPGMLERALARLGLDPERTVMIGDRLDTDILGAREAGARTILVLTGVTRP-ADLEKAPIR---PDYVVDDLAEA 75
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
235-315 7.79e-08

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 51.85  E-value: 7.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 235 GKPNPLVLEPFIKAEGLRTERTLMIGDcLKIDVGFASNCGMLSLLVGTGrYNNLSDVRLEkdrlpQPDFYLPRLGDLLNI 314
Cdd:COG0546  139 AKPKPEPLLEALERLGLDPEEVLMVGD-SPHDIEAARAAGVPFIGVTWG-YGSAEELEAA-----GADYVIDSLAELLAL 211


                 .
gi 939619903 315 L 315
Cdd:COG0546  212 L 212
HAD_like cd07525
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 25-306 3.98e-06

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: 47.32  E-value: 3.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  25 DTVLCDGDGTIWQDDTAIAGAPDVVNALQDRfDKKVYLITNNGlKTRQELFERSQRLGFHLPSDRHIISPTAAIADYLVG 104
Cdd:cd07525    1 DAFLLDLWGVLHDGNEPYPGAVEALAALRAA-GKTVVLVTNAP-RPAESVVRQLAKLGVPPSTYDAIITSGEVTRELLAR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 105 SPKFDRtrhKVYVVGNAaiaRELR-QRGIDSYGAGgtdelppgdkwpdfvtrefgNPEAAKDVGAVVVGWDEYFS---YC 180
Cdd:cd07525   79 EAGLGR---KVYHLGPE---RDANvLEGLDVVATD--------------------DAEKAEFILCTGLYDDETETpedYR 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 181 KM-----ARACHILCSNPDaafLVTNRdavHKYPSFCIpgtGAFVAGIEACSErEALEMGKPNPLVLEPFIK-AEGLRTE 254
Cdd:cd07525  133 KLlkaaaARGLPLICANPD---LVVPR---GGKLIYCA---GALAELYEELGG-EVIYFGKPHPPIYDLALArLGRPAKA 202

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 939619903 255 RTLMIGDCLKIDVGFASNCGMLSLLVGTGrYNNLSDVRLEKDRLPQPDFYLP 306
Cdd:cd07525  203 RILAVGDGLHTDILGANAAGLDSLFVTGG-IHRRLAAEAGIKSQIVPDFVIP 253
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 230-315 8.63e-06

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


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 45.79  E-value: 8.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 230 EALEMGKPNPLVLEPFIKAEGLRTERTLMIGDCLKIDVGFASNCGMLSLLVGtgrynnlsDVRLEKDRLPQPDFYLPRLG 309
Cdd:COG1011  143 EEVGVRKPDPEIFELALERLGVPPEEALFVGDSPETDVAGARAAGMRTVWVN--------RSGEPAPAEPRPDYVISDLA 214


                 ....*.
gi 939619903 310 DLLNIL 315
Cdd:COG1011  215 ELLELL 220
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 224-284 3.47e-04

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: 40.46  E-value: 3.47e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939619903 224 EACSERealemgKPNPLVLEPFIKAEGLRTERTLMIGDCLKiDVGFASNCGMLSLLVGTGR 284
Cdd:COG0241   96 DNCDCR------KPKPGMLLQAAERLGIDLSNSYMIGDRLS-DLQAAKAAGCKGILVLTGK 149
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 236-314 5.53e-04

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


Pssm-ID: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 40.34  E-value: 5.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903 236 KPNPlvlEPFIKAE---GLRTERTLMIGDClKIDVGFASNCGMLSLLVGTGRynnlsdVRLEKDRLPQPDFYLPRLGDLL 312
Cdd:cd02616  136 KPDP---EPVLKALellGAEPEEALMVGDS-PHDILAGKNAGVKTVGVTWGY------KGREYLKAFNPDFIIDKMSDLL 205


                 ..
gi 939619903 313 NI 314
Cdd:cd02616  206 TI 207
CECR5 TIGR01456
HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member ...
 187-302 7.05e-04

HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all eukaryotes. One sequence (GP|13344995) is called "Cat Eye Syndrome critical region protein 5" (CECR5). This gene has been cloned from a pericentromere region of human chromosome 22 believed to be the location of the gene or genes responsible for Cat Eye Syndrome. This is one of a number of candidate genes. The Schizosaccharomyces pombe sequence (EGAD|138276) is annotated as "phosphatidyl synthase," however this is due entirely to a C-terminal region of the protein (outside the region of similarity of this model) which is highly homologous to a family of CDP-alcohol phosphatidyltransferases. (Thus, the annotation of GP|4226073 from C. elegans as similar to phosphatidyl synthase, is a mistake as this gene does not contain the C-terminal portion). The physical connection of the phosphatidyl synthase and the HAD-superfamily hydrolase domain in S. pombe may, however, be an important clue to the substrate for the hydrolases in this equivalog.


Pssm-ID: 200106 [Multi-domain]  Cd Length: 321  Bit Score: 40.63  E-value: 7.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  187 HILCSNPDAAFLvtnrdAVHKYPSFcipGTGAFVAGIEACSER---EALE---MGKPNPLVlepFIKAEGLRTE------ 254
Cdd:TIGR01456 186 PIYFSNQDLLWA-----NEYKLNRF---GQGAFRLLLERIYLElngKPLQyytLGKPTKLT---YDFAEDVLIDwekrls 254

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 939619903  255 ---------RTL-MIGDCLKIDVGFASNCGMLSLLVGTGRYNNLSDVRLEKDRLPQPD 302
Cdd:TIGR01456 255 gtkpstspfHALyMVGDNPASDIIGAQNYGWFSCLVKTGVYNGGDDLKECKPTLIVND 312
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 235-292 5.00e-03

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


Pssm-ID: 319835 [Multi-domain]  Cd Length: 207  Bit Score: 37.38  E-value: 5.00e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 939619903 235 GKPNPLVLEPFIKAEGLRTERTLMIGDClKIDVGFASNCGMLSLLVGTGrYNNLSDVR 292
Cdd:cd07533  138 SKPHPEMLREILAELGVDPSRAVMVGDT-AYDMQMAANAGAHAVGVAWG-YHSLEDLR 193
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 155-274 5.63e-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: 37.18  E-value: 5.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619903  155 REFGNPEAAKDVGAVVVGWDEYFSYCKMARACHILCSNPDAAFLVTNRDAVHkyPSFCIPGTGAFVAgIEACSEREALEM 234
Cdd:pfam00702  76 EAEGLTVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEA--AEALLRLLGLDDY-FDVVISGDDVGV 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 939619903  235 GKPNPLVLEPFIKAEGLRTERTLMIGDCLKiDVGFASNCG 274
Cdd:pfam00702 153 GKPKPEIYLAALERLGVKPEEVLMVGDGVN-DIPAAKAAG 191
 
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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