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Conserved domains on  [gi|1773393088|pdb|6UTT|E]
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Protein Classification

ATP-dependent sacrificial sulfur transferase LarE( domain architecture ID 11446711)

ATP-dependent sacrificial sulfur transferase LarE catalyzes the ATP-dependent incorporation of two sulfur atoms in pyridinium-3,5-biscarboxylic acid mononucleotide (P2CMN) to yield pyridinium-3,5-bisthiocarboxylic acid mononucleotide (P2TMN)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG1606 COG1606
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
4-267 3.03e-125

ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];


:

Pssm-ID: 441214 [Multi-domain]  Cd Length: 265  Bit Score: 357.50  E-value: 3.03e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E        4 LATKKATLVAALKDLQRVTVAFSGGIDSTLVLKMALDVLGrDNVTAVVANSELFTDEEFDKAMSLAEELGANVQGTTLDY 83
Cdd:COG1606   1 LEEKLERLKAILKELGSVLVAFSGGVDSTLLAKVAHDVLG-DRVLAVTADSPSLPERELEEAKELAKEIGIRHEVIETDE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E       84 LSDDHIKNNTPDSWYYAKKMFYSRLNDIAANNGSAAVLDGMIKNDENDYRPGLKARSEAGARSLLQEADFFKTDVRALAQ 163
Cdd:COG1606  80 LEDPEFVANPPDRCYHCKKELFSKLKELAKELGYAVVADGTNADDLGDYRPGLRAAKELGVRSPLAEAGLTKAEIRELAR 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E      164 ELGLTNWNKVASCSVSSRFPYGTTLTHDNIAQVMAAEKYLRSLGFPTVRVRFHNDIARIELPEARIGDFLV--FNDRVNR 241
Cdd:COG1606 160 ELGLPTWDKPSSACLASRIPYGEEITPEKLRRVERAEAFLRSLGFRQVRVRHHGDLARIEVPPEELERLLEeeLREEIVE 239

                       250       260
                ....*....|....*....|....*.
6UTT_E      242 QLQSLGFRYVTLDLGGFRSGRMNDTL 267
Cdd:COG1606 240 KLKELGFRYVTLDLEGYRSGSMNEVL 265
 
Name Accession Description Interval E-value
COG1606 COG1606
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
4-267 3.03e-125

ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];


Pssm-ID: 441214 [Multi-domain]  Cd Length: 265  Bit Score: 357.50  E-value: 3.03e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E        4 LATKKATLVAALKDLQRVTVAFSGGIDSTLVLKMALDVLGrDNVTAVVANSELFTDEEFDKAMSLAEELGANVQGTTLDY 83
Cdd:COG1606   1 LEEKLERLKAILKELGSVLVAFSGGVDSTLLAKVAHDVLG-DRVLAVTADSPSLPERELEEAKELAKEIGIRHEVIETDE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E       84 LSDDHIKNNTPDSWYYAKKMFYSRLNDIAANNGSAAVLDGMIKNDENDYRPGLKARSEAGARSLLQEADFFKTDVRALAQ 163
Cdd:COG1606  80 LEDPEFVANPPDRCYHCKKELFSKLKELAKELGYAVVADGTNADDLGDYRPGLRAAKELGVRSPLAEAGLTKAEIRELAR 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E      164 ELGLTNWNKVASCSVSSRFPYGTTLTHDNIAQVMAAEKYLRSLGFPTVRVRFHNDIARIELPEARIGDFLV--FNDRVNR 241
Cdd:COG1606 160 ELGLPTWDKPSSACLASRIPYGEEITPEKLRRVERAEAFLRSLGFRQVRVRHHGDLARIEVPPEELERLLEeeLREEIVE 239

                       250       260
                ....*....|....*....|....*.
6UTT_E      242 QLQSLGFRYVTLDLGGFRSGRMNDTL 267
Cdd:COG1606 240 KLKELGFRYVTLDLEGYRSGSMNEVL 265
LarE-like cd01990
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ...
 20-241 2.39e-97

Lactate racemization operon protein LarE and similar proteins; This subfamily includes Lactiplantibacillus plantarum LarE, a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family. LarE is part of the lar operon, encoding five Lar proteins (LarA-E) that collaboratively synthesize and incorporate a niacin-derived Ni-containing cofactor into LarA, an Ni-dependent lactate racemase. It catalyzes successive thiolation reactions by donating the sulfur atom of their exclusive cysteine residues to the substrate. The LarE-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. Proteins from this subfamily probably binds ATP. This domain is about 200 amino acids long with a strongly conserved motif SGGxDS at the N-terminus.


Pssm-ID: 467494 [Multi-domain]  Cd Length: 222  Bit Score: 285.31  E-value: 2.39e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E       20 RVTVAFSGGIDSTLVLKMALDVLGrDNVTAVVANSELFTDEEFDKAMSLAEELGANVQGTTLDYLSDDHIKNNTPDSWYY 99
Cdd:cd01990   1 KVVVAFSGGVDSSLLAKLAKEVLG-DNVVAVTADSPLVPREELEEAKRIAEEIGIRHEIIKTDELDDEEYVANDPDRCYH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E      100 AKKMFYSRLNDIAANNGSAAVLDGMIKNDENDYRPGLKARSEAGARSLLQEADFFKTDVRALAQELGLTNWNKVASCSVS 179
Cdd:cd01990  80 CKKALYSTLKEIAKERGYDVVLDGTNADDLKDYRPGLLAAAELGIRSPLPELGLTKSEIRELARELGLPNWDKPASACLA 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
6UTT_E      180 SRFPYGTTLTHDNIAQVM-AAEKYLRSLGFPTVRVRFHNDIARIELPEARIGDFLVFNDRVNR 241
Cdd:cd01990 160 SRIPYGEEITPERLKRIEkAEELYLRLLGFRQVRVRHHGDIARIEVLDEEIESLLDKELREII 222
TIGR00268 TIGR00268
TIGR00268 family protein; The N-terminal region of the model shows similarity to ...
 15-261 2.65e-55

TIGR00268 family protein; The N-terminal region of the model shows similarity to Argininosuccinate synthase proteins using PSI-blast and using the recognize protein identification server. [Hypothetical proteins, Conserved]


Pssm-ID: 129369  Cd Length: 252  Bit Score: 179.22  E-value: 2.65e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E         15 LKDLQRVTVAFSGGIDSTLVLKMALDVLgrDNVTAVVANSELFTDEEFDKAMSLAEELGANVQGTTLDYLSDDHiKNNTP 94
Cdd:TIGR00268   9 LKEFKKVLIAYSGGVDSSLLAAVCSDAG--TEVLAITVVSPSISPRELEDAIIIAKEIGVNHEFVKIDKMINPF-RANVE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E         95 DSWYYAKKMFYSRLNDIAANNGSAAVLDGMIKNDENDYRPGLKARSEAGARSLLQEADFFKTDVRALAQELGLTNWNKVA 174
Cdd:TIGR00268  86 ERCYFCKKMVLSILVKEAEKRGYDVVVDGTNADDLFDHRPGYRAVKEFNGVSPWAEFGITKKEIREIAKSLGISFPDKPS 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E        175 SCSVSSRFPYGTTLTHDNIAQVMAAEKYLRSLGFPTVRVRFHNDIARIELPEARIGDFLVFNDRVNRQLQSLGFRYVTLD 254
Cdd:TIGR00268 166 EACLASRFPFGREIDEEKLKMVDEAEEVLRNAGVGQVRVRNYDNLAVIEVPEDELSKLLNEAEEVRDKFKDIGFRKVLID 245


                  ....*..
6UTT_E        255 LGGFRSG 261
Cdd:TIGR00268 246 LEGYRSG 252
NAD_synthase pfam02540
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ...
 19-166 5.98e-09

NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is induced by stress factors such as heat shock and glucose limitation.


Pssm-ID: 396888 [Multi-domain]  Cd Length: 241  Bit Score: 55.47  E-value: 5.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E         19 QRVTVAFSGGIDSTLVLKMALDVLGRDNVTAVVANSELFTDEEFDKAMSLAEELGANVQGTTLDYL---SDDHIKNNTpd 95
Cdd:pfam02540  19 KGVVLGLSGGIDSSLVAYLAVKALGKENVLALIMPSSQSSEEDVQDALALAENLGIEYKTIDIKPIvraFSQLFQDAS-- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E         96 swyyakkmfysrlNDIAANNGSA---AVLDGMIKNDENDYRPGLKARSEA----------GARSLLQEADFFKTDVRALA 162
Cdd:pfam02540  97 -------------EDFAKGNLKArirMAILYYIANKFNYLVLGTGNKSELavgyftkygdGACDIAPIGDLYKTQVYELA 163


                  ....
6UTT_E        163 QELG 166
Cdd:pfam02540 164 RYLN 167
PRK13980 PRK13980
NAD synthetase; Provisional
 19-166 8.63e-08

NAD synthetase; Provisional


Pssm-ID: 184435 [Multi-domain]  Cd Length: 265  Bit Score: 52.13  E-value: 8.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E        19 QRVTVAFSGGIDSTLVLKMALDVLGRDNVTAVVANSELFTDEEFDKAMSLAEELGANVQGTTLDYLSDDHIKNNtPDSWY 98
Cdd:PRK13980  31 KGVVLGLSGGIDSAVVAYLAVKALGKENVLALLMPSSVSPPEDLEDAELVAEDLGIEYKVIEITPIVDAFFSAI-PDADR 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E        99 YAKKMFYSR-----LNDIAANNGsAAVLdgmikndendyrpGLKARSEA----------GARSLLQEADFFKTDVRALAQ 163
Cdd:PRK13980 110 LRVGNIMARtrmvlLYDYANREN-RLVL-------------GTGNKSELllgyftkygdGAVDLNPIGDLYKTQVRELAR 175


                 ...
6UTT_E       164 ELG 166
Cdd:PRK13980 176 HLG 178
 
Name Accession Description Interval E-value
COG1606 COG1606
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
4-267 3.03e-125

ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];


Pssm-ID: 441214 [Multi-domain]  Cd Length: 265  Bit Score: 357.50  E-value: 3.03e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E        4 LATKKATLVAALKDLQRVTVAFSGGIDSTLVLKMALDVLGrDNVTAVVANSELFTDEEFDKAMSLAEELGANVQGTTLDY 83
Cdd:COG1606   1 LEEKLERLKAILKELGSVLVAFSGGVDSTLLAKVAHDVLG-DRVLAVTADSPSLPERELEEAKELAKEIGIRHEVIETDE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E       84 LSDDHIKNNTPDSWYYAKKMFYSRLNDIAANNGSAAVLDGMIKNDENDYRPGLKARSEAGARSLLQEADFFKTDVRALAQ 163
Cdd:COG1606  80 LEDPEFVANPPDRCYHCKKELFSKLKELAKELGYAVVADGTNADDLGDYRPGLRAAKELGVRSPLAEAGLTKAEIRELAR 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E      164 ELGLTNWNKVASCSVSSRFPYGTTLTHDNIAQVMAAEKYLRSLGFPTVRVRFHNDIARIELPEARIGDFLV--FNDRVNR 241
Cdd:COG1606 160 ELGLPTWDKPSSACLASRIPYGEEITPEKLRRVERAEAFLRSLGFRQVRVRHHGDLARIEVPPEELERLLEeeLREEIVE 239

                       250       260
                ....*....|....*....|....*.
6UTT_E      242 QLQSLGFRYVTLDLGGFRSGRMNDTL 267
Cdd:COG1606 240 KLKELGFRYVTLDLEGYRSGSMNEVL 265
LarE-like cd01990
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ...
 20-241 2.39e-97

Lactate racemization operon protein LarE and similar proteins; This subfamily includes Lactiplantibacillus plantarum LarE, a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family. LarE is part of the lar operon, encoding five Lar proteins (LarA-E) that collaboratively synthesize and incorporate a niacin-derived Ni-containing cofactor into LarA, an Ni-dependent lactate racemase. It catalyzes successive thiolation reactions by donating the sulfur atom of their exclusive cysteine residues to the substrate. The LarE-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. Proteins from this subfamily probably binds ATP. This domain is about 200 amino acids long with a strongly conserved motif SGGxDS at the N-terminus.


Pssm-ID: 467494 [Multi-domain]  Cd Length: 222  Bit Score: 285.31  E-value: 2.39e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E       20 RVTVAFSGGIDSTLVLKMALDVLGrDNVTAVVANSELFTDEEFDKAMSLAEELGANVQGTTLDYLSDDHIKNNTPDSWYY 99
Cdd:cd01990   1 KVVVAFSGGVDSSLLAKLAKEVLG-DNVVAVTADSPLVPREELEEAKRIAEEIGIRHEIIKTDELDDEEYVANDPDRCYH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E      100 AKKMFYSRLNDIAANNGSAAVLDGMIKNDENDYRPGLKARSEAGARSLLQEADFFKTDVRALAQELGLTNWNKVASCSVS 179
Cdd:cd01990  80 CKKALYSTLKEIAKERGYDVVLDGTNADDLKDYRPGLLAAAELGIRSPLPELGLTKSEIRELARELGLPNWDKPASACLA 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
6UTT_E      180 SRFPYGTTLTHDNIAQVM-AAEKYLRSLGFPTVRVRFHNDIARIELPEARIGDFLVFNDRVNR 241
Cdd:cd01990 160 SRIPYGEEITPERLKRIEkAEELYLRLLGFRQVRVRHHGDIARIEVLDEEIESLLDKELREII 222
TIGR00268 TIGR00268
TIGR00268 family protein; The N-terminal region of the model shows similarity to ...
 15-261 2.65e-55

TIGR00268 family protein; The N-terminal region of the model shows similarity to Argininosuccinate synthase proteins using PSI-blast and using the recognize protein identification server. [Hypothetical proteins, Conserved]


Pssm-ID: 129369  Cd Length: 252  Bit Score: 179.22  E-value: 2.65e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E         15 LKDLQRVTVAFSGGIDSTLVLKMALDVLgrDNVTAVVANSELFTDEEFDKAMSLAEELGANVQGTTLDYLSDDHiKNNTP 94
Cdd:TIGR00268   9 LKEFKKVLIAYSGGVDSSLLAAVCSDAG--TEVLAITVVSPSISPRELEDAIIIAKEIGVNHEFVKIDKMINPF-RANVE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E         95 DSWYYAKKMFYSRLNDIAANNGSAAVLDGMIKNDENDYRPGLKARSEAGARSLLQEADFFKTDVRALAQELGLTNWNKVA 174
Cdd:TIGR00268  86 ERCYFCKKMVLSILVKEAEKRGYDVVVDGTNADDLFDHRPGYRAVKEFNGVSPWAEFGITKKEIREIAKSLGISFPDKPS 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E        175 SCSVSSRFPYGTTLTHDNIAQVMAAEKYLRSLGFPTVRVRFHNDIARIELPEARIGDFLVFNDRVNRQLQSLGFRYVTLD 254
Cdd:TIGR00268 166 EACLASRFPFGREIDEEKLKMVDEAEEVLRNAGVGQVRVRNYDNLAVIEVPEDELSKLLNEAEEVRDKFKDIGFRKVLID 245


                  ....*..
6UTT_E        255 LGGFRSG 261
Cdd:TIGR00268 246 LEGYRSG 252
NadE COG0171
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ...
 11-74 3.29e-09

NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ synthetase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439941 [Multi-domain]  Cd Length: 542  Bit Score: 57.16  E-value: 3.29e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E       11 LVAALKD------LQRVTVAFSGGIDSTLVLKMALDVLGRDNVTAVVANSELFTDEEFDKAMSLAEELGA 74
Cdd:COG0171 273 LVLGLRDyvrkngFKGVVLGLSGGIDSALVAALAVDALGPENVLGVTMPSRYTSDESLEDAEELAENLGI 342
NAD_synthase pfam02540
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ...
 19-166 5.98e-09

NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is induced by stress factors such as heat shock and glucose limitation.


Pssm-ID: 396888 [Multi-domain]  Cd Length: 241  Bit Score: 55.47  E-value: 5.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E         19 QRVTVAFSGGIDSTLVLKMALDVLGRDNVTAVVANSELFTDEEFDKAMSLAEELGANVQGTTLDYL---SDDHIKNNTpd 95
Cdd:pfam02540  19 KGVVLGLSGGIDSSLVAYLAVKALGKENVLALIMPSSQSSEEDVQDALALAENLGIEYKTIDIKPIvraFSQLFQDAS-- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E         96 swyyakkmfysrlNDIAANNGSA---AVLDGMIKNDENDYRPGLKARSEA----------GARSLLQEADFFKTDVRALA 162
Cdd:pfam02540  97 -------------EDFAKGNLKArirMAILYYIANKFNYLVLGTGNKSELavgyftkygdGACDIAPIGDLYKTQVYELA 163


                  ....
6UTT_E        163 QELG 166
Cdd:pfam02540 164 RYLN 167
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 21-71 5.99e-08

adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide alpha hydrolase (AANH)-like proteins includes N-type ATP PPases and ATP sulfurylases. The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.


Pssm-ID: 467490 [Multi-domain]  Cd Length: 74  Bit Score: 48.99  E-value: 5.99e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
6UTT_E       21 VTVAFSGGIDSTLVLKMALDVLGRDNVTAVVANSELFTDEEFDKAMSLAEE 71
Cdd:cd01986   1 VVVGYSGGKDSSVALHLASRLGRKAEVAVVHIDHGIGFKEEAESVASIARR 51
PRK13980 PRK13980
NAD synthetase; Provisional
 19-166 8.63e-08

NAD synthetase; Provisional


Pssm-ID: 184435 [Multi-domain]  Cd Length: 265  Bit Score: 52.13  E-value: 8.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E        19 QRVTVAFSGGIDSTLVLKMALDVLGRDNVTAVVANSELFTDEEFDKAMSLAEELGANVQGTTLDYLSDDHIKNNtPDSWY 98
Cdd:PRK13980  31 KGVVLGLSGGIDSAVVAYLAVKALGKENVLALLMPSSVSPPEDLEDAELVAEDLGIEYKVIEITPIVDAFFSAI-PDADR 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E        99 YAKKMFYSR-----LNDIAANNGsAAVLdgmikndendyrpGLKARSEA----------GARSLLQEADFFKTDVRALAQ 163
Cdd:PRK13980 110 LRVGNIMARtrmvlLYDYANREN-RLVL-------------GTGNKSELllgyftkygdGAVDLNPIGDLYKTQVRELAR 175


                 ...
6UTT_E       164 ELG 166
Cdd:PRK13980 176 HLG 178
PRK13981 PRK13981
NAD synthetase; Provisional
 11-73 5.56e-07

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 50.54  E-value: 5.56e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
6UTT_E        11 LVAALKD------LQRVTVAFSGGIDSTLVLKMALDVLGRDNVTAVVANSELFTDEEFDKAMSLAEELG 73
Cdd:PRK13981 267 LVLGLRDyvrkngFPGVVLGLSGGIDSALVAAIAVDALGAERVRAVMMPSRYTSEESLDDAAALAKNLG 335
nadE TIGR00552
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ...
 19-166 2.11e-06

NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the biosynthesis of the essensial cofactor NAD. The member of this family from Bacillus subtilis is a strictly NH(3)-dependent NAD(+) synthetase of 272 amino acids. Proteins consisting only of the domain modeled here may be named as NH3-dependent NAD+ synthetase. Amidotransferase activity may reside in a separate protein, or not be present. Some other members of the family, such as from Mycobacterium tuberculosis, are considerably longer, contain an apparent amidotransferase domain, and show glutamine-dependent as well as NH(3)-dependent activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]


Pssm-ID: 273132 [Multi-domain]  Cd Length: 250  Bit Score: 47.77  E-value: 2.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E         19 QRVTVAFSGGIDSTLVLKMALDVLGRDNVTAVVANSELFTDEEFDKAMSLAEELGAN---VQGTTLDYLSDDHIKNNTPD 95
Cdd:TIGR00552  23 KGVVLGLSGGIDSAVVAALCVEALGEQNHALLLPHSVQTPEQDVQDALALAEPLGINyknIDIAPIAASFQAQTETGDEL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E         96 SWYYAKKMFYSRLNDIA----ANNGSAAVLdgmikndendyrpGLKARSEA----------GARSLLQEADFFKTDVRAL 161
Cdd:TIGR00552 103 SDFLAKGNLKARLRMAAlyaiANKHNLLVL-------------GTGNKSELmlgyftkygdGGCDIAPIGDLFKTQVYEL 169


                  ....*
6UTT_E        162 AQELG 166
Cdd:TIGR00552 170 AKRLN 174
NAD_synthase cd00553
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ...
 11-73 2.17e-06

NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de novo nicotinamide adenine dinucleotide (NAD(+)) biosynthesis, an amide transfer from either ammonia or glutamine to nicotinic acid adenine dinucleotide (NaAD). The conversion of NaAD to NAD(+) occurs via a NAD-adenylate intermediate and requires ATP and Mg(2+). The intermediate is subsequently cleaved into NAD(+) and AMP. In many prokaryotes, such as Escherichia coli, NAD synthase consists of a single domain and is strictly ammonia dependent. In contrast, eukaryotes and other prokaryotes have an additional N-terminal amidohydrolase domain that prefer glutamine. Interestingly, NAD(+) synthases in these prokaryotes, can also utilize ammonia as an amide source.


Pssm-ID: 467484 [Multi-domain]  Cd Length: 248  Bit Score: 47.94  E-value: 2.17e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
6UTT_E       11 LVAALKD------LQRVTVAFSGGIDSTLVLKMALDVLGRDNVTAVVANSELFTDEEFDKAMSLAEELG 73
Cdd:cd00553  10 LVCFLRDylrksgAKGFVLGLSGGIDSAVVAALAVRALGAENVLALIMPSRYSSKETRDDAKALAENLG 78
Asn_synthase_B_C cd01991
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ...
 20-85 3.07e-05

C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or synthetase) B is always associated with an N-terminal amidotransferase domain. Family members that contain this domain catalyze the conversion of aspartate to asparagine. Asparagine synthase B catalyzes the synthesis of asparagine from aspartate, Mg(2+)ATP, and glutamine. The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase.


Pssm-ID: 467495 [Multi-domain]  Cd Length: 224  Bit Score: 44.19  E-value: 3.07e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
6UTT_E       20 RVTVAFSGGIDSTLVLKMALDVLGRDNVTAVVANSELFTDEEFDKAMSLAEELGAN---VQGTTLDYLS 85
Cdd:cd01991   4 PVGVLLSGGLDSSLIAALAARLLPETPIDLFTVGFEGSPTPDRAAARRVAEELGTEhheVEVTIEELLD 72
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 20-76 6.31e-05

uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to Escherichia coli YbdN; This subgroup contains Escherichia coli YbdN and other phosphoadenosine phosphosulfate (PAPS) reductase (or PAPS sulfotransferase EC 1.8.4.8)-like proteins. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N-type ATP PPases and ATP sulfurylases. A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP).


Pssm-ID: 467512 [Multi-domain]  Cd Length: 206  Bit Score: 43.15  E-value: 6.31e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
6UTT_E       20 RVTVAFSGGIDSTLVLKMALDVLGR--DNVTAVVANSELFTDEEFDKAMSLAEELGANV 76
Cdd:cd23947  14 PVIVSFSGGKDSLVLLHLALEALRRlrKDVYVVFIDTGIEFPETIDFVEKLAETLGLDV 72
TIGR00364 TIGR00364
queuosine biosynthesis protein QueC; Members of this protein family are QueC, involved in ...
 23-82 3.08e-03

queuosine biosynthesis protein QueC; Members of this protein family are QueC, involved in synthesizing pre-Q0 from GTP en route to tRNA modification with queuosine. This protein family is represented by a single member in nearly every completed large (> 1000 genes) prokaryotic genome. In Rhizobium meliloti, the gene was designated exsB, possibly because of polar effects on exsA expression in a shared polycistronic mRNA. In Arthrobacter viscosus, the homologous gene was designated ALU1 and was associated with an aluminum tolerance phenotype. [Unknown function, General]


Pssm-ID: 129461 [Multi-domain]  Cd Length: 201  Bit Score: 38.14  E-value: 3.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E         23 VAFSGGIDSTLVLKMALDvlGRDNVTAVVANSELFTDEEFDKAMSLAEELGanVQGTTLD 82
Cdd:TIGR00364   3 VVLSGGQDSTTCLLWAKD--EGYEVHAVTFDYGQRHSRELESARKIAEALG--IEHHLLD 58
PRK08576 PRK08576
hypothetical protein; Provisional
 20-76 3.45e-03

hypothetical protein; Provisional


Pssm-ID: 236300 [Multi-domain]  Cd Length: 438  Bit Score: 38.52  E-value: 3.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
6UTT_E        20 RVTVAFSGGIDSTLVLKMALDVLGRdnVTAVVANSE---LFTDEEFDKamsLAEELGANV 76
Cdd:PRK08576 236 TVIVPWSGGKDSTAALLLAKKAFGD--VTAVYVDTGyemPLTDEYVEK---VAEKLGVDL 290
 
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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