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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446447047  32 GIITDLDNTLVGWDVKEPTERVKAWFKEANEKGITITIVSNNNESRVASFSQHLDIDFIFKARKPMGKAFDKAITKMNIR 111
Cdd:cd16416    1 GVITDLDNTLLAWDNPDLTPEVKAWLADLKEAGIKVVLVSNNNERRVAKVIEKLDLPFVARAGKPRPRAFRRALKEMDLP 80

                         90       100
                 ....*....|....*....|....*...
gi 446447047 112 PDQTVVIGDQMLTDVFGGNRRGLYTIMV 139
Cdd:cd16416   81 PEQVAMVGDQLFTDILGGNRAGLYTILV 108

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446447047   17 IFQIDLDKLVDKGVKGIITDLDNTLVGWDVKEPTERVKAWFKEANEKGITITIVSNNNESRVASFSQHLDIDFIF----- 91
Cdd:pfam00702  67 ILRGLVETLEAEGLTVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFdvvis 146

                          90       100       110
                  ....*....|....*....|....*....|...
gi 446447047   92 ----KARKPMGKAFDKAITKMNIRPDQTVVIGD 120
Cdd:pfam00702 147 gddvGVGKPKPEIYLAALERLGVKPEEVLMVGD 179

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446447047  32 GIITDLDNTLVGWDVKEPTERVKAWFKEANEKGITITIVSNNNESRVASFSQHLDIDFIFKARKPMGKAFDKAITKMNIR 111
Cdd:cd16416    1 GVITDLDNTLLAWDNPDLTPEVKAWLADLKEAGIKVVLVSNNNERRVAKVIEKLDLPFVARAGKPRPRAFRRALKEMDLP 80

                         90       100
                 ....*....|....*....|....*...
gi 446447047 112 PDQTVVIGDQMLTDVFGGNRRGLYTIMV 139
Cdd:cd16416   81 PEQVAMVGDQLFTDILGGNRAGLYTILV 108

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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446447047   31 KGIITDLDNTLVG-------WDVKEPTERVKAWFKEANEKGITITIVSNNN-----------ESRVASFSQHLDIDFIFK 92
Cdd:TIGR01662   1 KAVVLDLDGTLTDdvpyvsdEDERILYPEVPDALAELKEAGYKVVIVTNQSgigrgyfsrsfSGRVARRLEELGVPIDIL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446447047   93 -----ARKPMGKAFDKAITKMN-IRPDQTVVIGDQMLTDVFGGNRRGLYTIMVVP 141
Cdd:TIGR01662  81 yacpgCRKPKPGMFLEALKRFNeIDPEESVYVGDQDLTDLQAAKRVGLATILVAP 135

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446447047  53 VKAWFKEANEKGITITIVSNNNESRVASFSQHLDI----DFIF-----KARKPMGKAFDKAITKMNIRPDQTVVIGDQML 123
Cdd:COG1011   98 ALELLEALKARGYRLALLTNGSAELQEAKLRRLGLddlfDAVVsseevGVRKPDPEIFELALERLGVPPEEALFVGDSPE 177

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446447047 124 TDVFGGNRRGLYTIMVVPVKRTDGFITKFNRLIER 158
Cdd:COG1011  178 TDVAGARAAGMRTVWVNRSGEPAPAEPRPDYVISD 212

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446447047  33 IITDLDNTLVGwDVKEPTERVKawfkeaneKGITITIVSNN---------NESRVASFSQHLDIDFIFKARKPMGKAFDK 103
Cdd:cd04305    2 IIFDLDDTLLP-GAKELLEELK--------KGYKLGIITNGptevqweklEQLGIHKYFDHIVISEEVGVQKPNPEIFDY 72

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446447047 104 AITKMNIRPDQTVVIGDQMLTDVFGGNRRGLYTI 137
Cdd:cd04305   73 ALNQLGVKPEETLMVGDSLESDILGAKNAGIKTV 106

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

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446447047  95 KPMGKAFDKAITKMNIRPDQTVVIGDQMLTDVFGGNRRGLYTIMV 139
Cdd:COG0647  186 KPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAGLDTLLV 230

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446447047  21 DLDKLVDKGVKGIITDLDNTLVGWDVKEPTERVKAWFKEAN------------------EKGITITIVSNNNESRVASFS 82
Cdd:COG0546   39 ELRALIGLGLRELLRRLLGEDPDEELEELLARFRELYEEELldetrlfpgvrellealkARGIKLAVVTNKPREFAERLL 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446447047  83 QHLDIDFIFKA---------RKPMGKAFDKAITKMNIRPDQTVVIGDqMLTDVFGGNRRGLYTIMV 139
Cdd:COG0546  119 EALGLDDYFDAivggddvppAKPKPEPLLEALERLGLDPEEVLMVGD-SPHDIEAARAAGVPFIGV 183

Haloacid dehalogenase-like hydrolase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446447047   48 EPTERVKAWFKEANEKGITITIVSNNNESRVASFSQHLDI----DFI-----FKARKPMGKAFDKAITKMNIRPDQTVVI 118
Cdd:pfam13419  79 KPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLedyfDVIvggddVEGKKPDPDPILKALEQLGLKPEEVIYV 158

                          90       100
                  ....*....|....*....|.
gi 446447047  119 GDQmLTDVFGGNRRGLYTIMV 139
Cdd:pfam13419 159 GDS-PRDIEAAKNAGIKVIAV 178

HAD-IIA family hydrolase;

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 446447047  91 FKARKPMGKAFDKAITKMNIRPDQTVVIGDQMLTDVFGGNRRGLYTIMV 139
Cdd:PRK10444 170 FYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILV 218

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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446447047   63 KGITITIVSNNNESRVASFSqHLDI-----DFIFKARKPMGK----AFDKAITKMNIRPDQTVVIGDQmLTDVFGGNRRG 133
Cdd:TIGR01509  95 RGKKLALLTNSPRAHKLVLA-LLGLrdlfdVVIDSSDVGLGKpdpdIYLQALKALGLEPSECVFVDDS-PAGIEAAKAAG 172

                  ....*.
gi 446447047  134 LYTIMV 139
Cdd:TIGR01509 173 MHTVGV 178

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446447047  38 DNTLVGWDVKEPTERVKawfkeanEKGITITIVSNNNESRVASFSQHLDIDFIFK---------ARKPMGKAFDKAITKM 108
Cdd:cd02616   77 DLTKEYPGVYETLARLK-------SQGIKLGVVTTKLRETALKGLKLLGLDKYFDvivggddvtHHKPDPEPVLKALELL 149

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446447047 109 NIRPDQTVVIGDQMLtDVFGGNRRGLYTIMV 139
Cdd:cd02616  150 GAEPEEALMVGDSPH-DILAGKNAGVKTVGV 179

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to uncharacterized Drosophila melanogaster rhythmically expressed gene 2 protein and human haloacid dehalogenase-like hydrolase domain-containing protein 3; The haloacid dehalogenase-like (HAD) hydrolases are a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446447047  41 LVGWDVKEpTERVKAWFKEANEKGITITIVSNNNES--------RVASFSQHLDIDFIFKARKPMGKAFDKAITKMNIRP 112
Cdd:cd16415    1 LITFDVTG-TLLAVETLKDLKEKGLKLAVVSNFDRRlrellealGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSP 79

                         90       100
                 ....*....|....*....|....*....
gi 446447047 113 DQTVVIGDQMLTDVFGGNRRGLYTIMVVP 141
Cdd:cd16415   80 EEALHVGDDLKNDYLGARAVGWHALLVDR 108

FkbH-like domain; This model describes a domain of a family of proteins of unknown overall function. One of these, however, is a modular polyketide synthase 4800 amino acids in length from Streptomyces avermilitis in which this domain is the C-terminal segment. By contrast, the FkbH protein from Streptomyces hygroscopicus aparently contains only this domain. The remaining members of the family all contain an additional N-terminal domain of between 200 and 275 amino acids which show less than 20% identity to one another. It seems likely then that these proteins are involved in disparate functions, probably the biosynthesis of different natural products. For instance, the FkbH gene is found in a gene cluster believed to be responsible for the biosynthesis of unususal "PKS extender units" in the ascomycin pathway. This domain is composed of two parts, the first of which is a member of subfamily IIIC (TIGR01681) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. All of the characterized enzymes within subfamily III are phosphatases, and all of the active site residues characteristic of HAD-superfamily phosphatases are present in this domain. The C-terminal portion of this domain is unique to this family (by BLAST).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446447047   30 VKGIITDLDNTLVGWDV--------------KEPTERVKAWFKeaneKGITITIVSNNNESRVASFsqhLDI--DFIFKA 93
Cdd:TIGR01686   3 LKVLVLDLDNTLWGGVLgedgidnlnlsplhKTLQEKIKTLKK----QGFLLALASKNDEDDAKKV---FERrkDFILQA 75

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 446447047   94 R---------KPMGKAFDKAITKMNIRPDQTVVIGDQ 121
Cdd:TIGR01686  76 EdfdarsinwGPKSESLRKIAKKLNLGTDSFLFIDDN 112

Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, chaperones];

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446447047  48 EPT---ERVKAWFKEANEKGITITIVSN--NNESRVASFSQHLD---IDFifkarkpmgKAFD----KAITKMNIRP 112
Cdd:COG1180   83 EPTlqpEFLLDLAKLAKELGLHTALDTNgyIPEEALEELLPYLDavnIDL---------KAFDdefyRKLTGVSLEP 150

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-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, 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.

                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 446447047  33 IITDLDNTLVGwDVKEPTERVKAWFKEANEKGITITIVS 71
Cdd:cd07516    2 IALDLDGTLLN-SDKEISPRTKEAIKKAKEKGIKVVIAT 39

Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural subclass of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The classes are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Class I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Class II consists of sequences in which the capping domain is found between the second and third motifs. Class III sequences have no capping domain in iether of these positions. The Class IIA capping domain is predicted by PSI-PRED to consist of a mixed alpha-beta fold with the basic pattern: Helix-Helix-Helix-Sheet-Helix-Loop-Sheet-Helix-Sheet-Helix. Presently, this subfamily encompasses a single equivalog model (TIGR01452) for the eukaryotic phosphoglycolate phosphatase, as well as four hypothetical equivalogs covering closely related sequences (TIGR01456 and TIGR01458 in eukaryotes, TIGR01457 in gram positive bacteria and TIGR01459 in gram negative bacteria). The Escherishia coli NagD gene and the Bacillus subtilus AraL gene are members of this subfamily but are not members of the any of the presently defined equivalogs within it. NagD is part of the NAG operon responsible for N-acetylglucosamine metabolism. The function of this gene is unknown. Genes from several organisms have been annotated as NagD, or NagD-like. However, without data on the presence of other members of this pathway, (such as in the case of Yersinia pestis) these assignments should not be given great weight. The AraL gene is similar: it is part of the L-arabinose operon, but the function is unknown. A gene from Halobacterium has been annotated as AraL, but no other Ara operon genes have been annotated. Many of the genes in this subfamily have been annotated as "pNPPase" "4-nitrophenyl phosphatase" or "NPPase". These all refer to the same activity versus a common lab test compound used to determine phosphatase activity. There is no evidence that this activity is physiologically relevant. [Unknown function, Enzymes of unknown specificity]

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 446447047   95 KPMGKAFDKAITKMNIRPDQT-VVIGDQMLTDVFGGNRRGLYTIMV 139
Cdd:TIGR01460 188 KPSPAIYRAALNLLQARPERRdVMVGDNLRTDILGAKNAGFDTLLV 233