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Conserved domains on  [gi|15598130|ref|NP_251624|]
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CFTR inhibitory factor [Pseudomonas aeruginosa PAO1]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 11426811)

alpha/beta hydrolase family protein catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

PubMed:  1409539|12369917

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 35-317 2.25e-32

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


:

Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 119.72  E-value: 2.25e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130  35 ESAYREVDGVKLHYVKGG-QGPLVMLVHGFGQTWYEWHQLMPELAKRFTVIAPDLPGLGQSEPPKTGYSGEQVAVYLHKL 113
Cdd:COG0596   3 TPRFVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAAL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130 114 ARQFSPDRpFDLVAHDIGIWNTYPMVVKNQADIARLVYMEApipdariyrfpaftaqgeslvwhfsffaaddrlaetlia 193
Cdd:COG0596  83 LDALGLER-VVLVGHSMGGMVALELAARHPERVAGLVLVDE--------------------------------------- 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130 194 gkerfflehfikshssntevfserLLDLYARSYAKPHSLNASFeyYRALNESVRQNAELAKTRLQMPTMTLAGGGHGGMG 273
Cdd:COG0596 123 ------------------------VLAALAEPLRRPGLAPEAL--AALLRALARTDLRERLARITVPTLVIWGEKDPIVP 176

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15598130 274 TFQLEQMKAYADDVEGHVLPGCGHWLPEECAAPMNRLVIDFLSR 317
Cdd:COG0596 177 PALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 35-317 2.25e-32

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 119.72  E-value: 2.25e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130  35 ESAYREVDGVKLHYVKGG-QGPLVMLVHGFGQTWYEWHQLMPELAKRFTVIAPDLPGLGQSEPPKTGYSGEQVAVYLHKL 113
Cdd:COG0596   3 TPRFVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAAL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130 114 ARQFSPDRpFDLVAHDIGIWNTYPMVVKNQADIARLVYMEApipdariyrfpaftaqgeslvwhfsffaaddrlaetlia 193
Cdd:COG0596  83 LDALGLER-VVLVGHSMGGMVALELAARHPERVAGLVLVDE--------------------------------------- 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130 194 gkerfflehfikshssntevfserLLDLYARSYAKPHSLNASFeyYRALNESVRQNAELAKTRLQMPTMTLAGGGHGGMG 273
Cdd:COG0596 123 ------------------------VLAALAEPLRRPGLAPEAL--AALLRALARTDLRERLARITVPTLVIWGEKDPIVP 176

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15598130 274 TFQLEQMKAYADDVEGHVLPGCGHWLPEECAAPMNRLVIDFLSR 317
Cdd:COG0596 177 PALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 55-302 1.63e-15

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 74.85  E-value: 1.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130    55 PLVMLVHGFGQTWYEWHQLMPELAK-RFTVIAPDLPGLGQSEPPK--TGYSGEQVAVYLHKLaRQFSPDRPFDLVAHDIG 131
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARdGFRVIALDLRGFGKSSRPKaqDDYRTDDLAEDLEYI-LEALGLEKVNLVGHSMG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130   132 ---IWNtypMVVKNQADIARLVYMEAPIPDARIyrFPAFTAQGESLVWHFSFFAADD-RLAETLIAGKERFFLEHFIKSH 207
Cdd:pfam00561  80 gliALA---YAAKYPDRVKALVLLGALDPPHEL--DEADRFILALFPGFFDGFVADFaPNPLGRLVAKLLALLLLRLRLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130   208 SSNTEVFSERLLDLYARSYAKPHSLNASFEYYRALNESVRQNaelaktRLQMPTMTLAGGGHGGMGTFQLEQMKAYADDV 287
Cdd:pfam00561 155 KALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLG------RLDEPTLIIWGDQDPLVPPQALEKLAQLFPNA 228

                         250
                  ....*....|....*
gi 15598130   288 EGHVLPGCGHWLPEE 302
Cdd:pfam00561 229 RLVVIPDAGHFAFLE 243
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 28-242 1.53e-13

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 69.64  E-value: 1.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130   28 FPVPNGFESAYREVDGVKLHYVKGGQGPLVMLVHGFGQTWYEWHQLMPELAKRFTVIAPDLPGLGQSEPPKTGYSGEQVA 107
Cdd:PRK03592   1 FGVEPPGEMRRVEVLGSRMAYIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKPDIDYTFADHA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130  108 VYLHKLARQFSPDRPFdLVAHDIGIWNTYPMVVKNQADIARLVYMEAPIPDARIYRFPAFTAQgeslvwhfsFFAA--DD 185
Cdd:PRK03592  81 RYLDAWFDALGLDDVV-LVGHDWGSALGFDWAARHPDRVRGIAFMEAIVRPMTWDDFPPAVRE---------LFQAlrSP 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15598130  186 RLAETLIAgKERFFLEHFIksHSSNTEVFSERLLDLYARSYAKPHSLNASFEYYRAL 242
Cdd:PRK03592 151 GEGEEMVL-EENVFIERVL--PGSILRPLSDEEMAVYRRPFPTPESRRPTLSWPREL 204
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 53-126 8.27e-07

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 274729 [Multi-domain]  Cd Length: 252  Bit Score: 49.52  E-value: 8.27e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598130    53 QGPLVMLvHGFGQTWYEWHQLMPELAKRFTVIAPDLPGLGQSEPPKTG--YSGEQVAVY-LHKLARQFsPDRPFDLV 126
Cdd:TIGR03695   2 KPVLVFL-HGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSDIerYDFEEAAQLlLATLLDQL-GIEPFFLV 76
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 35-317 2.25e-32

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 119.72  E-value: 2.25e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130  35 ESAYREVDGVKLHYVKGG-QGPLVMLVHGFGQTWYEWHQLMPELAKRFTVIAPDLPGLGQSEPPKTGYSGEQVAVYLHKL 113
Cdd:COG0596   3 TPRFVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAAL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130 114 ARQFSPDRpFDLVAHDIGIWNTYPMVVKNQADIARLVYMEApipdariyrfpaftaqgeslvwhfsffaaddrlaetlia 193
Cdd:COG0596  83 LDALGLER-VVLVGHSMGGMVALELAARHPERVAGLVLVDE--------------------------------------- 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130 194 gkerfflehfikshssntevfserLLDLYARSYAKPHSLNASFeyYRALNESVRQNAELAKTRLQMPTMTLAGGGHGGMG 273
Cdd:COG0596 123 ------------------------VLAALAEPLRRPGLAPEAL--AALLRALARTDLRERLARITVPTLVIWGEKDPIVP 176

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15598130 274 TFQLEQMKAYADDVEGHVLPGCGHWLPEECAAPMNRLVIDFLSR 317
Cdd:COG0596 177 PALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 55-302 1.63e-15

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 74.85  E-value: 1.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130    55 PLVMLVHGFGQTWYEWHQLMPELAK-RFTVIAPDLPGLGQSEPPK--TGYSGEQVAVYLHKLaRQFSPDRPFDLVAHDIG 131
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARdGFRVIALDLRGFGKSSRPKaqDDYRTDDLAEDLEYI-LEALGLEKVNLVGHSMG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130   132 ---IWNtypMVVKNQADIARLVYMEAPIPDARIyrFPAFTAQGESLVWHFSFFAADD-RLAETLIAGKERFFLEHFIKSH 207
Cdd:pfam00561  80 gliALA---YAAKYPDRVKALVLLGALDPPHEL--DEADRFILALFPGFFDGFVADFaPNPLGRLVAKLLALLLLRLRLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130   208 SSNTEVFSERLLDLYARSYAKPHSLNASFEYYRALNESVRQNaelaktRLQMPTMTLAGGGHGGMGTFQLEQMKAYADDV 287
Cdd:pfam00561 155 KALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLG------RLDEPTLIIWGDQDPLVPPQALEKLAQLFPNA 228

                         250
                  ....*....|....*
gi 15598130   288 EGHVLPGCGHWLPEE 302
Cdd:pfam00561 229 RLVVIPDAGHFAFLE 243
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 28-242 1.53e-13

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 69.64  E-value: 1.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130   28 FPVPNGFESAYREVDGVKLHYVKGGQGPLVMLVHGFGQTWYEWHQLMPELAKRFTVIAPDLPGLGQSEPPKTGYSGEQVA 107
Cdd:PRK03592   1 FGVEPPGEMRRVEVLGSRMAYIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKPDIDYTFADHA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130  108 VYLHKLARQFSPDRPFdLVAHDIGIWNTYPMVVKNQADIARLVYMEAPIPDARIYRFPAFTAQgeslvwhfsFFAA--DD 185
Cdd:PRK03592  81 RYLDAWFDALGLDDVV-LVGHDWGSALGFDWAARHPDRVRGIAFMEAIVRPMTWDDFPPAVRE---------LFQAlrSP 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15598130  186 RLAETLIAgKERFFLEHFIksHSSNTEVFSERLLDLYARSYAKPHSLNASFEYYRAL 242
Cdd:PRK03592 151 GEGEEMVL-EENVFIERVL--PGSILRPLSDEEMAVYRRPFPTPESRRPTLSWPREL 204
PRK05855 PRK05855
SDR family oxidoreductase;
41-133 4.48e-13

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 69.62  E-value: 4.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130   41 VDGVKLHYVKGGQ--GPLVMLVHGFGQTWYEWHQLMPELAKRFTVIAPDLPGLGQSEPPKT--GYSGEQVAVYLHKLARQ 116
Cdd:PRK05855  10 SDGVRLAVYEWGDpdRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRtaAYTLARLADDFAAVIDA 89

                         90       100
                 ....*....|....*....|
gi 15598130  117 FSPDRPFDLVAHD---IGIW 133
Cdd:PRK05855  90 VSPDRPVHLLAHDwgsIQGW 109
PLN02578 PLN02578
hydrolase
 43-131 1.20e-12

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 67.56  E-value: 1.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130   43 GVKLHYVKGGQGPLVMLVHGFGQTWYEWHQLMPELAKRFTVIAPDLPGLGQSEPPKTGYSG----EQVAVYLHKLARqfs 118
Cdd:PLN02578  75 GHKIHYVVQGEGLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAmvwrDQVADFVKEVVK--- 151

                         90
                 ....*....|...
gi 15598130  119 pdRPFDLVAHDIG 131
Cdd:PLN02578 152 --EPAVLVGNSLG 162
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 57-305 4.58e-09

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 55.56  E-value: 4.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130    57 VMLVHGFgqtWYEWHQLMPELAKRFTVIAPDLPGLGQSEPPKTGYSGEQVavyLHKLARQFSPDRPFDLVAHDIGiwnTY 136
Cdd:pfam12697   1 VVLVHGA---GLSAAPLAALLAAGVAVLAPDLPGHGSSSPPPLDLADLAD---LAALLDELGAARPVVLVGHSLG---GA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130   137 PMVVKNQADIARLVYMEAPIPDARIYRFPAFTAQGESLVWHFSFFAADDRLAETLIAGkerfflehfikshssntevfsE 216
Cdd:pfam12697  72 VALAAAAAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDD---------------------L 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130   217 RLLDLYARSYAKPHSLNASFEYYRALNesvrqnaelaktRLQMPTMTLAGGGHGGMGTFQLEQMKAYADDVEGHVLPGCG 296
Cdd:pfam12697 131 PADAEWAAALARLAALLAALALLPLAA------------WRDLPVPVLVLAEEDRLVPELAQRLLAALAGARLVVLPGAG 198

                         250
                  ....*....|..
gi 15598130   297 HWL---PEECAA 305
Cdd:pfam12697 199 HLPlddPEEVAE 210
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
42-131 1.01e-08

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 54.62  E-value: 1.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130  42 DGVKLHYVK----GGQGPLVMLVHGFGQTWYEWHQLMPELAKR-FTVIAPDLPGLGQSEPPKTGYSG-EQVAVYLHKLAR 115
Cdd:COG2267  12 DGLRLRGRRwrpaGSPRGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHVDSfDDYVDDLRAALD 91

                        90
                ....*....|....*...
gi 15598130 116 QFS--PDRPFDLVAHDIG 131
Cdd:COG2267  92 ALRarPGLPVVLLGHSMG 109
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 57-128 8.83e-08

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 49.44  E-value: 8.83e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598130  57 VMLVHGFGQTWYEWHQLMPELAKR-FTVIAPDLPGLGQSEPPktgySGEQVAVYLHKLARQfSPDRPFDLVAH 128
Cdd:COG1075   8 VVLVHGLGGSAASWAPLAPRLRAAgYPVYALNYPSTNGSIED----SAEQLAAFVDAVLAA-TGAEKVDLVGH 75
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 51-97 4.37e-07

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 50.51  E-value: 4.37e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 15598130   51 GGQGPLVMLVHGFGQTWYEWHQLMPELAKRFTVIAPDLPGLGQSEPP 97
Cdd:PLN02824  26 GTSGPALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKP 72
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 54-131 5.51e-07

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 50.61  E-value: 5.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130   54 GPLVMLVHGFGQTWYEWHQLMPELAKRFTVIAPDLPGLGQSE-PPKTGYS----GEQVAVYLHKLARqfspdRPFDLVAH 128
Cdd:PLN02679  88 GPPVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDkPPGFSYTmetwAELILDFLEEVVQ-----KPTVLIGN 162


                 ...
gi 15598130  129 DIG 131
Cdd:PLN02679 163 SVG 165
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 53-126 8.27e-07

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 274729 [Multi-domain]  Cd Length: 252  Bit Score: 49.52  E-value: 8.27e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598130    53 QGPLVMLvHGFGQTWYEWHQLMPELAKRFTVIAPDLPGLGQSEPPKTG--YSGEQVAVY-LHKLARQFsPDRPFDLV 126
Cdd:TIGR03695   2 KPVLVFL-HGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSDIerYDFEEAAQLlLATLLDQL-GIEPFFLV 76
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 40-96 1.07e-06

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 49.56  E-value: 1.07e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15598130   40 EVDGVKLHYVKGGQ--GPLVMLVHGFGQTWYEWHQLMPELAKRFTVIAPDLPGLGQSEP 96
Cdd:PRK14875 115 RIGGRTVRYLRLGEgdGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSK 173
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 34-97 8.38e-06

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 46.50  E-value: 8.38e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598130   34 FESAYREVDG-----VKLHYVKGGQ--GPLVMLVHGfGQTW-YEWHQLMPELAKR-FTVIAPDLPGLGQSEPP 97
Cdd:PRK00870  19 FAPHYVDVDDgdggpLRMHYVDEGPadGPPVLLLHG-EPSWsYLYRKMIPILAAAgHRVIAPDLIGFGRSDKP 90
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 48-158 3.66e-05

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 44.87  E-value: 3.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130   48 YVKGG--QGPLVMLVHGFGQTWYEWHQLMPELAKRFTVIAPDLPGLGQSEPPKTG----YSGEQVAVYLHKLARQFSPDR 121
Cdd:PLN03084 119 CVESGsnNNPPVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDKPQPGygfnYTLDEYVSSLESLIDELKSDK 198

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 15598130  122 pFDLVAHdiGIWNtyPMVVK----NQADIARLVYMEAPIPD 158
Cdd:PLN03084 199 -VSLVVQ--GYFS--PPVVKyasaHPDKIKKLILLNPPLTK 234
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 34-131 3.99e-05

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 44.46  E-value: 3.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130   34 FESAYREVDGVKLHYVKGGQGPLVMLVHGfGQTW-YEWHQLMPELAKRFTVIAPDLPGLGQSEPPKT-GYSGEQVAVYLH 111
Cdd:PRK03204  14 FESRWFDSSRGRIHYIDEGTGPPILLCHG-NPTWsFLYRDIIVALRDRFRCVAPDYLGFGLSERPSGfGYQIDEHARVIG 92

                         90       100
                 ....*....|....*....|
gi 15598130  112 KLARQFSPDRpFDLVAHDIG 131
Cdd:PRK03204  93 EFVDHLGLDR-YLSMGQDWG 111
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
38-95 8.21e-05

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 43.08  E-value: 8.21e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598130  38 YREVDGVKLHYV-----KGGQGPLVMLVHGFGQT-WYEWHQLMPELAKR-FTVIAPDLPGLGQSE 95
Cdd:COG1506   2 FKSADGTTLPGWlylpaDGKKYPVVVYVHGGPGSrDDSFLPLAQALASRgYAVLAPDYRGYGESA 66
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 52-94 2.46e-04

pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273783 [Multi-domain]  Cd Length: 245  Bit Score: 41.73  E-value: 2.46e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 15598130    52 GQG-PLVMLVHGFGQTWYEWHQLMPELAKRFTVIAPDLPGLGQS 94
Cdd:TIGR01738   1 GQGnVHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRS 44
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
57-92 2.53e-04

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 41.85  E-value: 2.53e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 15598130  57 VMLVHGFGQTWYEWHQLMPELAKR-FTVIAPDLPGLG 92
Cdd:COG1647  18 VLLLHGFTGSPAEMRPLAEALAKAgYTVYAPRLPGHG 54
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
52-147 6.00e-04

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 40.77  E-value: 6.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130   52 GQGPL-VMLVHGFGQTWYEWHQLMPELAKRFTVIAPDLPGLGQSeppkTGYSGEQVAVYLHKLARQfSPDRPF------- 123
Cdd:PRK10349  10 GQGNVhLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRS----RGFGALSLADMAEAVLQQ-APDKAIwlgwslg 84

                         90       100
                 ....*....|....*....|....
gi 15598130  124 DLVAHDIGIwnTYPMVVKNQADIA 147
Cdd:PRK10349  85 GLVASQIAL--THPERVQALVTVA 106
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 40-228 1.16e-03

2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 40.61  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130    40 EVDG----VKLHYV-KGGQGPLVMLVHGFGQTWYEWHQLMPELAKRFTVIAPDLPGLGQSEPPKTG--------YSGEQV 106
Cdd:PLN02980 1352 DVDGfsclIKVHEVgQNAEGSVVLFLHGFLGTGEDWIPIMKAISGSARCISIDLPGHGGSKIQNHAketqteptLSVELV 1431

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130   107 AVYLHKLARQFSPDRpFDLVAHDIGIWNTYPMVVKNQADIARLVYMEAPI----PDARIYRfpaftaqgeslvwhfsfFA 182
Cdd:PLN02980 1432 ADLLYKLIEHITPGK-VTLVGYSMGARIALYMALRFSDKIEGAVIISGSPglkdEVARKIR-----------------SA 1493

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15598130   183 ADDRLAETLIAGKERFFLEHF--------IKSHSSNTEVFSERLLDLYARSYAK 228
Cdd:PLN02980 1494 KDDSRARMLIDHGLEIFLENWysgelwksLRNHPHFNKIVASRLLHKDVPSLAK 1547
PRK06489 PRK06489
hypothetical protein; Provisional
 5-100 5.79e-03

hypothetical protein; Provisional


Pssm-ID: 235815 [Multi-domain]  Cd Length: 360  Bit Score: 38.04  E-value: 5.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598130    5 RLCRGLLAGIALTFSLGGFAAEEFPVPN---------GFESAyREVDGVKLHYV---------KGGQGPLVMLVHGFGQT 66
Cdd:PRK06489   3 RLLLTLLAALLLPLSVSAAAAAAYPAPQegdwvardfTFHSG-ETLPELRLHYTtlgtphrnaDGEIDNAVLVLHGTGGS 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 15598130   67 WYEW--HQLMPEL--------AKRFTVIAPDLPGLGQSEPPKTG 100
Cdd:PRK06489  82 GKSFlsPTFAGELfgpgqpldASKYFIILPDGIGHGKSSKPSDG 125
 
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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