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Conserved domains on  [gi|1872276187|ref|WP_180167884|]
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HAD family phosphatase [Acinetobacter sp. YH12035]

Protein Classification

HAD family hydrolase( domain architecture ID 10001729)

haloacid dehalogenase (HAD) family hydrolase uses a nucleophilic aspartate in the phosphoryl transfer reaction; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

CATH:  3.30.1240.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  16889794|15337123|33940035|37786806
SCOP:  3001890

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-214 2.50e-77

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


:

Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 231.65  E-value: 2.50e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872276187   1 MKLALFDLDHTLLNTDSDHSWGEFLVNEGLVDPVHHRAMNDKFYEDYKKGQLDPYAYNEFVFQFLTQHDHDYLTELHQLF 80
Cdd:COG0560     3 MRLAVFDLDGTLIAGESIDELARFLGRRGLVDRREVLEEVAAITERAMAGELDFEESLRFRVALLAGLPEEELEELAERL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872276187  81 MQKVirPQMRPEGFKAIQCHKDAGHEIVGITATSDFITAPIFREFGITEIIATNAEVVDGKYTGKVTNIACYQQGKLTRL 160
Cdd:COG0560    83 FEEV--PRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDGRLTGEVVGPIVDGEGKAEAL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1872276187 161 EQWLA--GRDVTESWAYSDSINDRFLLEHADHAIAVNPDDRLEALA-KEQGWEIQDW 214
Cdd:COG0560   161 RELAAelGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREAAdRERGWPVLDL 217
 
Name Accession Description Interval E-value
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-214 2.50e-77

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 231.65  E-value: 2.50e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872276187   1 MKLALFDLDHTLLNTDSDHSWGEFLVNEGLVDPVHHRAMNDKFYEDYKKGQLDPYAYNEFVFQFLTQHDHDYLTELHQLF 80
Cdd:COG0560     3 MRLAVFDLDGTLIAGESIDELARFLGRRGLVDRREVLEEVAAITERAMAGELDFEESLRFRVALLAGLPEEELEELAERL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872276187  81 MQKVirPQMRPEGFKAIQCHKDAGHEIVGITATSDFITAPIFREFGITEIIATNAEVVDGKYTGKVTNIACYQQGKLTRL 160
Cdd:COG0560    83 FEEV--PRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDGRLTGEVVGPIVDGEGKAEAL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1872276187 161 EQWLA--GRDVTESWAYSDSINDRFLLEHADHAIAVNPDDRLEALA-KEQGWEIQDW 214
Cdd:COG0560   161 RELAAelGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREAAdRERGWPVLDL 217
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 3-197 2.05e-51

phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). 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: 319796 [Multi-domain]  Cd Length: 195  Bit Score: 164.79  E-value: 2.05e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872276187   3 LALFDLDHTLLNTDSdhsWGEFLVNEGLV--DPVHHRAMNDKFYEDYKKGQLDpYAYNEFVFQFLTQHDHDYLTELHQLF 80
Cdd:cd02612     1 LAFFDLDGTLIAGDS---FFAFLRFKGIAerRAPLEELLLLRLMALYALGRLD-GAGMEALLGFATAGLAGELAALVEEF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872276187  81 MQKVIRPQMRPEGFKAIQCHKDAGHEIVGITATSDFITAPIFREFGITEIIATNAEVVDGKYTGKVTNIACYQQGKLTRL 160
Cdd:cd02612    77 VEEYILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDNVLGTQLETEDGRYTGRIIGPPCYGEGKVKRL 156

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1872276187 161 EQWLAGRDVT--ESWAYSDSINDRFLLEHADHAIAVNPD 197
Cdd:cd02612   157 REWLAEEGIDlkDSYAYSDSINDLPMLEAVGHPVAVNPD 195
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 3-200 3.14e-37

HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences modelled here are all bacterial. The IB subfamily includes the enzyme phosphoserine phosphatase (TIGR00338). Due to this relationship, several of these sequences have been annotated as "phosphoserine phosphatase related proteins," or "Phosphoserine phosphatase-family enzymes." There is presently no evidence that any of the enzymes in this model possess PSPase activity. OMNI|NTL01ML1250 is annotated as a "possible transferase," however this is due to the C-terminal domain found on this sequence which is homologous to a group of glycerol-phosphate acyltransferases (between trusted and noise to TIGR00530). A subset of these sequences including OMNI|CC1962, the Caulobacter crescentus CicA protein cluster together and may represent a separate equivalog. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273654 [Multi-domain]  Cd Length: 202  Bit Score: 128.61  E-value: 3.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872276187   3 LALFDLDHTLLNTDSDHSWGEFLVNEGLVDPVHHRAMNDKFYEDYK-KGQLDPYAYNEFVFQFLTQHDHDYLTELHQLFM 81
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLASKNILFEELRLPKVLARFEFFLnRGLDYMAYYRAFALDALAGLLEEDVRAIVEEFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872276187  82 QKVIRPQMRPEGFKAIQCHKDAGHEIVGITATSDFITAPIFREFGITEIIATNAEVV-DGKYTGKVTNIACYQQGKLTRL 160
Cdd:TIGR01490  81 NQKIESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTRLEESeDGIYTGNIDGNNCKGEGKVHAL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1872276187 161 EQWLA--GRDVTESWAYSDSINDRFLLEHADHAIAVNPDDRL 200
Cdd:TIGR01490 161 AELLAeeQIDLKDSYAYGDSISDLPLLSLVGHPYVVNPDKKL 202
HAD pfam12710
haloacid dehalogenase-like hydrolase;
4-186 6.83e-36

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 124.95  E-value: 6.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872276187   4 ALFDLDHTLLNTDSDHSWGEFLVNEGLVDPVHHRAMNDKFYEDYKKGQLDPYAYNEFVFQFLTQHDhDYLTELHQLFMQK 83
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALLRRGGPDLWRALLVLLLLALLRLLGRLSRAGARELLRALLAGLP-EEDAAELERFVAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872276187  84 VIRPQMRPEGFKAIQCHKDAGHEIVGITATSDFITAPIFREFGITEIIATNAEVVDGKYTGKVTNIA--CYQQGKLTRLE 161
Cdd:pfam12710  80 VALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATELEVDDGRFTGELRLIGppCAGEGKVRRLR 159

                         170       180
                  ....*....|....*....|....*....
gi 1872276187 162 QWLAGR----DVTESWAYSDSINDRFLLE 186
Cdd:pfam12710 160 AWLAARglglDLADSVAYGDSPSDLPMLR 188
 
Name Accession Description Interval E-value
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-214 2.50e-77

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 231.65  E-value: 2.50e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872276187   1 MKLALFDLDHTLLNTDSDHSWGEFLVNEGLVDPVHHRAMNDKFYEDYKKGQLDPYAYNEFVFQFLTQHDHDYLTELHQLF 80
Cdd:COG0560     3 MRLAVFDLDGTLIAGESIDELARFLGRRGLVDRREVLEEVAAITERAMAGELDFEESLRFRVALLAGLPEEELEELAERL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872276187  81 MQKVirPQMRPEGFKAIQCHKDAGHEIVGITATSDFITAPIFREFGITEIIATNAEVVDGKYTGKVTNIACYQQGKLTRL 160
Cdd:COG0560    83 FEEV--PRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDGRLTGEVVGPIVDGEGKAEAL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1872276187 161 EQWLA--GRDVTESWAYSDSINDRFLLEHADHAIAVNPDDRLEALA-KEQGWEIQDW 214
Cdd:COG0560   161 RELAAelGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREAAdRERGWPVLDL 217
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 3-197 2.05e-51

phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). 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: 319796 [Multi-domain]  Cd Length: 195  Bit Score: 164.79  E-value: 2.05e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872276187   3 LALFDLDHTLLNTDSdhsWGEFLVNEGLV--DPVHHRAMNDKFYEDYKKGQLDpYAYNEFVFQFLTQHDHDYLTELHQLF 80
Cdd:cd02612     1 LAFFDLDGTLIAGDS---FFAFLRFKGIAerRAPLEELLLLRLMALYALGRLD-GAGMEALLGFATAGLAGELAALVEEF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872276187  81 MQKVIRPQMRPEGFKAIQCHKDAGHEIVGITATSDFITAPIFREFGITEIIATNAEVVDGKYTGKVTNIACYQQGKLTRL 160
Cdd:cd02612    77 VEEYILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDNVLGTQLETEDGRYTGRIIGPPCYGEGKVKRL 156

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1872276187 161 EQWLAGRDVT--ESWAYSDSINDRFLLEHADHAIAVNPD 197
Cdd:cd02612   157 REWLAEEGIDlkDSYAYSDSINDLPMLEAVGHPVAVNPD 195
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 3-200 3.14e-37

HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences modelled here are all bacterial. The IB subfamily includes the enzyme phosphoserine phosphatase (TIGR00338). Due to this relationship, several of these sequences have been annotated as "phosphoserine phosphatase related proteins," or "Phosphoserine phosphatase-family enzymes." There is presently no evidence that any of the enzymes in this model possess PSPase activity. OMNI|NTL01ML1250 is annotated as a "possible transferase," however this is due to the C-terminal domain found on this sequence which is homologous to a group of glycerol-phosphate acyltransferases (between trusted and noise to TIGR00530). A subset of these sequences including OMNI|CC1962, the Caulobacter crescentus CicA protein cluster together and may represent a separate equivalog. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273654 [Multi-domain]  Cd Length: 202  Bit Score: 128.61  E-value: 3.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872276187   3 LALFDLDHTLLNTDSDHSWGEFLVNEGLVDPVHHRAMNDKFYEDYK-KGQLDPYAYNEFVFQFLTQHDHDYLTELHQLFM 81
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLASKNILFEELRLPKVLARFEFFLnRGLDYMAYYRAFALDALAGLLEEDVRAIVEEFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872276187  82 QKVIRPQMRPEGFKAIQCHKDAGHEIVGITATSDFITAPIFREFGITEIIATNAEVV-DGKYTGKVTNIACYQQGKLTRL 160
Cdd:TIGR01490  81 NQKIESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTRLEESeDGIYTGNIDGNNCKGEGKVHAL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1872276187 161 EQWLA--GRDVTESWAYSDSINDRFLLEHADHAIAVNPDDRL 200
Cdd:TIGR01490 161 AELLAeeQIDLKDSYAYGDSISDLPLLSLVGHPYVVNPDKKL 202
HAD pfam12710
haloacid dehalogenase-like hydrolase;
4-186 6.83e-36

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 124.95  E-value: 6.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872276187   4 ALFDLDHTLLNTDSDHSWGEFLVNEGLVDPVHHRAMNDKFYEDYKKGQLDPYAYNEFVFQFLTQHDhDYLTELHQLFMQK 83
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALLRRGGPDLWRALLVLLLLALLRLLGRLSRAGARELLRALLAGLP-EEDAAELERFVAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872276187  84 VIRPQMRPEGFKAIQCHKDAGHEIVGITATSDFITAPIFREFGITEIIATNAEVVDGKYTGKVTNIA--CYQQGKLTRLE 161
Cdd:pfam12710  80 VALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATELEVDDGRFTGELRLIGppCAGEGKVRRLR 159

                         170       180
                  ....*....|....*....|....*....
gi 1872276187 162 QWLAGR----DVTESWAYSDSINDRFLLE 186
Cdd:pfam12710 160 AWLAARglglDLADSVAYGDSPSDLPMLR 188
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 3-186 2.26e-16

Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model represents a subfamily of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. Subfamily IA, B, C and D are distinguished from the rest of the superfamily by the presence of a variable domain between the first and second conserved catalytic motifs. In subfamilies IA and IB, this domain consists of an alpha-helical bundle. It was necessary to model these two subfamilies separately, breaking them at a an apparent phylogenetic bifurcation, so that the resulting model(s) are not so broadly defined that members of subfamily III (which lack the variable domain) are included. Subfamily IA includes the enzyme phosphoserine phosphatase (TIGR00338) as well as three hypothetical equivalogs. Many members of these hypothetical equivalogs have been annotated as PSPase-like or PSPase-family proteins. In particular, the hypothetical equivalog which appears to be most closely related to PSPase contains only Archaea (while TIGR00338 contains only eukaryotes and bacteria) of which some are annotated as PSPases. Although this is a reasonable conjecture, none of these sequences has sufficient evidence for this assignment. If such should be found, this model should be retired while the PSPase model should be broadened to include these sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273653 [Multi-domain]  Cd Length: 177  Bit Score: 73.54  E-value: 2.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872276187   3 LALFDLDHTLLNTDSdhswgeflvnegLVDPVHHRAMNDKFYEDYKKGQLDPYAYNEFVFQFLTQHDHDYLTELHQlfmQ 82
Cdd:TIGR01488   1 LAIFDFDGTLTRQDS------------LIDLLAKLLGTNDEVIELTRLAPSGRISFEDALGRRLALLHRSRSEEVA---K 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872276187  83 KVIRPQ-MRPEGFKA-IQCHKDAGHEIVGITATSDFITAPIFREFGITEIIATNAEVVD-GKYTGK-VTNIACYQQGKLT 158
Cdd:TIGR01488  66 EFLARQvALRPGARElISWLKERGIDTVIVSGGFDFFVEPVAEKLGIDDVFANRLEFDDnGLLTGPiEGQVNPEGECKGK 145

                         170       180       190
                  ....*....|....*....|....*....|
gi 1872276187 159 RLEQWLA--GRDVTESWAYSDSINDRFLLE 186
Cdd:TIGR01488 146 VLKELLEesKITLKKIIAVGDSVNDLPMLK 175
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 2-195 4.23e-04

phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction 3-phospho-serine + H2O = L-serine + phosphate. It catalyzes the last of three steps in the biosynthesis of serine from D-3-phosphoglycerate. Note that this enzyme acts on free phosphoserine, not on phosphoserine residues of phosphoproteins. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273022 [Multi-domain]  Cd Length: 219  Bit Score: 40.03  E-value: 4.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872276187   2 KLALFDLDHTLLNTDSDHSWGEFLVNEGLVDPVHHRAMNDKFyeDYKKgqldpyAYNEFVfqfltqhdhDYLTELHQLFM 81
Cdd:TIGR00338  15 KLVVFDMDSTLINAETIDEIAKIAGVEEEVSEITERAMRGEL--DFKA------SLRERV---------ALLKGLPVELL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872276187  82 QKVIRPQMRPEGFKA-IQCHKDAGHEIVGITATSDFITAPIFREFGITEIIATNAEVVDGKYTGKVTNIACYQQGKLTRL 160
Cdd:TIGR00338  78 KEVRENLPLTEGAEElVKTLKEKGYKVAVISGGFDLFAEHVKDKLGLDAAFANRLEVEDGKLTGLVEGPIVDASYKGKTL 157

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1872276187 161 EQWLA--GRDVTESWAYSDSINDRFLLEHADHAIAVN 195
Cdd:TIGR00338 158 LILLRkeGISPENTVAVGDGANDLSMIKAAGLGIAFN 194
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 1-127 8.70e-04

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: 39.24  E-value: 8.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872276187   1 MKLALFDLDHTLLNTDSDHSWGEFLVNE--GLVDPVHH-----RAMNDKFYEDYKKGQLDpyaYNEFVFQFLTQHDHDYL 73
Cdd:COG1011     1 IKAVLFDLDGTLLDFDPVIAEALRALAErlGLLDEAEElaeayRAIEYALWRRYERGEIT---FAELLRRLLEELGLDLA 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1872276187  74 TELHQLFMQKVIR-PQMRPEGFKAIQCHKDAGHEIVGITATSDFITAPIFREFGI 127
Cdd:COG1011    78 EELAEAFLAALPElVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGL 132
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 97-195 1.42e-03

phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p; This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. 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: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 38.30  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872276187  97 IQCHKDAGHEIVGITATSDFITAPIFREFGITEIIATNAEVVDGKYTGKVTNIACYQQGKLTRLEQWLA--GRDVTESWA 174
Cdd:cd07500    79 IQTLKAKGYKTAVVSGGFTYFTDRLAEELGLDYAFANELEIKDGKLTGKVLGPIVDAQRKAETLQELAArlGIPLEQTVA 158

                          90       100
                  ....*....|....*....|.
gi 1872276187 175 YSDSINDRFLLEHADHAIAVN 195
Cdd:cd07500   159 VGDGANDLPMLKAAGLGIAFH 179
 
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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