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Conserved domains on  [gi|392926599|ref|NP_509345|]
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Phosphoglycolate phosphatase [Caenorhabditis elegans]

Protein Classification

HAD family hydrolase( domain architecture ID 11425524)

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

CATH:  3.30.1240.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  16889794|7966317

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
50-279 1.81e-31

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


:

Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 116.18  E-value: 1.81e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599  50 LVIFDKDGTLLCFHTMWIPWIQHTAQsiETSTGLVLFPKIAQSLGLCLAEnkvkpgLLAEGTTGQIANEISSLLmdngiK 129
Cdd:COG0546    3 LVLFDLDGTLVDSAPDIAAALNEALA--ELGLPPLDLEELRALIGLGLRE------LLRRLLGEDPDEELEELL-----A 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599 130 SFEAReitnnsltnsYDKILsTDLVKELADTVALFTRLKQHGTKIAVCTADNRKSSLLALKRMNVDHLVDMIVCGDDkNT 209
Cdd:COG0546   70 RFREL----------YEEEL-LDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDD-VP 137

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392926599 210 APKPSPHNAIKICKHLGVDQSKAIMVGDTRVDMEMAHNAELgAAVGVLSGIGCKDHL--HRADVLLEHIGHL 279
Cdd:COG0546  138 PAKPKPEPLLEALERLGLDPEEVLMVGDSPHDIEAARAAGV-PFIGVTWGYGSAEELeaAGADYVIDSLAEL 208
 
Name Accession Description Interval E-value
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
50-279 1.81e-31

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 116.18  E-value: 1.81e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599  50 LVIFDKDGTLLCFHTMWIPWIQHTAQsiETSTGLVLFPKIAQSLGLCLAEnkvkpgLLAEGTTGQIANEISSLLmdngiK 129
Cdd:COG0546    3 LVLFDLDGTLVDSAPDIAAALNEALA--ELGLPPLDLEELRALIGLGLRE------LLRRLLGEDPDEELEELL-----A 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599 130 SFEAReitnnsltnsYDKILsTDLVKELADTVALFTRLKQHGTKIAVCTADNRKSSLLALKRMNVDHLVDMIVCGDDkNT 209
Cdd:COG0546   70 RFREL----------YEEEL-LDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDD-VP 137

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392926599 210 APKPSPHNAIKICKHLGVDQSKAIMVGDTRVDMEMAHNAELgAAVGVLSGIGCKDHL--HRADVLLEHIGHL 279
Cdd:COG0546  138 PAKPKPEPLLEALERLGLDPEEVLMVGDSPHDIEAARAAGV-PFIGVTWGYGSAEELeaAGADYVIDSLAEL 208
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 50-248 2.59e-19

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: 83.40  E-value: 2.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599   50 LVIFDKDGTLLCFHTmwipwiQHTAQSIETSTGLVLFPKIAqslglcLAENKVKPGLLAEGTTGQIANE--ISSLLMDNG 127
Cdd:pfam00702   3 AVVFDLDGTLTDGEP------VVTEAIAELASEHPLAKAIV------AAAEDLPIPVEDFTARLLLGKRdwLEELDILRG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599  128 IKSFEAREITNNSLTNSYDKILSTDLVKELADTVALFTRLKQHGTKIAVCTADNRKSSLLALKRMNVDHLVDMIVCGDDk 207
Cdd:pfam00702  71 LVETLEAEGLTVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDD- 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 392926599  208 NTAPKPSPHNAIKICKHLGVDQSKAIMVGDTRVDMEMAHNA 248
Cdd:pfam00702 150 VGVGKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAA 190
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 50-281 1.78e-18

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: 81.56  E-value: 1.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599  50 LVIFDKDGTLlcfhtmwipwiqhtaqsIETSTGLVL-FPKIAQSLGLC-LAENKVKPgllaegTTGQIANEISSLLMdnG 127
Cdd:cd02616    3 TILFDLDGTL-----------------IDTNELIIKsFNHTLKEYGLEgYTREEVLP------FIGPPLRETFEKID--P 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599 128 IKSFEAREItnnsLTNSYDKILStDLVKELADTVALFTRLKQHGTKIAVCTADNRKSSLLALKRMNVDHLVDMIVCGDDK 207
Cdd:cd02616   58 DKLEDMVEE----FRKYYREHND-DLTKEYPGVYETLARLKSQGIKLGVVTTKLRETALKGLKLLGLDKYFDVIVGGDDV 132

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392926599 208 nTAPKPSPHNAIKICKHLGVDQSKAIMVGDTRVDMEMAHNAELgAAVGVLSGIGCKDHL--HRADVLLEHIGHLVN 281
Cdd:cd02616  133 -THHKPDPEPVLKALELLGAEPEEALMVGDSPHDILAGKNAGV-KTVGVTWGYKGREYLkaFNPDFIIDKMSDLLT 206
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
45-248 8.92e-13

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 65.99  E-value: 8.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599  45 HESPSLVIFDKDGTLLcfhtmwipwiqHTAqsietstglvlfPKIAQSLGLCLAEnkvkpgL-LAEGTTGQIANEISsll 123
Cdd:PRK13222   3 FMDIRAVAFDLDGTLV-----------DSA------------PDLAAAVNAALAA------LgLPPAGEERVRTWVG--- 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599 124 mdNGIKSFEAREITNNSltnsydKILSTDLVKEL--------ADTVALFTR-----------LKQHGTKIAVCTadNRKS 184
Cdd:PRK13222  51 --NGADVLVERALTWAG------REPDEELLEKLrelfdrhyAENVAGGSRlypgvketlaaLKAAGYPLAVVT--NKPT 120

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392926599 185 SLLA--LKRMNVDHLVDMIVCGDDKnTAPKPSPHNAIKICKHLGVDQSKAIMVGDTRVDMEMAHNA 248
Cdd:PRK13222 121 PFVAplLEALGIADYFSVVIGGDSL-PNKKPDPAPLLLACEKLGLDPEEMLFVGDSRNDIQAARAA 185
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 50-248 9.98e-09

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


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 53.55  E-value: 9.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599   50 LVIFDKDGTLLcfhtmwipwiqHTAQSIETstglvLFPKIAQSLGLCLAENKVkpgLLAEGttgqianeissllmdngik 129
Cdd:TIGR01549   1 AILFDIDGTLV-----------DIKFAIRR-----AFPQTFEEFGLDPASFKA---LKQAG------------------- 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599  130 SFEAREITNNsLTNSYDKILSTDLV------KELADTVALFTRLKQHGTKIAVCTADNRKSSLLALKRMNVDHLVDMIVC 203
Cdd:TIGR01549  43 GLAEEEWYRI-ATSALEELQGRFWSeydaeeAYIRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILV 121

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 392926599  204 GDDknTAPKPSPHNAIKICKHLGVDqSKAIMVGDTRVDMEMAHNA 248
Cdd:TIGR01549 122 SDE--PGSKPEPEIFLAALESLGVP-PEVLHVGDNLNDIEGARNA 163
 
Name Accession Description Interval E-value
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
50-279 1.81e-31

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 116.18  E-value: 1.81e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599  50 LVIFDKDGTLLCFHTMWIPWIQHTAQsiETSTGLVLFPKIAQSLGLCLAEnkvkpgLLAEGTTGQIANEISSLLmdngiK 129
Cdd:COG0546    3 LVLFDLDGTLVDSAPDIAAALNEALA--ELGLPPLDLEELRALIGLGLRE------LLRRLLGEDPDEELEELL-----A 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599 130 SFEAReitnnsltnsYDKILsTDLVKELADTVALFTRLKQHGTKIAVCTADNRKSSLLALKRMNVDHLVDMIVCGDDkNT 209
Cdd:COG0546   70 RFREL----------YEEEL-LDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDD-VP 137

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392926599 210 APKPSPHNAIKICKHLGVDQSKAIMVGDTRVDMEMAHNAELgAAVGVLSGIGCKDHL--HRADVLLEHIGHL 279
Cdd:COG0546  138 PAKPKPEPLLEALERLGLDPEEVLMVGDSPHDIEAARAAGV-PFIGVTWGYGSAEELeaAGADYVIDSLAEL 208
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 50-248 2.59e-19

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: 83.40  E-value: 2.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599   50 LVIFDKDGTLLCFHTmwipwiQHTAQSIETSTGLVLFPKIAqslglcLAENKVKPGLLAEGTTGQIANE--ISSLLMDNG 127
Cdd:pfam00702   3 AVVFDLDGTLTDGEP------VVTEAIAELASEHPLAKAIV------AAAEDLPIPVEDFTARLLLGKRdwLEELDILRG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599  128 IKSFEAREITNNSLTNSYDKILSTDLVKELADTVALFTRLKQHGTKIAVCTADNRKSSLLALKRMNVDHLVDMIVCGDDk 207
Cdd:pfam00702  71 LVETLEAEGLTVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDD- 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 392926599  208 NTAPKPSPHNAIKICKHLGVDQSKAIMVGDTRVDMEMAHNA 248
Cdd:pfam00702 150 VGVGKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAA 190
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
145-248 7.02e-19

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 81.86  E-value: 7.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599  145 YDKILSTDLVKELADTVALFTRLKQHGTKIAVCTADNRKSSLLALKRMNVDHLVDMIVCGDDKnTAPKPSPHNAIKICKH 224
Cdd:pfam13419  69 YNEELHDKLVKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDV-EGKKPDPDPILKALEQ 147

                          90       100
                  ....*....|....*....|....
gi 392926599  225 LGVDQSKAIMVGDTRVDMEMAHNA 248
Cdd:pfam13419 148 LGLKPEEVIYVGDSPRDIEAAKNA 171
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 50-281 1.78e-18

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: 81.56  E-value: 1.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599  50 LVIFDKDGTLlcfhtmwipwiqhtaqsIETSTGLVL-FPKIAQSLGLC-LAENKVKPgllaegTTGQIANEISSLLMdnG 127
Cdd:cd02616    3 TILFDLDGTL-----------------IDTNELIIKsFNHTLKEYGLEgYTREEVLP------FIGPPLRETFEKID--P 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599 128 IKSFEAREItnnsLTNSYDKILStDLVKELADTVALFTRLKQHGTKIAVCTADNRKSSLLALKRMNVDHLVDMIVCGDDK 207
Cdd:cd02616   58 DKLEDMVEE----FRKYYREHND-DLTKEYPGVYETLARLKSQGIKLGVVTTKLRETALKGLKLLGLDKYFDVIVGGDDV 132

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392926599 208 nTAPKPSPHNAIKICKHLGVDQSKAIMVGDTRVDMEMAHNAELgAAVGVLSGIGCKDHL--HRADVLLEHIGHLVN 281
Cdd:cd02616  133 -THHKPDPEPVLKALELLGAEPEEALMVGDSPHDILAGKNAGV-KTVGVTWGYKGREYLkaFNPDFIIDKMSDLLT 206
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
48-279 5.98e-17

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 77.17  E-value: 5.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599  48 PSLVIFDKDGTLlcFHTMWIpWIQHTAQsietstglvlfpkIAQSLGLCLAENkvkpglLAEGTTGQIANEISSLLMDNG 127
Cdd:COG0637    2 IKAVIFDMDGTL--VDSEPL-HARAWRE-------------AFAELGIDLTEE------EYRRLMGRSREDILRYLLEEY 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599 128 IKSFEAREITNnSLTNSYDKILSTDLVKELADTVALFTRLKQHGTKIAVCTADNRKSSLLALKRMNVDHLVDMIVCGDDk 207
Cdd:COG0637   60 GLDLPEEELAA-RKEELYRELLAEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDD- 137

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392926599 208 NTAPKPSP----HNAikicKHLGVDQSKAIMVGDTRVDMEMAHNAelGA-AVGVLSGIGCKDHLHRADVLLEHIGHL 279
Cdd:COG0637  138 VARGKPDPdiylLAA----ERLGVDPEECVVFEDSPAGIRAAKAA--GMrVVGVPDGGTAEEELAGADLVVDDLAEL 208
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 160-256 7.72e-17

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


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 74.35  E-value: 7.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599 160 TVALFTRLKQHGTKIAVCTADNRKSSLLALKRMNVDHLVDMIVCGDDKNTaPKPSPHNAIKICKHLGVDQSKAIMVGDTR 239
Cdd:cd01427   12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGT-PKPKPKPLLLLLLKLGVDPEEVLFVGDSE 90

                         90
                 ....*....|....*..
gi 392926599 240 VDMEMAHNAElGAAVGV 256
Cdd:cd01427   91 NDIEAARAAG-GRTVAV 106
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 167-275 4.14e-13

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: 66.65  E-value: 4.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599 167 LKQHGTKIAVCTADNRKSSLLALKRMNVDHLVDMIVCGDDknTAPKPSPHNAIKICKHLGVDQSKAIMVGDTRVDMEMAH 246
Cdd:cd07533   96 LAAQGVLLAVATGKSRRGLDRVLEQHGLGGYFDATRTADD--TPSKPHPEMLREILAELGVDPSRAVMVGDTAYDMQMAA 173

                         90       100       110
                 ....*....|....*....|....*....|.
gi 392926599 247 NAELgAAVGVLSGIGCKDHLHR--ADVLLEH 275
Cdd:cd07533  174 NAGA-HAVGVAWGYHSLEDLRSagADAVVDH 203
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
45-248 8.92e-13

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 65.99  E-value: 8.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599  45 HESPSLVIFDKDGTLLcfhtmwipwiqHTAqsietstglvlfPKIAQSLGLCLAEnkvkpgL-LAEGTTGQIANEISsll 123
Cdd:PRK13222   3 FMDIRAVAFDLDGTLV-----------DSA------------PDLAAAVNAALAA------LgLPPAGEERVRTWVG--- 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599 124 mdNGIKSFEAREITNNSltnsydKILSTDLVKEL--------ADTVALFTR-----------LKQHGTKIAVCTadNRKS 184
Cdd:PRK13222  51 --NGADVLVERALTWAG------REPDEELLEKLrelfdrhyAENVAGGSRlypgvketlaaLKAAGYPLAVVT--NKPT 120

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392926599 185 SLLA--LKRMNVDHLVDMIVCGDDKnTAPKPSPHNAIKICKHLGVDQSKAIMVGDTRVDMEMAHNA 248
Cdd:PRK13222 121 PFVAplLEALGIADYFSVVIGGDSL-PNKKPDPAPLLLACEKLGLDPEEMLFVGDSRNDIQAARAA 185
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 51-248 3.34e-12

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: 64.28  E-value: 3.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599  51 VIFDKDGTLLCFHTMWIPWIQHTAQSIEtstGLVLFPKIAQSLglclaeNKVKPGLLAEGTTGQIANE--ISSLLMDNGI 128
Cdd:COG1011    4 VLFDLDGTLLDFDPVIAEALRALAERLG---LLDEAEELAEAY------RAIEYALWRRYERGEITFAelLRRLLEELGL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599 129 KSFEAreitnnsLTNSYDKILStDLVKELADTVALFTRLKQHGTKIAVCTADNRKSSLLALKRMNVDHLVDMIVCGDDKN 208
Cdd:COG1011   75 DLAEE-------LAEAFLAALP-ELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVG 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 392926599 209 tAPKPSPhnAI--KICKHLGVDQSKAIMVGDT-RVDMEMAHNA 248
Cdd:COG1011  147 -VRKPDP--EIfeLALERLGVPPEEALFVGDSpETDVAGARAA 186
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 152-280 5.13e-11

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 60.81  E-value: 5.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599 152 DLVKELADTVALFTRLKQHGTKIAVCTADNRKSSLLALKRMNVDHLVDMIVCGDDKnTAPKPSPHNAIKICKHLGVDQSK 231
Cdd:PRK13288  79 ELVTEYETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDV-EHAKPDPEPVLKALELLGAKPEE 157

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 392926599 232 AIMVGDTRVDMEMAHNAELGAAvGVLSGIGCKDHL--HRADVLLEHIGHLV 280
Cdd:PRK13288 158 ALMVGDNHHDILAGKNAGTKTA-GVAWTIKGREYLeqYKPDFMLDKMSDLL 207
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 51-248 7.91e-11

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


Pssm-ID: 319815 [Multi-domain]  Cd Length: 214  Bit Score: 60.41  E-value: 7.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599  51 VIFDKDGTLLcfhtmwipwiqHTAqsietstglvlfPKIAQSLGLCLAENKVKPGLLAE--GTTGQIAneisSLLMDNGi 128
Cdd:cd07512    2 VIFDLDGTLI-----------DSA------------PDLHAALNAVLAAEGLAPLSLAEvrSFVGHGA----PALIRRA- 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599 129 ksFEAREITNNSLTNS--YDKILS------TDLVKELADTVALFTRLKQHGTKIAVCTADNRKSSLLALKRMNVDHLVDM 200
Cdd:cd07512   54 --FAAAGEDLDGPLHDalLARFLDhyeadpPGLTRPYPGVIEALERLRAAGWRLAICTNKPEAPARALLSALGLADLFAA 131

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 392926599 201 IVCGDdknTAP--KPSPHNAIKICKHLGVDQSKAIMVGDTRVDMEMAHNA 248
Cdd:cd07512  132 VVGGD---TLPqrKPDPAPLRAAIRRLGGDVSRALMVGDSETDAATARAA 178
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 145-256 4.03e-10

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


Pssm-ID: 319808 [Multi-domain]  Cd Length: 143  Bit Score: 56.86  E-value: 4.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599 145 YDKILSTDLVKELADTVALFTRLKQHGTKIAVCTADNRKSSLLALKRMNV-DHLVDMIVCGDDkNTAPKPSPHNAIKICK 223
Cdd:cd07505   31 LLELIASEGLKLKPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLlRGYFDVIVSGDD-VERGKPAPDIYLLAAE 109

                         90       100       110
                 ....*....|....*....|....*....|...
gi 392926599 224 HLGVDQSKAIMVGDTRVDMEMAHNAELgAAVGV 256
Cdd:cd07505  110 RLGVDPERCLVFEDSLAGIEAAKAAGM-TVVAV 141
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 50-248 9.98e-09

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


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 53.55  E-value: 9.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599   50 LVIFDKDGTLLcfhtmwipwiqHTAQSIETstglvLFPKIAQSLGLCLAENKVkpgLLAEGttgqianeissllmdngik 129
Cdd:TIGR01549   1 AILFDIDGTLV-----------DIKFAIRR-----AFPQTFEEFGLDPASFKA---LKQAG------------------- 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599  130 SFEAREITNNsLTNSYDKILSTDLV------KELADTVALFTRLKQHGTKIAVCTADNRKSSLLALKRMNVDHLVDMIVC 203
Cdd:TIGR01549  43 GLAEEEWYRI-ATSALEELQGRFWSeydaeeAYIRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILV 121

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 392926599  204 GDDknTAPKPSPHNAIKICKHLGVDqSKAIMVGDTRVDMEMAHNA 248
Cdd:TIGR01549 122 SDE--PGSKPEPEIFLAALESLGVP-PEVLHVGDNLNDIEGARNA 163
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 50-248 1.02e-08

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


Pssm-ID: 319854 [Multi-domain]  Cd Length: 212  Bit Score: 54.16  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599  50 LVIFDKDGTLLcfhtmwipwiqHTAQSIETSTGLVLfpkiaQSLGL-CLAENKVK-------PGLLAEGTTGQIANEISS 121
Cdd:cd16417    1 LVAFDLDGTLV-----------DSAPDLAEAANAML-----AALGLpPLPEETVRtwigngaDVLVERALTGAREAEPDE 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599 122 LLMDNGIKSFEAR-EITNNSLTNSYDkilstdlvkELADTVALftrLKQHGTKIAVCTADNRKSSLLALKRMNVDHLVDM 200
Cdd:cd16417   65 ELFKEARALFDRHyAETLSVHSHLYP---------GVKEGLAA---LKAQGYPLACVTNKPERFVAPLLEALGISDYFSL 132

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 392926599 201 IVCGDdknTAP--KPSPHNAIKICKHLGVDQSKAIMVGDTRVDMEMAHNA 248
Cdd:cd16417  133 VLGGD---SLPekKPDPAPLLHACEKLGIAPAQMLMVGDSRNDILAARAA 179
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 161-256 8.84e-08

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


Pssm-ID: 319857 [Multi-domain]  Cd Length: 105  Bit Score: 49.38  E-value: 8.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599 161 VALFTRLKQHGTKIAVctADNRKSsllALKRMNVDHLV----DMIVcGDDKNTAPKPSPHNAIKICKHLGVDQSKAIMVG 236
Cdd:cd16421   13 LELLKALRQKGIKLAV--LSNKPN---EAVQVLVEELFpgsfDFVL-GEKEGIRRKPDPT*ALECAKVLGVPPDEVLYVG 86

                         90       100
                 ....*....|....*....|
gi 392926599 237 DTRVDMEMAHNAELgAAVGV 256
Cdd:cd16421   87 DSGVDMQTARNAGM-DEIGV 105
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 157-248 1.38e-06

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


Pssm-ID: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 46.00  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599 157 LADTVALFTRLKqHGTKIAVCTADNRKSSLLALKRMNVDHLVDMIVCGDDKNTApKPSPHNAIKICKHLGVDQSKAIMVG 236
Cdd:cd04305   11 LPGAKELLEELK-KGYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQ-KPNPEIFDYALNQLGVKPEETLMVG 88

                         90
                 ....*....|...
gi 392926599 237 DT-RVDMEMAHNA 248
Cdd:cd04305   89 DSlESDILGAKNA 101
PRK13478 PRK13478
phosphonoacetaldehyde hydrolase; Provisional
 151-259 5.22e-06

phosphonoacetaldehyde hydrolase; Provisional


Pssm-ID: 184075 [Multi-domain]  Cd Length: 267  Bit Score: 46.78  E-value: 5.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599 151 TDLVKELADTVAlftRLKQHGTKIAVCTADNRKSsllalkrMNVdhLV----------DMIVCGDDKnTAPKPSPHNAIK 220
Cdd:PRK13478 100 ATPIPGVLEVIA---ALRARGIKIGSTTGYTREM-------MDV--VVplaaaqgyrpDHVVTTDDV-PAGRPYPWMALK 166

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 392926599 221 ICKHLGVDQSKAIM-VGDTRVDMEMAHNAelGA-AVGV-LSG 259
Cdd:PRK13478 167 NAIELGVYDVAACVkVDDTVPGIEEGLNA--GMwTVGViLSG 206
Hydrolase_like pfam13242
HAD-hyrolase-like;
212-279 5.25e-06

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 43.37  E-value: 5.25e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392926599  212 KPSPHNAIKICKHLGVDQSKAIMVGDT-RVDMEMAHNAELgAAVGVLSGIGCKDHL----HRADVLLEHIGHL 279
Cdd:pfam13242   4 KPNPGMLERALARLGLDPERTVMIGDRlDTDILGAREAGA-RTILVLTGVTRPADLekapIRPDYVVDDLAEA 75
HAD-SF-IA-hyp1 TIGR01548
haloacid dehalogenase superfamily, subfamily IA hydrolase, TIGR01548; This model represents a ...
 167-248 7.85e-06

haloacid dehalogenase superfamily, subfamily IA hydrolase, TIGR01548; This model represents a small and phylogenetically curious clade of sequences. Sequences are found from Halobacterium (an archaeon), Nostoc and Synechococcus (cyanobacteria) and Phytophthora (a stramenophile eukaryote). These appear to be members of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases by general homology and the conservation of all of the recognized catalytic motifs. The variable domain is found in between motifs 1 and 2, indicating membership in subfamily I and phylogeny and prediction of the alpha helical nature of the variable domain (by PSI-PRED) indicate membership in subfamily IA. All but the Halobacterium sequence currently found are annotated as "Imidazoleglycerol-phosphate dehydratase", however, the source of the annotation could not be traced and significant homology could not be found between any of these sequences and known IGPD's.


Pssm-ID: 273685  Cd Length: 197  Bit Score: 45.69  E-value: 7.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599  167 LKQHGTKIAVCTADNRKSSLLALKRMNVDHLVDMIVCGDDknTAPKPSPHNAIKICKHLGVDQSKAIMVGDTRVDMEMAH 246
Cdd:TIGR01548 118 LHRAPKGMAVVTGRPRKDAAKFLTTHGLEILFPVQIWMED--CPPKPNPEPLILAAKALGVEACHAAMVGDTVDDIITGR 195


                  ..
gi 392926599  247 NA 248
Cdd:TIGR01548 196 KA 197
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 145-239 1.66e-05

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


Pssm-ID: 319859 [Multi-domain]  Cd Length: 169  Bit Score: 44.17  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599 145 YDKILSTDLVKELADTV-ALFTRLKQHGTKIAVCTADNRKSSLLALKRMNVDHLVDMIVCGDDKnTAPKPSPHNAIKICK 223
Cdd:cd16423   33 IKRQFSEKTDLPPIEGVkELLEFLKEKGIKLAVASSSPRRWIEPHLERLGLLDYFEVIVTGDDV-EKSKPDPDLYLEAAE 111

                         90
                 ....*....|....*.
gi 392926599 224 HLGVDQSKAIMVGDTR 239
Cdd:cd16423  112 RLGVNPEECVVIEDSR 127
Histidinol-ppas TIGR01656
histidinol-phosphate phosphatase family domain; This domain is found in authentic ...
 211-259 3.59e-05

histidinol-phosphate phosphatase family domain; This domain is found in authentic histidinol-phosphate phosphatases which are sometimes found as stand-alone entities and sometimes as fusions with imidazoleglycerol-phosphate dehydratase (TIGR01261). Additionally, a family of proteins including YaeD from E. coli (TIGR00213) and various other proteins are closely related but may not have the same substrate specificity. This domain is a member of the haloacid-dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. This superfamily is distinguished by the presence of three motifs: an N-terminal motif containing the nucleophilic aspartate, a central motif containing an conserved serine or threonine, and a C-terminal motif containing a conserved lysine (or arginine) and conserved aspartates. More specifically, the domian modelled here is a member of subfamily III of the HAD-superfamily by virtue of lacking a "capping" domain in either of the two common positions, between motifs 1 and 2, or between motifs 2 and 3.


Pssm-ID: 273737  Cd Length: 147  Bit Score: 42.77  E-value: 3.59e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 392926599  211 PKPSPHNAIKICKHLGVDQSKAIMVGDTRVDMEMAHNAELgAAVGVLSG 259
Cdd:TIGR01656 100 RKPKPGLILEALKRLGVDASRSLVVGDRLRDLQAARNAGA-AAGLLVSG 147
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 51-248 3.87e-05

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


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 43.18  E-value: 3.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599   51 VIFDKDGTLLC---FHTMWIpwiqhtAQSIETSTGLVLFPKIAQSLGLCLAENKVKPGLLAEGTTGQIaneissllmdng 127
Cdd:TIGR01509   2 ILFDLDGVLVDtefAIAKLI------NREELGLVPDELGVSAVGRLELALRRFKAQYGRTISPEDAQL------------ 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599  128 iksFEAREItnnsltnsYDKILSTDLVKELADTVALFTRLKQHGTKIAVCTADNRKSSLLALKRMNVDHLvDMIVCGDDK 207
Cdd:TIGR01509  64 ---LYKQLF--------YEQIEEEAKLKPLPGVRALLEALRARGKKLALLTNSPRAHKLVLALLGLRDLF-DVVIDSSDV 131

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 392926599  208 nTAPKPSPHNAIKICKHLGVDQSKAIMVGDTRVDMEMAHNA 248
Cdd:TIGR01509 132 -GLGKPDPDIYLQALKALGLEPSECVFVDDSPAGIEAAKAA 171
HAD_PHN cd02586
Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; ...
 151-259 5.14e-05

Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; Degradation of the ubiquitous natural phosphonate 2-aminoethylphosphonate (AEP) into useable forms of nitrogen, carbon, and phosphorus is a two-step metabolic pathway. The first step, catalyzed by AEP transaminase, involves the transfer of NH3 from AEP to pyruvate, yielding phosphonoacetaldehyde (P-Ald) and alanine. In the second step, phosphonatase catalyzes the hydrolytic P-C bond cleavage of P-Ald to form orthophosphate and acetaldehyde. 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: 319785 [Multi-domain]  Cd Length: 242  Bit Score: 43.44  E-value: 5.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599 151 TDLVKELADTVAlftRLKQHGTKIAVCTADNRKSSLLALKRMNVD-HLVDMIVCGDDKnTAPKPSPHNAIKICKHLGVDQ 229
Cdd:cd02586   97 SSPIPGVLEVIA---KLRARGIKIGSTTGYTREMMDIVLPEAAAQgYRPDSLVTPDDV-PAGRPYPWMCYKNAIELGVYD 172

                         90       100       110
                 ....*....|....*....|....*....|..
gi 392926599 230 SKAIM-VGDTRVDMEMAHNAelGA-AVGVLSG 259
Cdd:cd02586  173 VAAVVkVGDTVPDIKEGLNA--GMwTVGVILS 202
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
212-279 7.81e-05

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 43.17  E-value: 7.81e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392926599 212 KPSPhnAI--KICKHLGVDQSKAIMVGDT-RVDMEMAHNAELGAAVgVLSGIGCKDHLHRADV----LLEHIGHL 279
Cdd:COG0647  186 KPSP--PIyeLALERLGVDPERVLMVGDRlDTDILGANAAGLDTLL-VLTGVTTAEDLEAAPIrpdyVLDSLAEL 257
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 163-279 7.82e-05

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; 5'-nucleotidases dephosphorylate nucleoside 5'-monophosphates to nucleosides and inorganic phosphate. Purified Pseudomonas aeruginosa PA0065 displayed high activity toward 5'-UMP and 5'-IMP, significant activity against 5'-XMP and 5'-TMP, and low activity against 5'-CMP. 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: 319798 [Multi-domain]  Cd Length: 209  Bit Score: 42.96  E-value: 7.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599 163 LFTRLKQHGTKIAVCTADNRKSSLLALKRMNVDHLVDMIVCGDDKNTAPKPSPHnaIKIC-KHLGVDQSKAIMVGDTRVD 241
Cdd:cd04302   89 LLEKLKAAGYRLYVATSKPEVFARRILEHFGLDEYFDGIAGASLDGSRVHKADV--IRYAlDTLGIAPEQAVMIGDRKHD 166

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 392926599 242 MEMAHNAELgAAVGVLSGIGCKDHL--HRADVLLEHIGHL 279
Cdd:cd04302  167 IIGARANGI-DSIGVLYGYGSEDELeeAGATYIVETPAEL 205
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 212-259 3.72e-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: 3.72e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 392926599 212 KPSPHNAIKICKHLGVDQSKAIMVGDTRVDMEMAHNAelGA-AVGVLSG 259
Cdd:COG0241  102 KPKPGMLLQAAERLGIDLSNSYMIGDRLSDLQAAKAA--GCkGILVLTG 148
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 212-248 1.31e-03

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


Pssm-ID: 319806 [Multi-domain]  Cd Length: 142  Bit Score: 38.28  E-value: 1.31e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 392926599 212 KPSPHNAIKICKHLGVDQSKAIMVGDTRVDMEMAHNA 248
Cdd:cd07503   99 KPKPGMLLDAAKELGIDLARSFVIGDRLSDIQAARNA 135
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 145-255 1.37e-03

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 38.96  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599 145 YDKILSTDLVKELADtvalftRLKQHGTKIAVCTADNrkssllalkrmnvDHLVDMIVCGDDKNTApkpsphnAIKICKH 224
Cdd:COG0561   79 YERPLDPEDVREILE------LLREHGLHLQVVVRSG-------------PGFLEILPKGVSKGSA-------LKKLAER 132

                         90       100       110
                 ....*....|....*....|....*....|.
gi 392926599 225 LGVDQSKAIMVGDTRVDMEMAHNAELGAAVG 255
Cdd:COG0561  133 LGIPPEEVIAFGDSGNDLEMLEAAGLGVAMG 163
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 158-248 2.07e-03

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


Pssm-ID: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 38.40  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599 158 ADTVALFTRLKQHGTKIAVCTADNRKSSLLALKRMNVDHLVDMIVCGDDKNTApKPSPHNAIKICKHLGVDQSKAIMVGD 237
Cdd:cd02588   94 PDVVAGLRRLREAGYRLAILSNGSPDLIEDVVANAGLRDLFDAVLSAEDVRAY-KPAPAVYELAAERLGVPPDEILHVAS 172

                         90
                 ....*....|.
gi 392926599 238 TRVDMEMAHNA 248
Cdd:cd02588  173 HAWDLAGARAL 183
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 139-257 4.16e-03

HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class III subfamilies are characterized by the lack of any domains located between either between the first and second conserved catalytic motifs (as in the Class I subfamilies, TIGR01493, TIGR01509, TIGR01488 and TIGR01494) or between the second and third conserved catalytic motifs (as in the Class II subfamilies, TIGR01460 and TIGR01484) of the superfamily domain. The IIIA subfamily contains five major clades: histidinol-phosphatase (TIGR01261) and histidinol-phosphatase-related protein (TIGR00213) which together form a subfamily (TIGR01656), DNA 3'-phosphatase (TIGR01663, TIGR01664), YqeG (TIGR01668) and YrbI (TIGR01670). In the case of histidinol phosphatase and PNK-3'-phosphatase, this model represents a domain of a bifunctional system. In the histidinol phosphatase HisB, a C-terminal domain is an imidazoleglycerol-phosphate dehydratase which catalyzes a related step in histidine biosynthesis. In PNK-3'-phosphatase, N- and C-terminal domains constitute the polynucleotide kinase and DNA-binding components of the enzyme. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273742 [Multi-domain]  Cd Length: 135  Bit Score: 36.61  E-value: 4.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599  139 NSLTNSYDKILSTDLVKELADTVALFTRLKQHGTKIAVCT----ADNRKSSLLALKRMN-----VDHLVDM-IVCGDDKn 208
Cdd:TIGR01662   9 GTLTDDVPYVSDEDERILYPEVPDALAELKEAGYKVVIVTnqsgIGRGYFSRSFSGRVArrleeLGVPIDIlYACPGCR- 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 392926599  209 tapKPSPHNAIKICKHL-GVDQSKAIMVGDTR-VDMEMAHNAelGAAVGVL 257
Cdd:TIGR01662  88 ---KPKPGMFLEALKRFnEIDPEESVYVGDQDlTDLQAAKRV--GLATILV 133
HAD pfam12710
haloacid dehalogenase-like hydrolase;
51-246 4.98e-03

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 37.13  E-value: 4.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599   51 VIFDKDGTLLCFHTMWiPWIQHTAQSIETSTGLVLFPKIAQSLGLCLAENKVKpgllaegttgQIANEISSLLMDngiks 130
Cdd:pfam12710   1 ALFDLDGTLLDGDSLF-LLIRALLRRGGPDLWRALLVLLLLALLRLLGRLSRA----------GARELLRALLAG----- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926599  131 feAREITNNSLTNSYDKILSTDLVKELADTVAlftRLKQHGTKIAVCTADNRKSSLLALKRMNVDHLV-------DMIVC 203
Cdd:pfam12710  65 --LPEEDAAELERFVAEVALPRLHPGALELLA---AHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLatelevdDGRFT 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 392926599  204 GDDKNTAP------KPSPHNAIKICKHLGVDQSKAIMVGDTRVDMEMAH 246
Cdd:pfam12710 140 GELRLIGPpcagegKVRRLRAWLAARGLGLDLADSVAYGDSPSDLPMLR 188
 
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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