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Conserved domains on  [gi|1473377617|ref|WP_117841813|]
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MULTISPECIES: phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase [unclassified Roseburia]

Protein Classification

beta/alpha barrel domain-containing protein( domain architecture ID 229392)

beta/alpha barrel domain-containing protein belongs to a large superfamily with a wide variety of enzymatic functions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TIM super family cl21457
TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate ...
 1-258 1.03e-133

TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate isomerase (TIM) which, in general, share an eight beta/alpha closed barrel structure.


The actual alignment was detected with superfamily member PLN02446:

Pssm-ID: 473867  Cd Length: 262  Bit Score: 377.89  E-value: 1.03e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617   1 MEFRPCIDIHNGKVKQIVGGSLKD------EGNQAKENFVAEQDAAYFAEFYKKDKICGGHIILLNPADSSyyketKRQA 74
Cdd:PLN02446    1 VRFRPCIDIHKGKVKQIVGSTLKDskdgseDGSELVTNFESDKSAAEFAEMYKRDGLTGGHVIMLGADDAS-----LAAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617  75 LLALHTYPGGMQVGGGIHAENAKEFIEAGASHVIVTSYVFKDGKVNYNNLEKILAAVGKEHLVLDLSCRKKDGDYYIVTD 154
Cdd:PLN02446   76 LEALRAYPGGLQVGGGVNSENAMSYLDAGASHVIVTSYVFRDGQIDLERLKDLVRLVGKQRLVLDLSCRKKDGRYYVVTD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617 155 RWQKFTEEKITPELLDKLKEYADEFLVHAVDVEGKASGIEVPLAEMLGDWGRIPITYAGGVGSFEDLKQLKEHGKGRLNV 234
Cdd:PLN02446  156 RWQKFSDLAVDEETLEFLAAYCDEFLVHGVDVEGKRLGIDEELVALLGEHSPIPVTYAGGVRSLDDLERVKVAGGGRVDV 235

                         250       260
                  ....*....|....*....|....
gi 1473377617 235 TIGSALDLFGGRMAYKEVLQYINQ 258
Cdd:PLN02446  236 TVGSALDIFGGNLPYDDVVAWHKQ 259
 
Name Accession Description Interval E-value
PLN02446 PLN02446
(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 1-258 1.03e-133

(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase


Pssm-ID: 215245  Cd Length: 262  Bit Score: 377.89  E-value: 1.03e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617   1 MEFRPCIDIHNGKVKQIVGGSLKD------EGNQAKENFVAEQDAAYFAEFYKKDKICGGHIILLNPADSSyyketKRQA 74
Cdd:PLN02446    1 VRFRPCIDIHKGKVKQIVGSTLKDskdgseDGSELVTNFESDKSAAEFAEMYKRDGLTGGHVIMLGADDAS-----LAAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617  75 LLALHTYPGGMQVGGGIHAENAKEFIEAGASHVIVTSYVFKDGKVNYNNLEKILAAVGKEHLVLDLSCRKKDGDYYIVTD 154
Cdd:PLN02446   76 LEALRAYPGGLQVGGGVNSENAMSYLDAGASHVIVTSYVFRDGQIDLERLKDLVRLVGKQRLVLDLSCRKKDGRYYVVTD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617 155 RWQKFTEEKITPELLDKLKEYADEFLVHAVDVEGKASGIEVPLAEMLGDWGRIPITYAGGVGSFEDLKQLKEHGKGRLNV 234
Cdd:PLN02446  156 RWQKFSDLAVDEETLEFLAAYCDEFLVHGVDVEGKRLGIDEELVALLGEHSPIPVTYAGGVRSLDDLERVKVAGGGRVDV 235

                         250       260
                  ....*....|....*....|....
gi 1473377617 235 TIGSALDLFGGRMAYKEVLQYINQ 258
Cdd:PLN02446  236 TVGSALDIFGGNLPYDDVVAWHKQ 259
hisA_euk TIGR02129
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, eukaryotic type; This ...
 3-255 5.29e-109

phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, eukaryotic type; This enzyme acts in the biosynthesis of histidine and has been characterized in S. cerevisiae and Arabidopsis where it complements the E. coli HisA gene. In eukaryotes the gene is known as HIS6. In bacteria, this gene is found in Fibrobacter succinogenes, presumably due to lateral gene transfer from plants in the rumen gut. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 162719  Cd Length: 253  Bit Score: 314.80  E-value: 5.29e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617   3 FRPCIDIHNGKVKQIVGGSLKDE-GNQAKENFVAEQDAAYFAEFYKKDKICGGHIILLNPADSSyyketkrQALLALHTY 81
Cdd:TIGR02129   3 FRPCIDIHNGKVKQIVGGTLTSKkGSVLKTNFVSDKPSSYYAKLYKDDGVKGCHVIMLGPNNDD-------AAKEALHAY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617  82 PGGMQVGGGIHAENAKEFIEAGASHVIVTSYVFKDGKVNYNNLEKILAAVGKEHLVLDLSCRKK-DGDYYIVTDRWQKFT 160
Cdd:TIGR02129  76 PGGLQVGGGINDTNAQEWLDEGASHVIVTSWLFTKGKFDLKRLKEIVSLVGKDRLIVDLSCRKTqDGRWIVAMNKWQTIT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617 161 EEKITPELLDKLKEYADEFLVHAVDVEGKASGIEVPLAEMLGDWGRIPITYAGGVGSFEDLKQLKEHGKGRLNVTIGSAL 240
Cdd:TIGR02129 156 DLELNAETLEELSKYCDEFLIHAADVEGLCKGIDEELVSKLGEWSPIPITYAGGAKSIDDLDLVDELSKGKVDLTIGSAL 235

                         250
                  ....*....|....*.
gi 1473377617 241 DLFGGR-MAYKEVLQY 255
Cdd:TIGR02129 236 DIFGGNlVKFTDCVAW 251
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 2-254 1.10e-60

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) and the cyclase subunit of imidazoleglycerol phosphate synthase (HisF). The ProFAR isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene. The Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.


Pssm-ID: 240074 [Multi-domain]  Cd Length: 233  Bit Score: 191.33  E-value: 1.10e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617   2 EFRPCIDIHNGKVKQIVGGSLKDEGnQAKENFVAEQDAAYFAEFYKKDKICGGHIILLNPADSSyyKETKRQALLALHTY 81
Cdd:cd04723     1 RIIPVIDLKDGVVVHGVGGDRDNYR-PITSNLCSTSDPLDVARAYKELGFRGLYIADLDAIMGR--GDNDEAIRELAAAW 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617  82 PGGMQVGGGIHA-ENAKEFIEAGASHVIVTSYVFKDGkvnynNLEKILAAVGKEHLVLDLSCRKKDGDyyivtdrwqKFT 160
Cdd:cd04723    78 PLGLWVDGGIRSlENAQEWLKRGASRVIVGTETLPSD-----DDEDRLAALGEQRLVLSLDFRGGQLL---------KPT 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617 161 EEKITPELLDKLKEYADEFLVHAVDVEGKASGIEVPLAEMLGDWGRIPITYAGGVGSFEDLKQLKEhgKGRLNVTIGSAL 240
Cdd:cd04723   144 DFIGPEELLRRLAKWPEELIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGGVRSVEDLELLKK--LGASGALVASAL 221

                         250
                  ....*....|....
gi 1473377617 241 DlfGGRMAYKEVLQ 254
Cdd:cd04723   222 H--DGGLTLEDVVR 233
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 2-257 1.11e-55

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino acid transport and metabolism]; Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439876  Cd Length: 236  Bit Score: 178.69  E-value: 1.11e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617   2 EFRPCIDIHNGKVKQIVGGSLKDEgnqakenFVAEQDAAYFAEFYKKDKICGGHIILLNPADSsyyKETKRQALLA--LH 79
Cdd:COG0106     1 IIIPAIDLKDGKCVRLVQGDYDQE-------TVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFA---GKPVNLELIEeiAK 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617  80 TYPGGMQVGGGIH-AENAKEFIEAGASHVIVTSYVFKDGKVnynnLEKILAAVGkEHLVLDLSCRkkdgDYYIVTDRWQK 158
Cdd:COG0106    71 ATGLPVQVGGGIRsLEDIERLLDAGASRVILGTAAVKDPEL----VKEALEEFP-ERIVVGLDAR----DGKVATDGWQE 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617 159 FTEEKITPELLDKLKEYADEFLVHAVDVEGKASGIEVPLAEMLGDWGRIPITYAGGVGSFEDLKQLKEHgkGRLNVTIGS 238
Cdd:COG0106   142 TSGVDLEELAKRFEDAGVAAILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLRALKEL--GVEGAIVGK 219

                         250
                  ....*....|....*....
gi 1473377617 239 AldLFGGRMAYKEVLQYIN 257
Cdd:COG0106   220 A--LYEGKIDLEEALALAR 236
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 5-240 2.88e-27

Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.


Pssm-ID: 425971  Cd Length: 228  Bit Score: 104.87  E-value: 2.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617   5 PCIDIHNGKVKQIVGGslkdegnqakENFVAEQDA---AYFAEFYKKDKICGGHIILLN------PADSSYYKETKRQAL 75
Cdd:pfam00977   4 PAIDLKDGRVVRLVKG----------DYFQNTVYAgdpVELAKRYEEEGADELHFVDLDaakegrPVNLDVVEEIAEEVF 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617  76 LALhtypggmQVGGGI-HAENAKEFIEAGASHVIVTSYVFKDGKVnynnLEKILAAVGKEHLVLDLSCRKKdgdyYIVTD 154
Cdd:pfam00977  74 IPV-------QVGGGIrSLEDVERLLSAGADRVIIGTAAVKNPEL----IKEAAEKFGSQCIVVAIDARRG----KVAIN 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617 155 RWQKFTEEKITpELLDKLKEY-ADEFLVHAVDVEGKASGIEVPLAEMLGDWGRIPITYAGGVGSFEDLKQLKEHGK-Grl 232
Cdd:pfam00977 139 GWREDTGIDAV-EWAKELEELgAGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTEGVdG-- 215


                  ....*...
gi 1473377617 233 nVTIGSAL 240
Cdd:pfam00977 216 -VIAGSAL 222
 
Name Accession Description Interval E-value
PLN02446 PLN02446
(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 1-258 1.03e-133

(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase


Pssm-ID: 215245  Cd Length: 262  Bit Score: 377.89  E-value: 1.03e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617   1 MEFRPCIDIHNGKVKQIVGGSLKD------EGNQAKENFVAEQDAAYFAEFYKKDKICGGHIILLNPADSSyyketKRQA 74
Cdd:PLN02446    1 VRFRPCIDIHKGKVKQIVGSTLKDskdgseDGSELVTNFESDKSAAEFAEMYKRDGLTGGHVIMLGADDAS-----LAAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617  75 LLALHTYPGGMQVGGGIHAENAKEFIEAGASHVIVTSYVFKDGKVNYNNLEKILAAVGKEHLVLDLSCRKKDGDYYIVTD 154
Cdd:PLN02446   76 LEALRAYPGGLQVGGGVNSENAMSYLDAGASHVIVTSYVFRDGQIDLERLKDLVRLVGKQRLVLDLSCRKKDGRYYVVTD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617 155 RWQKFTEEKITPELLDKLKEYADEFLVHAVDVEGKASGIEVPLAEMLGDWGRIPITYAGGVGSFEDLKQLKEHGKGRLNV 234
Cdd:PLN02446  156 RWQKFSDLAVDEETLEFLAAYCDEFLVHGVDVEGKRLGIDEELVALLGEHSPIPVTYAGGVRSLDDLERVKVAGGGRVDV 235

                         250       260
                  ....*....|....*....|....
gi 1473377617 235 TIGSALDLFGGRMAYKEVLQYINQ 258
Cdd:PLN02446  236 TVGSALDIFGGNLPYDDVVAWHKQ 259
hisA_euk TIGR02129
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, eukaryotic type; This ...
 3-255 5.29e-109

phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, eukaryotic type; This enzyme acts in the biosynthesis of histidine and has been characterized in S. cerevisiae and Arabidopsis where it complements the E. coli HisA gene. In eukaryotes the gene is known as HIS6. In bacteria, this gene is found in Fibrobacter succinogenes, presumably due to lateral gene transfer from plants in the rumen gut. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 162719  Cd Length: 253  Bit Score: 314.80  E-value: 5.29e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617   3 FRPCIDIHNGKVKQIVGGSLKDE-GNQAKENFVAEQDAAYFAEFYKKDKICGGHIILLNPADSSyyketkrQALLALHTY 81
Cdd:TIGR02129   3 FRPCIDIHNGKVKQIVGGTLTSKkGSVLKTNFVSDKPSSYYAKLYKDDGVKGCHVIMLGPNNDD-------AAKEALHAY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617  82 PGGMQVGGGIHAENAKEFIEAGASHVIVTSYVFKDGKVNYNNLEKILAAVGKEHLVLDLSCRKK-DGDYYIVTDRWQKFT 160
Cdd:TIGR02129  76 PGGLQVGGGINDTNAQEWLDEGASHVIVTSWLFTKGKFDLKRLKEIVSLVGKDRLIVDLSCRKTqDGRWIVAMNKWQTIT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617 161 EEKITPELLDKLKEYADEFLVHAVDVEGKASGIEVPLAEMLGDWGRIPITYAGGVGSFEDLKQLKEHGKGRLNVTIGSAL 240
Cdd:TIGR02129 156 DLELNAETLEELSKYCDEFLIHAADVEGLCKGIDEELVSKLGEWSPIPITYAGGAKSIDDLDLVDELSKGKVDLTIGSAL 235

                         250
                  ....*....|....*.
gi 1473377617 241 DLFGGR-MAYKEVLQY 255
Cdd:TIGR02129 236 DIFGGNlVKFTDCVAW 251
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 2-254 1.10e-60

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) and the cyclase subunit of imidazoleglycerol phosphate synthase (HisF). The ProFAR isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene. The Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.


Pssm-ID: 240074 [Multi-domain]  Cd Length: 233  Bit Score: 191.33  E-value: 1.10e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617   2 EFRPCIDIHNGKVKQIVGGSLKDEGnQAKENFVAEQDAAYFAEFYKKDKICGGHIILLNPADSSyyKETKRQALLALHTY 81
Cdd:cd04723     1 RIIPVIDLKDGVVVHGVGGDRDNYR-PITSNLCSTSDPLDVARAYKELGFRGLYIADLDAIMGR--GDNDEAIRELAAAW 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617  82 PGGMQVGGGIHA-ENAKEFIEAGASHVIVTSYVFKDGkvnynNLEKILAAVGKEHLVLDLSCRKKDGDyyivtdrwqKFT 160
Cdd:cd04723    78 PLGLWVDGGIRSlENAQEWLKRGASRVIVGTETLPSD-----DDEDRLAALGEQRLVLSLDFRGGQLL---------KPT 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617 161 EEKITPELLDKLKEYADEFLVHAVDVEGKASGIEVPLAEMLGDWGRIPITYAGGVGSFEDLKQLKEhgKGRLNVTIGSAL 240
Cdd:cd04723   144 DFIGPEELLRRLAKWPEELIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGGVRSVEDLELLKK--LGASGALVASAL 221

                         250
                  ....*....|....
gi 1473377617 241 DlfGGRMAYKEVLQ 254
Cdd:cd04723   222 H--DGGLTLEDVVR 233
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 2-257 1.11e-55

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino acid transport and metabolism]; Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439876  Cd Length: 236  Bit Score: 178.69  E-value: 1.11e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617   2 EFRPCIDIHNGKVKQIVGGSLKDEgnqakenFVAEQDAAYFAEFYKKDKICGGHIILLNPADSsyyKETKRQALLA--LH 79
Cdd:COG0106     1 IIIPAIDLKDGKCVRLVQGDYDQE-------TVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFA---GKPVNLELIEeiAK 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617  80 TYPGGMQVGGGIH-AENAKEFIEAGASHVIVTSYVFKDGKVnynnLEKILAAVGkEHLVLDLSCRkkdgDYYIVTDRWQK 158
Cdd:COG0106    71 ATGLPVQVGGGIRsLEDIERLLDAGASRVILGTAAVKDPEL----VKEALEEFP-ERIVVGLDAR----DGKVATDGWQE 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617 159 FTEEKITPELLDKLKEYADEFLVHAVDVEGKASGIEVPLAEMLGDWGRIPITYAGGVGSFEDLKQLKEHgkGRLNVTIGS 238
Cdd:COG0106   142 TSGVDLEELAKRFEDAGVAAILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLRALKEL--GVEGAIVGK 219

                         250
                  ....*....|....*....
gi 1473377617 239 AldLFGGRMAYKEVLQYIN 257
Cdd:COG0106   220 A--LYEGKIDLEEALALAR 236
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 5-240 2.88e-27

Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.


Pssm-ID: 425971  Cd Length: 228  Bit Score: 104.87  E-value: 2.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617   5 PCIDIHNGKVKQIVGGslkdegnqakENFVAEQDA---AYFAEFYKKDKICGGHIILLN------PADSSYYKETKRQAL 75
Cdd:pfam00977   4 PAIDLKDGRVVRLVKG----------DYFQNTVYAgdpVELAKRYEEEGADELHFVDLDaakegrPVNLDVVEEIAEEVF 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617  76 LALhtypggmQVGGGI-HAENAKEFIEAGASHVIVTSYVFKDGKVnynnLEKILAAVGKEHLVLDLSCRKKdgdyYIVTD 154
Cdd:pfam00977  74 IPV-------QVGGGIrSLEDVERLLSAGADRVIIGTAAVKNPEL----IKEAAEKFGSQCIVVAIDARRG----KVAIN 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617 155 RWQKFTEEKITpELLDKLKEY-ADEFLVHAVDVEGKASGIEVPLAEMLGDWGRIPITYAGGVGSFEDLKQLKEHGK-Grl 232
Cdd:pfam00977 139 GWREDTGIDAV-EWAKELEELgAGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTEGVdG-- 215


                  ....*...
gi 1473377617 233 nVTIGSAL 240
Cdd:pfam00977 216 -VIAGSAL 222
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 86-240 6.17e-19

HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene.


Pssm-ID: 240083  Cd Length: 234  Bit Score: 82.91  E-value: 6.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617  86 QVGGGIH-AENAKEFIEAGASHVIVTSYVFKDGKVnynnLEKILAAVGKEHLVLDLSCRkkdgDYYIVTDRWQKFTEEKI 164
Cdd:cd04732    77 QVGGGIRsLEDIERLLDLGVSRVIIGTAAVKNPEL----VKELLKEYGGERIVVGLDAK----DGKVATKGWLETSEVSL 148

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1473377617 165 TpELLDKLKEY-ADEFLVHAVDVEGKASGIEVPLAEMLGDWGRIPITYAGGVGSFEDLKQLKEHG-KGrlnVTIGSAL 240
Cdd:cd04732   149 E-ELAKRFEELgVKAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDDIKALKELGvAG---VIVGKAL 222
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 5-240 1.87e-17

phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family consists of HisA, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, the enzyme catalyzing the fourth step in histidine biosynthesis. It is closely related to the enzyme HisF for the sixth step. Examples of this enzyme in Actinobacteria have been found to be bifunctional, also possessing phosphoribosylanthranilate isomerase activity; the trusted cutoff here has now been raised to 275.0 to exclude the bifunctional group, now represented by model TIGR01919. HisA from Lactococcus lactis was reported to be inactive (MEDLINE:93322317). [Amino acid biosynthesis, Histidine family]


Pssm-ID: 272850 [Multi-domain]  Cd Length: 230  Bit Score: 78.78  E-value: 1.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617   5 PCIDIHNGKVKQIVggslkdEGNQAKENFVAEqDAAYFAEFYKKDKICGGHIILLNPADSSYYKETKR-QALLALHTYPg 83
Cdd:TIGR00007   3 PAIDIKDGKCVRLY------QGDYDKETVYGD-DPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPViKKIVRETGVP- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617  84 gMQVGGGIH-AENAKEFIEAGASHVIVTSYVFKdgkvNYNNLEKILAAVGKEHLVLDLSCRkkdgDYYIVTDRWQKFTEE 162
Cdd:TIGR00007  75 -VQVGGGIRsLEDVEKLLDLGVDRVIIGTAAVE----NPDLVKELLKEYGPERIVVSLDAR----GGEVAVKGWLEKSEV 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617 163 KITpELLDKLKEY-ADEFLVHAVDVEGKASGIEVPLAEMLGDWGRIPITYAGGVGSFEDLKQLKEHG-KGrlnVTIGSAL 240
Cdd:TIGR00007 146 SLE-ELAKRLEELgLEGIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDDLIALKKLGvYG---VIVGKAL 221
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 1-258 3.13e-17

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;


Pssm-ID: 184165  Cd Length: 241  Bit Score: 78.41  E-value: 3.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617   1 MEFRPCIDIHNGKVKQIVGGslkdEGNQAKENFVAEQDAAyfaefykKDKICGG----HIILLnpaDSSYYKETKRQALL 76
Cdd:PRK13585    3 FEVIPAVDMKGGKCVQLVQG----EPGTETVSYGDPVEVA-------KRWVDAGaetlHLVDL---DGAFEGERKNAEAI 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617  77 A--LHTYPGGMQVGGGIH-AENAKEFIEAGASHVIVTSYVFKDGKVnynnLEKILAAVGKEHLVLDLSCrkKDGDyyIVT 153
Cdd:PRK13585   69 EkiIEAVGVPVQLGGGIRsAEDAASLLDLGVDRVILGTAAVENPEI----VRELSEEFGSERVMVSLDA--KDGE--VVI 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617 154 DRWQKFTEekITP-ELLDKLKEY-ADEFLVHAVDVEGKASGIEVPLAEMLGDWGRIPITYAGGVGSFEDLKQLKEHGKGr 231
Cdd:PRK13585  141 KGWTEKTG--YTPvEAAKRFEELgAGSILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASGGVTTLDDLRALKEAGAA- 217

                         250       260
                  ....*....|....*....|....*..
gi 1473377617 232 lNVTIGSAldLFGGRMAYKEVLQYINQ 258
Cdd:PRK13585  218 -GVVVGSA--LYKGKFTLEEAIEAVKG 241
PRK04128 PRK04128
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 1-254 4.24e-09

1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;


Pssm-ID: 167709  Cd Length: 228  Bit Score: 55.16  E-value: 4.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617   1 MEFRPCIDIHNGKVKQIVGGSlkdegnqaKENFVAEQDAAYFAEFYKK--DKIcggHIILLN------PADSSYYKETKR 72
Cdd:PRK04128    2 MRIYPAIDLMNGKAVRLYKGR--------KEEVKVYGDPVEIALRFSEyvDKI---HVVDLDgafegkPKNLDVVKNIIR 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617  73 QALLALhtypggmQVGGGIHA-ENAKEFIEAGASHVIVTSYVFkdgkvNYNNLEKILAAVGKEHLVLDLscrkKDGDyyI 151
Cdd:PRK04128   71 ETGLKV-------QVGGGLRTyESIKDAYEIGVENVIIGTKAF-----DLEFLEKVTSEFEGITVSLDV----KGGR--I 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617 152 VTDRWqkFTEEKITPE-LLDKLKEYADEFLVHAVDVEGKASGIEvplaEMLGDWGRIPITYAGGVGSFEDLKQLKEHGKG 230
Cdd:PRK04128  133 AVKGW--LEESSIKVEdAYEMLKNYVNRFIYTSIERDGTLTGIE----EIERFWGDEEFIYAGGVSSAEDVKKLAEIGFS 206

                         250       260
                  ....*....|....*....|....
gi 1473377617 231 rlNVTIGSAldLFGGRMAYKEVLQ 254
Cdd:PRK04128  207 --GVIIGKA--LYEGRISLEELLE 226
PRK14114 PRK14114
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 5-226 3.21e-08

1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;


Pssm-ID: 172604  Cd Length: 241  Bit Score: 53.09  E-value: 3.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617   5 PCIDIHNGKVKQIVGGSlkdegnqaKENFVaeqdaayfaeFYKKD------KICGGHIILLNPADSSYYKETKRQ---AL 75
Cdd:PRK14114    5 PAIDLFRGKVARMVKGK--------KENTI----------FYEKDpaelveKLIEEGFTLIHVVDLSKAIENSVEnlpVL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617  76 LALHTYPGGMQVGGGIHA-ENAKEFIEAGASHVIVTSYVFKDgkvnyNNLEKILAAVGKEHlVLDLSCRKKDgdyyIVTD 154
Cdd:PRK14114   67 EKLSEFAEHIQIGGGIRSlDYAEKLRKLGYRRQIVSSKVLED-----PSFLKFLKEIDVEP-VFSLDTRGGK----VAFK 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1473377617 155 RWqkFTEEKITP-ELLDKLKEYADEFLVHA-VDVEGKASGIEVPLAEMLGDWGRIPITYAGGVGSFEDLKQLKE 226
Cdd:PRK14114  137 GW--LAEEEIDPvSLLKRLKEYGLEEIVHTeIEKDGTLQEHDFSLTRKIAIEAEVKVFAAGGISSENSLKTAQR 208
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 87-229 9.48e-08

The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.


Pssm-ID: 240082  Cd Length: 243  Bit Score: 51.31  E-value: 9.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617  87 VGGGIHA-ENAKEFIEAGASHVIVTSYVFKDGKVnynnLEKILAAVGKEHLVLDLSCRKKDGDYYIVTDRWQKFTEEKIT 165
Cdd:cd04731    76 VGGGIRSlEDARRLLRAGADKVSINSAAVENPEL----IREIAKRFGSQCVVVSIDAKRRGDGGYEVYTHGGRKPTGLDA 151

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1473377617 166 PELLDKLKEY-ADEFLVHAVDVEGKASGIEVPLAEMLGDWGRIPITYAGGVGSFEDLKQLKEHGK 229
Cdd:cd04731   152 VEWAKEVEELgAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGG 216
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 86-240 1.24e-07

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated


Pssm-ID: 179108  Cd Length: 233  Bit Score: 50.83  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617  86 QVGGGI-HAENAKEFIEAGASHVIVTSyvfkdgkvnynnlekilAAVGKEHLVLDLsCRKKDG---------DYYIVTDR 155
Cdd:PRK00748   78 QVGGGIrSLETVEALLDAGVSRVIIGT-----------------AAVKNPELVKEA-CKKFPGkivvgldarDGKVATDG 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617 156 WQKFTEEKitpeLLDKLKEYADEFLVHAV--DVE--GKASGIEVPLAEMLGDWGRIPITYAGGVGSFEDLKQLKEHGK-- 229
Cdd:PRK00748  140 WLETSGVT----AEDLAKRFEDAGVKAIIytDISrdGTLSGPNVEATRELAAAVPIPVIASGGVSSLDDIKALKGLGAve 215

                         170
                  ....*....|.
gi 1473377617 230 GrlnVTIGSAL 240
Cdd:PRK00748  216 G---VIVGRAL 223
PRK13586 PRK13586
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 85-228 3.97e-06

1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;


Pssm-ID: 237439  Cd Length: 232  Bit Score: 46.66  E-value: 3.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617  85 MQVGGGIHA-ENAKEFIEAGASHVIVTSYVFKdgkvNYNNLEKILAAVGKEHLVLDLScrkKDGDYYIVTDRWQKFTEEK 163
Cdd:PRK13586   76 IQVGGGIRDiEKAKRLLSLDVNALVFSTIVFT----NFNLFHDIVREIGSNRVLVSID---YDNTKRVLIRGWKEKSMEV 148

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1473377617 164 ItpELLDKLKEYADE-FLVHAVDVEGKASGIEVPLAEMLGDWgRIPITYAGGVGSFEDLKQLKEHG 228
Cdd:PRK13586  149 I--DGIKKVNELELLgIIFTYISNEGTTKGIDYNVKDYARLI-RGLKEYAGGVSSDADLEYLKNVG 211
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 86-131 2.36e-04

Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; Pentose-5-phosphate-3-epimerase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 439806  Cd Length: 218  Bit Score: 41.21  E-value: 2.36e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1473377617  86 QVGGGIHAENAKEFIEAGASHVIVTSYVFKDG--KVNYNNLEKILAAV 131
Cdd:COG0036   171 EVDGGINAETIPELAEAGADVLVAGSAVFGAEdyAAAIAALREAAAAA 218
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 63-117 7.94e-04

Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate, as part of the Calvin cycle (reductive pentose phosphate pathway) in chloroplasts and in the oxidative pentose phosphate pathway. In the Calvin cycle Ru5P is phosphorylated by phosphoribulose kinase to ribulose-1,5-bisphosphate, which in turn is used by RubisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) to incorporate CO2 as the central step in carbohydrate synthesis.


Pssm-ID: 238244  Cd Length: 211  Bit Score: 39.39  E-value: 7.94e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1473377617  63 DSSYYKETKRQALLALHTYPGGMQVGGGIHAENAKEFIEAGASHVIVTSYVFKDG 117
Cdd:cd00429   147 PEVLEKIRKLRELIPENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSD 201
Eda COG0800
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ...
 89-127 2.16e-03

2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; 2-keto-3-deoxy-6-phosphogluconate aldolase is part of the Pathway/BioSystem: Entner-Doudoroff pathway


Pssm-ID: 440563  Cd Length: 213  Bit Score: 38.14  E-value: 2.16e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1473377617  89 GGIHAENAKEFIEAGASHVIVTSYVFKDGKVNYNNLEKI 127
Cdd:COG0800   159 GGVSPDNAADYLAAGAVAVGGGSWLVPKGAIAAGDWAAI 197
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 87-229 3.52e-03

Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; Imidazole glycerol phosphate synthase subunit HisF is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439877  Cd Length: 251  Bit Score: 37.70  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473377617  87 VGGGIHA-ENAKEFIEAGASHVIVTSYVFKDGKVnynnLEKILAAVGKEHLVLDLSCRK-KDGDYYIVTDRWQKFTeeKI 164
Cdd:COG0107    78 VGGGIRSvEDARRLLRAGADKVSINSAAVKNPEL----ITEAAERFGSQCIVVAIDAKRvPDGGWEVYTHGGRKPT--GL 151

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1473377617 165 TP-ELLDKLKEY-ADEFLVHAVDVEGKASGIEVPLAEMLGDWGRIPITYAGGVGSFEDLKQLKEHGK 229
Cdd:COG0107   152 DAvEWAKEAEELgAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGG 218
ComA pfam02679
(2R)-phospho-3-sulfolactate synthase (ComA); In methanobacteria (2R)-phospho-3-sulfolactate ...
 94-136 7.36e-03

(2R)-phospho-3-sulfolactate synthase (ComA); In methanobacteria (2R)-phospho-3-sulfolactate synthase (ComA) catalyzes the first step of the biosynthesis of coenzyme M from phosphoenolpyruvate (P-enolpyruvate). This novel enzyme catalyzes the stereospecific Michael addition of sulfite to P-enolpyruvate, forming L-2-phospho-3-sulfolactate (PSL). It is suggested that the ComA-catalyzed reaction is analogous to those reactions catalyzed by beta-elimination enzymes that proceed through an enolate intermediate.


Pssm-ID: 426922  Cd Length: 238  Bit Score: 36.71  E-value: 7.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1473377617  94 ENAKEFIEAGASHVIV-------TSYVF-KDGKVNYNNLEKILAAVGKEHL 136
Cdd:pfam02679 149 EQAKRDLEAGADKVIIearesgtTVGIYdEDGEVRTDLVEEIIERLGLEKI 199
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
 86-115 8.95e-03

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 36.32  E-value: 8.95e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1473377617  86 QVGGGIHAENAKEFIEAGASHVIVTSYVFK 115
Cdd:PRK05581  174 EVDGGINADNIKECAEAGADVFVAGSAVFG 203
 
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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