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Conserved domains on  [gi|2065838525|gb|KAG7605537|]
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Pyridoxine 5'-phosphate oxidase dimerization C-terminal [Arabidopsis thaliana x Arabidopsis arenosa]

Protein Classification

pyridoxal 5'-phosphate synthase( domain architecture ID 11477288)

pyridoxal 5'-phosphate synthase catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02918 PLN02918
pyridoxine (pyridoxamine) 5'-phosphate oxidase
4-530 0e+00

pyridoxine (pyridoxamine) 5'-phosphate oxidase


:

Pssm-ID: 215496 [Multi-domain]  Cd Length: 544  Bit Score: 1053.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525   4 VIRRVTTMTFTFLLQSPPLPISP-SPPQFSLSSSPLSKTQRFITPSQG----SRLRTLCTKV-------------IIPNM 65
Cdd:PLN02918    1 NIKSTATMTFTFLLQSLLPLPISpPPPHSSSLSSSPSPTQRFLTPSQGsrlpPRRRALCTKSqdprwrramaslaVIPNM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525  66 QDSGSPPLSYLTQREAAEIDETLMGPLGFSIDQLMELAGLSVAASIAEVYKPEEYSRVLAICGPGNNGGDGLVAARHLHH 145
Cdd:PLN02918   81 QDSGSPPLSYLTQREAAEIDETLMGPLGFSVDQLMELAGLSVAASIAEVYKPGEYSRVLAICGPGNNGGDGLVAARHLHH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 146 FGYKPFICYPKRTAKPLYTGLVTQLDSLSVPFVSVEDLPDDLSKDFDVIVDAMFGFSFHGAPRPPFDDLIRRLVSLQNYE 225
Cdd:PLN02918  161 FGYKPFVCYPKRTAKPLYTGLVTQLESLSVPFVSVEDLPADLSKDFDIIVDAMFGFSFHGAPRPPFDDLIRRLVSLQNYE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 226 QTLqKHPVIVSVDIPSGWHVEEGDHEDGGIKPDMLVSLTAPKLCAKRFRGPHHFLGGRFVPPSVAEKYKLELPSYPGTSM 305
Cdd:PLN02918  241 QTL-KHPVIVSVDIPSGWHVEEGDHEGGGIKPDMLVSLTAPKLCAKKFRGPHHFLGGRFVPPSIVEKYKLHLPPYPGTSM 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 306 CVRIGKPPKVDISAMRVNYVSPELLEEQVETDPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENG 385
Cdd:PLN02918  320 CVRIGKPPSVDISALRENYISPELLEEQVETDPTDQFRKWFDEAVAAGLREPNAMALSTANKDGKPSSRMVLLKGVDKNG 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 386 FVWFTNYESKKGSDLSENPSAALLFYWEILNRQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYD 465
Cdd:PLN02918  400 FVWYTNYESQKGSDLSENPSAALLFYWEELNRQVRVEGSVQKVPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYQ 479
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2065838525 466 EYEELTKQYSDGSVIPKPKNWGGFRLKPNLFEFWQGQPSRLHDRLQYSLQDVNGNPAWKIHRLAP 530
Cdd:PLN02918  480 EYKELEKKYSDGSVIPKPKNWGGYRLKPNLFEFWQGQQSRLHDRLQYSLQEVNGKPVWKIHRLAP 544
 
Name Accession Description Interval E-value
PLN02918 PLN02918
pyridoxine (pyridoxamine) 5'-phosphate oxidase
4-530 0e+00

pyridoxine (pyridoxamine) 5'-phosphate oxidase


Pssm-ID: 215496 [Multi-domain]  Cd Length: 544  Bit Score: 1053.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525   4 VIRRVTTMTFTFLLQSPPLPISP-SPPQFSLSSSPLSKTQRFITPSQG----SRLRTLCTKV-------------IIPNM 65
Cdd:PLN02918    1 NIKSTATMTFTFLLQSLLPLPISpPPPHSSSLSSSPSPTQRFLTPSQGsrlpPRRRALCTKSqdprwrramaslaVIPNM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525  66 QDSGSPPLSYLTQREAAEIDETLMGPLGFSIDQLMELAGLSVAASIAEVYKPEEYSRVLAICGPGNNGGDGLVAARHLHH 145
Cdd:PLN02918   81 QDSGSPPLSYLTQREAAEIDETLMGPLGFSVDQLMELAGLSVAASIAEVYKPGEYSRVLAICGPGNNGGDGLVAARHLHH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 146 FGYKPFICYPKRTAKPLYTGLVTQLDSLSVPFVSVEDLPDDLSKDFDVIVDAMFGFSFHGAPRPPFDDLIRRLVSLQNYE 225
Cdd:PLN02918  161 FGYKPFVCYPKRTAKPLYTGLVTQLESLSVPFVSVEDLPADLSKDFDIIVDAMFGFSFHGAPRPPFDDLIRRLVSLQNYE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 226 QTLqKHPVIVSVDIPSGWHVEEGDHEDGGIKPDMLVSLTAPKLCAKRFRGPHHFLGGRFVPPSVAEKYKLELPSYPGTSM 305
Cdd:PLN02918  241 QTL-KHPVIVSVDIPSGWHVEEGDHEGGGIKPDMLVSLTAPKLCAKKFRGPHHFLGGRFVPPSIVEKYKLHLPPYPGTSM 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 306 CVRIGKPPKVDISAMRVNYVSPELLEEQVETDPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENG 385
Cdd:PLN02918  320 CVRIGKPPSVDISALRENYISPELLEEQVETDPTDQFRKWFDEAVAAGLREPNAMALSTANKDGKPSSRMVLLKGVDKNG 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 386 FVWFTNYESKKGSDLSENPSAALLFYWEILNRQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYD 465
Cdd:PLN02918  400 FVWYTNYESQKGSDLSENPSAALLFYWEELNRQVRVEGSVQKVPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYQ 479
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2065838525 466 EYEELTKQYSDGSVIPKPKNWGGFRLKPNLFEFWQGQPSRLHDRLQYSLQDVNGNPAWKIHRLAP 530
Cdd:PLN02918  480 EYKELEKKYSDGSVIPKPKNWGGYRLKPNLFEFWQGQQSRLHDRLQYSLQEVNGKPVWKIHRLAP 544
PdxH COG0259
Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine ...
316-530 9.74e-114

Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine/pyridoxamine 5'-phosphate oxidase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 440029  Cd Length: 212  Bit Score: 335.62  E-value: 9.74e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 316 DISAMRVNYVSPELLEEQVETDPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENGFVWFTNYESK 395
Cdd:COG0259     3 DLADLRREYTKGGLDESDLPADPLALFARWLEEAEAAGVPEPNAMTLATVDADGRPSARTVLLKGVDERGFVFYTNYESR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 396 KGSDLSENPSAALLFYWEILNRQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYDEYEELTKQYS 475
Cdd:COG0259    83 KGRELAANPRAALTFFWPELERQVRIEGRVEKVSAAESDAYFASRPRGSQLGAWASPQSQPIASREELEARFAELEARFA 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2065838525 476 DGSViPKPKNWGGFRLKPNLFEFWQGQPSRLHDRLQYSLQDVNgnpaWKIHRLAP 530
Cdd:COG0259   163 GGDV-PRPPHWGGYRVVPDRIEFWQGRPSRLHDRLRYTREDGG----WTIERLAP 212
pdxH TIGR00558
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is ...
337-530 2.02e-113

pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is designed to find only true pyridoxamine-phosphate oxidase and to ignore the related protein PhzG involved in phenazine biosynthesis. This protein from E. coli was characterized as a homodimer with two FMN per dimer. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]


Pssm-ID: 273138  Cd Length: 190  Bit Score: 334.08  E-value: 2.02e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 337 DPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENGFVWFTNYESKKGSDLSENPSAALLFYWEILN 416
Cdd:TIGR00558   1 DPIEQFERWFEEAIEAELPEPNAMTLATVDADGRPSARIVLLKGFDERGFVFYTNYESRKGQELAANPKAALLFPWHSLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 417 RQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYDEYEELTKQYSDGSViPKPKNWGGFRLKPNLF 496
Cdd:TIGR00558  81 RQVRIEGRVEKVSREESDAYFASRPRGSQIGAWASQQSRPIASREELEARFAELKARFPDGEV-PRPEFWGGYRVVPDEI 159
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2065838525 497 EFWQGQPSRLHDRLQYSLQDVNGnpaWKIHRLAP 530
Cdd:TIGR00558 160 EFWQGRPSRLHDRFRYRRDGDGS---WRIERLAP 190
phena_PhzG NF038138
phenazine biosynthesis FMN-dependent oxidase PhzG;
337-530 3.42e-52

phenazine biosynthesis FMN-dependent oxidase PhzG;


Pssm-ID: 468380  Cd Length: 205  Bit Score: 176.40  E-value: 3.42e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 337 DPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENGFVWFTNYESKKGSDLSENPSAALLFYWEILN 416
Cdd:NF038138   19 EPLGLLRRWLEAAVALGVREPRALALATADADGRPSTRIVVVKEVSDRGLVFTTHAGSRKGRELAANPWASGVLYWRETS 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 417 RQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYDEYEELTKQysdGSVIPKPKNWGGFRLKPNLF 496
Cdd:NF038138   99 QQISLSGPVERLPDAESDALWAARPVATHAMTAASRQSEPLDDEAALRAEARELAEA---GGPLPRPARFVGYRLVPEEV 175
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2065838525 497 EFWQGQPSRLHDRLQYslqDVNGnPAWKIHRLAP 530
Cdd:NF038138  176 EFWAAGPDRLHRRLRY---DRDG-DGWTHVRLQP 205
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
97-269 1.99e-41

YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a set of catalytic residues and structural features that are different from the conventional dehydrogenases. YjeF-N domain is fused to Ribokinases in bacteria (YjeF), where they may be phosphatases, and to divergent Sm and the FDF domain in eukaryotes (Dcp3p and FLJ21128), where they may be involved in decapping and catalyze hydrolytic RNA-processing reactions.


Pssm-ID: 427546 [Multi-domain]  Cd Length: 168  Bit Score: 146.60  E-value: 1.99e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525  97 DQLMELAGLSVAASIAEVYKPEEySRVLAICGPGNNGGDGLVAARHLHHFGYK--PFICYPkrtaKPLYTGLV-TQLDSL 173
Cdd:pfam03853   2 AVLMENAGRAAARVLKALLSPAG-PKVLILCGPGNNGGDGLAAARHLANRGAKvtVLLLGP----EEKLSEDArRQLDLF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 174 S------VPFVSVEDLPDDLSkDFDVIVDAMFGFSFHGAPRPPFDDLIRRLvslqnyeqtLQKHPVIVSVDIPSGWHVEE 247
Cdd:pfam03853  77 KklggkiVTDNPDEDLEKLLS-PVDLIIDALLGTGLSGPLRGEYAALIEWI---------NQSGAPVLAVDIPSGLDADT 146
                         170       180
                  ....*....|....*....|..
gi 2065838525 248 GDHEDGGIKPDMLVSLTAPKLC 269
Cdd:pfam03853 147 GAVLGTAVRADHTVTFGAPKPG 168
 
Name Accession Description Interval E-value
PLN02918 PLN02918
pyridoxine (pyridoxamine) 5'-phosphate oxidase
4-530 0e+00

pyridoxine (pyridoxamine) 5'-phosphate oxidase


Pssm-ID: 215496 [Multi-domain]  Cd Length: 544  Bit Score: 1053.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525   4 VIRRVTTMTFTFLLQSPPLPISP-SPPQFSLSSSPLSKTQRFITPSQG----SRLRTLCTKV-------------IIPNM 65
Cdd:PLN02918    1 NIKSTATMTFTFLLQSLLPLPISpPPPHSSSLSSSPSPTQRFLTPSQGsrlpPRRRALCTKSqdprwrramaslaVIPNM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525  66 QDSGSPPLSYLTQREAAEIDETLMGPLGFSIDQLMELAGLSVAASIAEVYKPEEYSRVLAICGPGNNGGDGLVAARHLHH 145
Cdd:PLN02918   81 QDSGSPPLSYLTQREAAEIDETLMGPLGFSVDQLMELAGLSVAASIAEVYKPGEYSRVLAICGPGNNGGDGLVAARHLHH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 146 FGYKPFICYPKRTAKPLYTGLVTQLDSLSVPFVSVEDLPDDLSKDFDVIVDAMFGFSFHGAPRPPFDDLIRRLVSLQNYE 225
Cdd:PLN02918  161 FGYKPFVCYPKRTAKPLYTGLVTQLESLSVPFVSVEDLPADLSKDFDIIVDAMFGFSFHGAPRPPFDDLIRRLVSLQNYE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 226 QTLqKHPVIVSVDIPSGWHVEEGDHEDGGIKPDMLVSLTAPKLCAKRFRGPHHFLGGRFVPPSVAEKYKLELPSYPGTSM 305
Cdd:PLN02918  241 QTL-KHPVIVSVDIPSGWHVEEGDHEGGGIKPDMLVSLTAPKLCAKKFRGPHHFLGGRFVPPSIVEKYKLHLPPYPGTSM 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 306 CVRIGKPPKVDISAMRVNYVSPELLEEQVETDPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENG 385
Cdd:PLN02918  320 CVRIGKPPSVDISALRENYISPELLEEQVETDPTDQFRKWFDEAVAAGLREPNAMALSTANKDGKPSSRMVLLKGVDKNG 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 386 FVWFTNYESKKGSDLSENPSAALLFYWEILNRQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYD 465
Cdd:PLN02918  400 FVWYTNYESQKGSDLSENPSAALLFYWEELNRQVRVEGSVQKVPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYQ 479
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2065838525 466 EYEELTKQYSDGSVIPKPKNWGGFRLKPNLFEFWQGQPSRLHDRLQYSLQDVNGNPAWKIHRLAP 530
Cdd:PLN02918  480 EYKELEKKYSDGSVIPKPKNWGGYRLKPNLFEFWQGQQSRLHDRLQYSLQEVNGKPVWKIHRLAP 544
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
60-530 0e+00

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 854.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525  60 VIIPNMQDSGSppLSYLTQREAAEIDETLMGPLGFSIDQLMELAGLSVAASIAEVYKPEEYSRVLAICGPGNNGGDGLVA 139
Cdd:PLN03049    1 VAVQHLHNPDS--ISYLSQREAIAIDEHLMGPLGFSVDQLMELAGLSVASAIAEVYSPSEYRRVLALCGPGNNGGDGLVA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 140 ARHLHHFGYKPFICYPKRTAKPLYTGLVTQLDSLSVPFVSVEDLPDDLSKDFDVIVDAMFGFSFHGAPRPPFDDLIRRLV 219
Cdd:PLN03049   79 ARHLHHFGYKPSICYPKRTDKPLYNGLVTQLESLSVPFLSVEDLPSDLSSQFDIVVDAMFGFSFHGAPRPPFDDLIQKLV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 220 SLQNyeqtlqkHPVIVSVDIPSGWHVEEGDHEDGGIKPDMLVSLTAPKLCAKRFRGPHHFLGGRFVPPSVAEKYKLELPS 299
Cdd:PLN03049  159 RAAG-------PPPIVSVDIPSGWHVEEGDVNGEGLKPDMLVSLTAPKLCAKMFKGPHHFLGGRFVPPAIVEKFKLHLPP 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 300 YPGTSMCVRIGKPPKVDISAMRVNYVSPELLEEQVETDPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLK 379
Cdd:PLN03049  232 YPGTSMCVRIGKTPSVDIAALRENYVGPELLEEQVNADPIDQFKEWFDDAVAAGLREPNAMTLATAGEDGRPSARIVLLK 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 380 GFDENGFVWFTNYESKKGSDLSENPSAALLFYWEILNRQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPG 459
Cdd:PLN03049  312 GVDKRGFVWYTNYDSRKAHELSANPKASLVFYWDGLHRQVRVEGSVEKVSEEESDQYFHSRPRGSQIGALVSKQSTVIPG 391
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2065838525 460 RHVLYDEYEELTKQYSDGSVIPKPKNWGGFRLKPNLFEFWQGQPSRLHDRLQYSLQDVNGNPAWKIHRLAP 530
Cdd:PLN03049  392 RHILDQSYKELEAKYADSSAIPKPKHWGGYRLKPELIEFWQGRESRLHDRLQYTREEINGKSVWKIDRLAP 462
PdxH COG0259
Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine ...
316-530 9.74e-114

Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine/pyridoxamine 5'-phosphate oxidase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 440029  Cd Length: 212  Bit Score: 335.62  E-value: 9.74e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 316 DISAMRVNYVSPELLEEQVETDPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENGFVWFTNYESK 395
Cdd:COG0259     3 DLADLRREYTKGGLDESDLPADPLALFARWLEEAEAAGVPEPNAMTLATVDADGRPSARTVLLKGVDERGFVFYTNYESR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 396 KGSDLSENPSAALLFYWEILNRQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYDEYEELTKQYS 475
Cdd:COG0259    83 KGRELAANPRAALTFFWPELERQVRIEGRVEKVSAAESDAYFASRPRGSQLGAWASPQSQPIASREELEARFAELEARFA 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2065838525 476 DGSViPKPKNWGGFRLKPNLFEFWQGQPSRLHDRLQYSLQDVNgnpaWKIHRLAP 530
Cdd:COG0259   163 GGDV-PRPPHWGGYRVVPDRIEFWQGRPSRLHDRLRYTREDGG----WTIERLAP 212
pdxH TIGR00558
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is ...
337-530 2.02e-113

pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is designed to find only true pyridoxamine-phosphate oxidase and to ignore the related protein PhzG involved in phenazine biosynthesis. This protein from E. coli was characterized as a homodimer with two FMN per dimer. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]


Pssm-ID: 273138  Cd Length: 190  Bit Score: 334.08  E-value: 2.02e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 337 DPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENGFVWFTNYESKKGSDLSENPSAALLFYWEILN 416
Cdd:TIGR00558   1 DPIEQFERWFEEAIEAELPEPNAMTLATVDADGRPSARIVLLKGFDERGFVFYTNYESRKGQELAANPKAALLFPWHSLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 417 RQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYDEYEELTKQYSDGSViPKPKNWGGFRLKPNLF 496
Cdd:TIGR00558  81 RQVRIEGRVEKVSREESDAYFASRPRGSQIGAWASQQSRPIASREELEARFAELKARFPDGEV-PRPEFWGGYRVVPDEI 159
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2065838525 497 EFWQGQPSRLHDRLQYSLQDVNGnpaWKIHRLAP 530
Cdd:TIGR00558 160 EFWQGRPSRLHDRFRYRRDGDGS---WRIERLAP 190
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
65-309 2.36e-113

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 336.08  E-value: 2.36e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525  65 MQDSGsppLSYLTQREAAEIDETLMGPLGFSIDQLMELAGLSVAASIAEVYK-------PEEYSRVLAICGPGNNGGDGL 137
Cdd:PLN03050    1 MSNIQ---TGYLNAQDAAALDEELMSTPGFSLEQLMELAGLSVAEAVYEVADgekasnpPGRHPRVLLVCGPGNNGGDGL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 138 VAARHLHHFGYKPFICYPKRTAKPLYTGLVTQLDSLSVPFVSV----EDLPDDLSKDFDVIVDAMFGFSFHGAPRPPFDD 213
Cdd:PLN03050   78 VAARHLAHFGYEVTVCYPKQSSKPHYENLVTQCEDLGIPFVQAiggtNDSSKPLETTYDVIVDAIFGFSFHGAPRAPFDT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 214 LIRRLVSLQNyeqtlqKHPVIVSVDIPSGWHVEEGDHEDGGIKPDMLVSLTAPKLCAKRFRGpHHFLGGRFVPPSVAEKY 293
Cdd:PLN03050  158 LLAQMVQQQK------SPPPIVSVDVPSGWDVDEGDVSGTGMRPDVLVSLTAPKLSAKKFEG-RHFVGGRFLPPAIAEKY 230
                         250
                  ....*....|....*.
gi 2065838525 294 KLELPSYPGTSMCVRI 309
Cdd:PLN03050  231 GLQKPPYPGVSQVMEV 246
PRK05679 PRK05679
pyridoxal 5'-phosphate synthase;
331-530 2.49e-98

pyridoxal 5'-phosphate synthase;


Pssm-ID: 235555  Cd Length: 195  Bit Score: 295.59  E-value: 2.49e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 331 EEQVETDPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENGFVWFTNYESKKGSDLSENPSAALLF 410
Cdd:PRK05679    1 RADLPAEPLALFERWLAEAVKAELNDPNAMTLATVDEDGRPSQRIVLLKGFDERGFVFYTNYESRKGRQLAANPKAALLF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 411 YWEILNRQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYDEYEELTKQYSDGSViPKPKNWGGFR 490
Cdd:PRK05679   81 PWKSLERQVRVEGRVEKVSAEESDAYFASRPRGSQIGAWASKQSRPISSRAALEAKFAEVKAKFAQGEV-PRPPHWGGYR 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2065838525 491 LKPNLFEFWQGQPSRLHDRLQYSLQDvngnPAWKIHRLAP 530
Cdd:PRK05679  160 VVPESIEFWQGRPSRLHDRILYRRDD----GGWKIERLAP 195
phena_PhzG NF038138
phenazine biosynthesis FMN-dependent oxidase PhzG;
337-530 3.42e-52

phenazine biosynthesis FMN-dependent oxidase PhzG;


Pssm-ID: 468380  Cd Length: 205  Bit Score: 176.40  E-value: 3.42e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 337 DPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENGFVWFTNYESKKGSDLSENPSAALLFYWEILN 416
Cdd:NF038138   19 EPLGLLRRWLEAAVALGVREPRALALATADADGRPSTRIVVVKEVSDRGLVFTTHAGSRKGRELAANPWASGVLYWRETS 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 417 RQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYDEYEELTKQysdGSVIPKPKNWGGFRLKPNLF 496
Cdd:NF038138   99 QQISLSGPVERLPDAESDALWAARPVATHAMTAASRQSEPLDDEAALRAEARELAEA---GGPLPRPARFVGYRLVPEEV 175
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2065838525 497 EFWQGQPSRLHDRLQYslqDVNGnPAWKIHRLAP 530
Cdd:NF038138  176 EFWAAGPDRLHRRLRY---DRDG-DGWTHVRLQP 205
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
81-287 5.22e-45

yjeF N-terminal region; The protein region corresponding to this model shows no clear homology to any protein of known function. This model is built on yeast protein YNL200C and the N-terminal regions of E. coli yjeF and its orthologs in various species. The C-terminal region of yjeF and its orthologs shows similarity to hydroxyethylthiazole kinase (thiM) and other enzymes involved in thiamine biosynthesis. Yeast YKL151C and B. subtilis yxkO match the yjeF C-terminal domain but lack this region. [Unknown function, General]


Pssm-ID: 272956 [Multi-domain]  Cd Length: 205  Bit Score: 157.19  E-value: 5.22e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525  81 AAEIDETLMGPLGFSIDQLMELAGLSVAASIAEVYKPEEysRVLAICGPGNNGGDGLVAARHLHhfGYKPFICYPKRTAK 160
Cdd:TIGR00197   8 DMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAG--HVIIFCGPGNNGGDGFVVARHLK--GFGVEVFLLKKEKR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 161 -PLYTGLVTQLDSLSVPFVSVEDLPDDLSKDFDVIVDAMFGFSFHGAPRPPFDDLIrrlvslqnyeQTLQKHPV-IVSVD 238
Cdd:TIGR00197  84 iECTEQAEVNLKALKVGGISIDEGNLVKPEDCDVIIDAILGTGFKGKLREPFKTIV----------ESINELPApIVSVD 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2065838525 239 IPSGWHVEEGDHEDGGIKPDMLVSLTAPKLCAKRFRGPH---HFLGGRFVPP 287
Cdd:TIGR00197 154 IPSGLDVDTGAIEGPAVNADLTITFHAIKPCLLSDRADVtgeLKVGGIGIPP 205
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
97-269 1.99e-41

YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a set of catalytic residues and structural features that are different from the conventional dehydrogenases. YjeF-N domain is fused to Ribokinases in bacteria (YjeF), where they may be phosphatases, and to divergent Sm and the FDF domain in eukaryotes (Dcp3p and FLJ21128), where they may be involved in decapping and catalyze hydrolytic RNA-processing reactions.


Pssm-ID: 427546 [Multi-domain]  Cd Length: 168  Bit Score: 146.60  E-value: 1.99e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525  97 DQLMELAGLSVAASIAEVYKPEEySRVLAICGPGNNGGDGLVAARHLHHFGYK--PFICYPkrtaKPLYTGLV-TQLDSL 173
Cdd:pfam03853   2 AVLMENAGRAAARVLKALLSPAG-PKVLILCGPGNNGGDGLAAARHLANRGAKvtVLLLGP----EEKLSEDArRQLDLF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 174 S------VPFVSVEDLPDDLSkDFDVIVDAMFGFSFHGAPRPPFDDLIRRLvslqnyeqtLQKHPVIVSVDIPSGWHVEE 247
Cdd:pfam03853  77 KklggkiVTDNPDEDLEKLLS-PVDLIIDALLGTGLSGPLRGEYAALIEWI---------NQSGAPVLAVDIPSGLDADT 146
                         170       180
                  ....*....|....*....|..
gi 2065838525 248 GDHEDGGIKPDMLVSLTAPKLC 269
Cdd:pfam03853 147 GAVLGTAVRADHTVTFGAPKPG 168
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
76-281 2.20e-41

NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and metabolism];


Pssm-ID: 439832 [Multi-domain]  Cd Length: 499  Bit Score: 155.41  E-value: 2.20e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525  76 LTQREAAEIDETLMGPLGFSIDQLMELAGLSVAASIAEVYkPEEYSRVLAICGPGNNGGDGLVAARHLHHFGYKPFICYP 155
Cdd:COG0062     4 LTAAQMRALDRAAIEALGIPGLVLMERAGRAVARAIRRRF-PSAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 156 KRTAKplYTGL----VTQLDSLSVPFVSVEDLPDDLSkDFDVIVDAMFGFSFHGAPRPPFDDLIRRLVSLQNYeqtlqkh 231
Cdd:COG0062    83 GDPEK--LSGDaaanLERLKAAGIPILELDDELPELA-EADLIVDALFGTGLSRPLRGPYAELIEAINASGAP------- 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2065838525 232 pvIVSVDIPSGWHVEEGDHEDGGIKPDMLVSLTAPKLCakrfrgphHFLG 281
Cdd:COG0062   153 --VLAVDIPSGLDADTGEVLGAAVRADLTVTFGAPKPG--------LLLG 192
Putative_PNPOx pfam01243
Pyridoxamine 5'-phosphate oxidase; Family of domains with putative PNPOx function. Family ...
346-432 7.10e-26

Pyridoxamine 5'-phosphate oxidase; Family of domains with putative PNPOx function. Family members were predicted to encode pyridoxamine 5'-phosphate oxidase, based on sequence similarity. However, there is no experimental data to validate the predicted activity and purified proteins, such as Swiss:Q06199 and its paralogs, do not possess this activity, nor do they bind to flavin mononucleotide (FMN). To date, the only time functional oxidase activity has been experimentally demonstrated is when the sequences contain both pfam01243 and pfam10590. Moreover, some of the family members that contain both domains have been shown to be involved in phenazine biosynthesis. While some molecular function has been experimentally validated for the proteins containing both domains, the role performed by each domain on its own is unknown.


Pssm-ID: 426149 [Multi-domain]  Cd Length: 88  Bit Score: 101.17  E-value: 7.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 346 FDEAVAAGLRETNAMALSTANKDKKPSSRMVLLK-GFDENGFVWFTNYESKKGSDLSENPSAALLFYWEILNRQVRIEGP 424
Cdd:pfam01243   1 LTEEIREFLAEPNAVVLATVDKDGRPNVRPVGLKyGFDTVGILFATNTDSRKARNLEENPRVALLFGDPELRRGVRIEGT 80

                  ....*...
gi 2065838525 425 VERIPESE 432
Cdd:pfam01243  81 AEIVTDGE 88
PNP_phzG_C pfam10590
Pyridoxine 5'-phosphate oxidase C-terminal dimerization region; This domain represents one of ...
486-530 9.01e-21

Pyridoxine 5'-phosphate oxidase C-terminal dimerization region; This domain represents one of the two dimerization regions of the protein, located at the edge of the dimer interface, at the C-terminus, being the last three beta strands, S6, S7, and S8 along with the last three residues to the end. In Swiss:P21159, S6 runs from residues 178-192, S7 from 200-206 and S8 from 211-215. the extended loop, of residues 167-177 may well be involved in the pocket formed between the two dimers that positions the FMN molecule.To date, the only time functional oxidase or phenazine biosynthesis activities have been experimentally demonstrated is when the sequences contain both pfam01243 and pfam10590. It is unknown the role performed by each domain in bringing about molecular functions of either oxidase or phenazine activity.


Pssm-ID: 463161  Cd Length: 42  Bit Score: 85.25  E-value: 9.01e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2065838525 486 WGGFRLKPNLFEFWQGQPSRLHDRLQYSLQDvngNPAWKIHRLAP 530
Cdd:pfam10590   1 WGGYRLVPEEIEFWQGRPSRLHDRIRYTREG---DGGWTIERLAP 42
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
72-267 8.30e-12

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 67.39  E-value: 8.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525  72 PLSYLTQREAAEIDEtlmgpLGFSIDQLMELAGLSvAASIAEVYKPEEySRVLAICGPGNNGGDGLVAARhlhhfgykpf 151
Cdd:PRK10565   19 PADDIRRGEREAADA-----LGLTLYELMLRAGEA-AFQVARSAYPDA-RHWLVLCGHGNNGGDGYVVAR---------- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 152 icypkrtakplytglVTQLDSLSVPFVSVED---LPDD---------------------LSKDFDVIVDAMFGFSFHGAP 207
Cdd:PRK10565   82 ---------------LAQAAGIDVTLLAQESdkpLPEEaalareawlnaggeihaadivWPESVDLIVDALLGTGLRQAP 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2065838525 208 RPPFDDLIRRlvslqnyeqtLQKHPV-IVSVDIPSGWHVEEGDHEDGGIKPDMLVSLTAPK 267
Cdd:PRK10565  147 REPYAALIDQ----------ANAHPApVVALDIPSGLLAETGATPGAVINADHTVTFIALK 197
YzzA COG3871
General stress protein 26 (function unknown) [Function unknown];
348-428 8.31e-04

General stress protein 26 (function unknown) [Function unknown];


Pssm-ID: 443080 [Multi-domain]  Cd Length: 132  Bit Score: 39.53  E-value: 8.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065838525 348 EAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENGFVWF-TNYESKKGSDLSENPSAALLFYWEILNRQVRIEGPVE 426
Cdd:COG3871     9 EKLWELLEDIRTAMLATVDADGRPHSRPMWFQVDVDDGTLWFfTSRDSAKVRNIRRDPRVSLSFADPGDDRYVSVEGTAE 88

                  ..
gi 2065838525 427 RI 428
Cdd:COG3871    89 IV 90
 
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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