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Conserved domains on  [gi|446500661|ref|WP_000578515|]
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MULTISPECIES: metalloenzyme [Leptospira]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ALP_like super family cl23718
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 204-284 1.76e-08

alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.


The actual alignment was detected with superfamily member pfam01676:

Pssm-ID: 474031  Cd Length: 410  Bit Score: 55.48  E-value: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500661  204 EDDYTLCIYEFFLTDKIGHKMNWEAAEKHISELESFLTGILEELNPEEDQLIVTSDHGNLENLSVDVHTLNQVPTVLYGK 283
Cdd:pfam01676 297 KEKYDFVFVNFANTDMVGHTGDVEGKVKAIEAVDERLGELLDALEEDDGLLIITADHGNPEEMKDTDHTREPVPILIYGK 376


                  .
gi 446500661  284 Y 284
Cdd:pfam01676 377 G 377
 
Name Accession Description Interval E-value
Metalloenzyme pfam01676
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ...
 204-284 1.76e-08

Metalloenzyme superfamily; This family includes phosphopentomutase and 2,3-bisphosphoglycerate-independent phosphoglycerate mutase. This family is also related to pfam00245. The alignment contains the most conserved residues that are probably involved in metal binding and catalysis.


Pssm-ID: 396305  Cd Length: 410  Bit Score: 55.48  E-value: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500661  204 EDDYTLCIYEFFLTDKIGHKMNWEAAEKHISELESFLTGILEELNPEEDQLIVTSDHGNLENLSVDVHTLNQVPTVLYGK 283
Cdd:pfam01676 297 KEKYDFVFVNFANTDMVGHTGDVEGKVKAIEAVDERLGELLDALEEDDGLLIITADHGNPEEMKDTDHTREPVPILIYGK 376


                  .
gi 446500661  284 Y 284
Cdd:pfam01676 377 G 377
PRK12383 PRK12383
putative mutase; Provisional
 217-309 1.05e-06

putative mutase; Provisional


Pssm-ID: 237085  Cd Length: 406  Bit Score: 49.97  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500661 217 TDKIGHKMNWEAAEKHISELESFLTGILEELNPEeDQLIVTSDHGNLENLSVDVHTLNQVPTVLYGKYTSKMEQKIR-SI 295
Cdd:PRK12383 297 TDLAGHAEDVARYAERLEVVDRNLARLLEAMTPD-DCLVVMADHGNDPTIGHSHHTREVVPLLVYQKGLQATQLGVRtTL 375

                         90
                 ....*....|....
gi 446500661 296 VDIPSAIYDVLGID 309
Cdd:PRK12383 376 SDVGATVCEFFGAP 389
iPGM cd16010
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ...
 218-310 1.61e-04

2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- independent phosphoglycerate mutase (iPGM) catalyzes the interconversion of 3-phosphoglycerate (3PGA) and 2-phosphoglycerate (2PGA). They are the predominant PGM in plants and some other bacteria, including endospore forming Gram-positive bacteria and their close relatives. The two steps catalysis is a phosphatase reaction removing the phosphate from 2- or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The iPGM exists as a dimer, each monomer binding 2 magnesium atoms, which are essential for enzymatic activity.


Pssm-ID: 293734  Cd Length: 503  Bit Score: 43.17  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500661 218 DKIGHKMNWEAAEKHISELESFLTGILEELNPEEDQLIVTSDHGNLENLsVDV--------HTLNQVPTVLYGKYTSKME 289
Cdd:cd16010  394 DMVGHTGNLEAAVKAVEAVDECLGRIVEAVLENGGTLLITADHGNAEEM-IDPetggphtaHTTNPVPFIIVDPGLKRKL 472

                         90       100
                 ....*....|....*....|.
gi 446500661 290 QKIRSIVDIPSAIYDVLGIDI 310
Cdd:cd16010  473 LKDGGLADVAPTILDLLGIEK 493
GpmI COG0696
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ...
 254-310 9.97e-03

Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and metabolism]; Phosphoglycerate mutase (BPG-independent), AlkP superfamily is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 440460  Cd Length: 511  Bit Score: 37.34  E-value: 9.97e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446500661 254 LIVTSDHGNLENLsVDV--------HTLNQVPTVLYGKytsKMEQKIRS---IVDIPSAIYDVLGIDI 310
Cdd:COG0696  436 LLITADHGNAEQM-IDPdtggphtaHTTNPVPFILVGG---DKGVKLREdgrLADIAPTILELMGLPQ 499
 
Name Accession Description Interval E-value
Metalloenzyme pfam01676
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ...
 204-284 1.76e-08

Metalloenzyme superfamily; This family includes phosphopentomutase and 2,3-bisphosphoglycerate-independent phosphoglycerate mutase. This family is also related to pfam00245. The alignment contains the most conserved residues that are probably involved in metal binding and catalysis.


Pssm-ID: 396305  Cd Length: 410  Bit Score: 55.48  E-value: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500661  204 EDDYTLCIYEFFLTDKIGHKMNWEAAEKHISELESFLTGILEELNPEEDQLIVTSDHGNLENLSVDVHTLNQVPTVLYGK 283
Cdd:pfam01676 297 KEKYDFVFVNFANTDMVGHTGDVEGKVKAIEAVDERLGELLDALEEDDGLLIITADHGNPEEMKDTDHTREPVPILIYGK 376


                  .
gi 446500661  284 Y 284
Cdd:pfam01676 377 G 377
PRK12383 PRK12383
putative mutase; Provisional
 217-309 1.05e-06

putative mutase; Provisional


Pssm-ID: 237085  Cd Length: 406  Bit Score: 49.97  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500661 217 TDKIGHKMNWEAAEKHISELESFLTGILEELNPEeDQLIVTSDHGNLENLSVDVHTLNQVPTVLYGKYTSKMEQKIR-SI 295
Cdd:PRK12383 297 TDLAGHAEDVARYAERLEVVDRNLARLLEAMTPD-DCLVVMADHGNDPTIGHSHHTREVVPLLVYQKGLQATQLGVRtTL 375

                         90
                 ....*....|....
gi 446500661 296 VDIPSAIYDVLGID 309
Cdd:PRK12383 376 SDVGATVCEFFGAP 389
PRK04135 PRK04135
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
212-285 3.68e-05

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


Pssm-ID: 179745 [Multi-domain]  Cd Length: 395  Bit Score: 44.91  E-value: 3.68e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446500661 212 YEFFL-----TDKIGHKMNWEAAEKHISELESFLTGILeELNPeeDQLIVTSDHGNLENLSvdVHTLNQVPTVLYGKYT 285
Cdd:PRK04135 280 YDFFFlhvkkTDSYGEDGNFEEKVKVIEEVDALLPEIL-ALKP--DVLVITGDHSTPAVLK--GHSWHPVPLLLYSKYC 353
iPGM cd16010
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ...
 218-310 1.61e-04

2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- independent phosphoglycerate mutase (iPGM) catalyzes the interconversion of 3-phosphoglycerate (3PGA) and 2-phosphoglycerate (2PGA). They are the predominant PGM in plants and some other bacteria, including endospore forming Gram-positive bacteria and their close relatives. The two steps catalysis is a phosphatase reaction removing the phosphate from 2- or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The iPGM exists as a dimer, each monomer binding 2 magnesium atoms, which are essential for enzymatic activity.


Pssm-ID: 293734  Cd Length: 503  Bit Score: 43.17  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500661 218 DKIGHKMNWEAAEKHISELESFLTGILEELNPEEDQLIVTSDHGNLENLsVDV--------HTLNQVPTVLYGKYTSKME 289
Cdd:cd16010  394 DMVGHTGNLEAAVKAVEAVDECLGRIVEAVLENGGTLLITADHGNAEEM-IDPetggphtaHTTNPVPFIIVDPGLKRKL 472

                         90       100
                 ....*....|....*....|.
gi 446500661 290 QKIRSIVDIPSAIYDVLGIDI 310
Cdd:cd16010  473 LKDGGLADVAPTILDLLGIEK 493
PRK04024 PRK04024
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
212-283 4.15e-04

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


Pssm-ID: 235203  Cd Length: 412  Bit Score: 41.82  E-value: 4.15e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446500661 212 YEFFL-----TDKIGHKMNWEAAEKHISELESFLTGILEELNPEEDQLIVTSDHGNleNLSVDVHTLNQVPTVLYGK 283
Cdd:PRK04024 294 YDFVLlnikgTDEAGHDGDFEGKVEVIEKIDKMLGYILDNLDLDEVYIAVTGDHST--PVEVKDHSGDPVPILIYGP 368
PPM cd16009
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ...
 203-283 4.23e-04

Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase superfamily members that interconvert alpha-D-ribose 5-phosphate (ribose 5-phosphate) and alpha-D-ribose 1-phosphate (ribose 1-phosphate). This reaction bridges glucose metabolism and RNA biosynthesis. PPM is a Mn(2+)-dependent enzyme and protein phosphorylation activates the enzyme.


Pssm-ID: 293733  Cd Length: 382  Bit Score: 41.67  E-value: 4.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500661 203 KEDDYTLCiyeFF----LTDKIGHKMNWEAAEKHISELESFLTGILEELNPEeDQLIVTSDHGNlenlsvDV------HT 272
Cdd:cd16009  267 KEDFNGLI---FTnlvdFDMLYGHRRDPEGYAEALEEFDRRLPELLAKLKED-DLLIITADHGN------DPtiggtdHT 336

                         90
                 ....*....|.
gi 446500661 273 LNQVPTVLYGK 283
Cdd:cd16009  337 REYVPLLVYGK 347
PRK05434 PRK05434
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
198-310 3.29e-03

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


Pssm-ID: 235463  Cd Length: 507  Bit Score: 38.93  E-value: 3.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500661 198 IIRNCKEDDYTLCIYEFFLTDKIGHKMNWEAAEKHISELESFLTGILEELNPEEDQLIVTSDHGNLENLSVDV------- 270
Cdd:PRK05434 379 LVEAIESGKYDFIILNFANPDMVGHTGNLEAAVKAVEAVDECLGRVVDAVLKVGGTLLITADHGNAEQMIDPEtgqphta 458

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446500661 271 HTLNQVPTVLYGKYTSKMEQKIRSivDIPSAIYDVLGIDI 310
Cdd:PRK05434 459 HTTNPVPFILVGGKALRLEGGKLA--DIAPTILDLLGLEQ 496
GpmI COG0696
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ...
 254-310 9.97e-03

Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and metabolism]; Phosphoglycerate mutase (BPG-independent), AlkP superfamily is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 440460  Cd Length: 511  Bit Score: 37.34  E-value: 9.97e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446500661 254 LIVTSDHGNLENLsVDV--------HTLNQVPTVLYGKytsKMEQKIRS---IVDIPSAIYDVLGIDI 310
Cdd:COG0696  436 LLITADHGNAEQM-IDPdtggphtaHTTNPVPFILVGG---DKGVKLREdgrLADIAPTILELMGLPQ 499
 
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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