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Conserved domains on  [gi|500472519|ref|WP_011939353|]
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chorismate mutase [Geotalea uraniireducens]

Protein Classification

chorismate mutase( domain architecture ID 10004036)

chorismate mutase catalyzes the interconversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PheA COG1605
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ...
 1-84 7.19e-24

Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


:

Pssm-ID: 441213 [Multi-domain]  Cd Length: 166  Bit Score: 88.67  E-value: 7.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500472519   1 MNIDNLREQIDNLDSELLRIFNERANLALKIGEIKKGLALPVYDPSREKKIFKRMQEENPGP-LDDQAIVRLFERVIDES 79
Cdd:COG1605    5 ESLEELRAEIDEIDRQLLELLAERAELAKEVGELKKEHGLPIYDPEREAEVLERLRELAEELgLDPEFVEAIFREIISES 84


                 ....*
gi 500472519  80 RRLER 84
Cdd:COG1605   85 IALQE 89
 
Name Accession Description Interval E-value
PheA COG1605
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ...
 1-84 7.19e-24

Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 441213 [Multi-domain]  Cd Length: 166  Bit Score: 88.67  E-value: 7.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500472519   1 MNIDNLREQIDNLDSELLRIFNERANLALKIGEIKKGLALPVYDPSREKKIFKRMQEENPGP-LDDQAIVRLFERVIDES 79
Cdd:COG1605    5 ESLEELRAEIDEIDRQLLELLAERAELAKEVGELKKEHGLPIYDPEREAEVLERLRELAEELgLDPEFVEAIFREIISES 84


                 ....*
gi 500472519  80 RRLER 84
Cdd:COG1605   85 IALQE 89
CM_2 pfam01817
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of ...
 7-84 2.27e-20

Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis. This enzyme is negatively regulated by tyrosine, tryptophan and phenylalanine.


Pssm-ID: 460345 [Multi-domain]  Cd Length: 79  Bit Score: 77.15  E-value: 2.27e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500472519   7 REQIDNLDSELLRIFNERANLALKIGEIKKGLALPVYDPSREKKIFKRMQEE-NPGPLDDQAIVRLFERVIDESRRLER 84
Cdd:pfam01817  1 RAEIDEIDREILELLAERMELAREIGEYKKENGLPVYDPEREEEVLERLRAGaEELGLDPDFIEAIFREIISESRALQK 79
PRK12595 PRK12595
bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed
 3-91 4.32e-19

bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed


Pssm-ID: 183614 [Multi-domain]  Cd Length: 360  Bit Score: 79.25  E-value: 4.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500472519   3 IDNLREQIDNLDSELLRIFNERANLALKIGEIKKGLALPVYDPSREKKIFKRMQEENPGPLDDQAIVRLFERVIDESRRL 82
Cdd:PRK12595   6 LEQLRKEIDEINLQLLELLSKRGELVQEIGEEKTKQGTKRYDPVREREMLDMIAENNEGPFEDSTIQHLFKEIFKASLEL 85


                 ....*....
gi 500472519  83 ERIMTSREL 91
Cdd:PRK12595  86 QEDDNRKAL 94
CM_2 smart00830
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ...
 7-84 1.93e-18

Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis. This enzyme is negatively regulated by tyrosine, tryptophan and phenylalanine..


Pssm-ID: 214841 [Multi-domain]  Cd Length: 79  Bit Score: 72.23  E-value: 1.93e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500472519    7 REQIDNLDSELLRIFNERANLALKIGEIKKGLALPVYDPSREKKIFKRMQEENPGP-LDDQAIVRLFERVIDESRRLER 84
Cdd:smart00830  1 RAEIDAIDDQILALLAERAALAREVARLKAKNGLPIRDPEREAEVLERLRALAEGPgLDPELVERIFREIIEASIALQK 79
CM_P2 TIGR01807
chorismate mutase domain of proteobacterial P-protein, clade 2; This model represents one of ...
 6-76 6.37e-16

chorismate mutase domain of proteobacterial P-protein, clade 2; This model represents one of two separate clades of the chorismate mutase domain of the gamma and beta and epsilon proteobacterial "P-protein" which contains an N-terminal chorismate mutase domain and a C-terminal prephenate dehydratase domain. It is also found in Aquifex aolicus. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130866 [Multi-domain]  Cd Length: 76  Bit Score: 65.93  E-value: 6.37e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500472519   6 LREQIDNLDSELLRIFNERANLALKIGEIKKGLA--LPVYDPSREKKIFKRMQEENPGPLDDQAIVRLFERVI 76
Cdd:TIGR01807  4 LRNKIDAIDDRILDLLSERATYAQAVGELKGSGAsgASFYRPEREAQVIRRLQNLNKGPLDQEAIARIFREIM 76
 
Name Accession Description Interval E-value
PheA COG1605
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ...
 1-84 7.19e-24

Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 441213 [Multi-domain]  Cd Length: 166  Bit Score: 88.67  E-value: 7.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500472519   1 MNIDNLREQIDNLDSELLRIFNERANLALKIGEIKKGLALPVYDPSREKKIFKRMQEENPGP-LDDQAIVRLFERVIDES 79
Cdd:COG1605    5 ESLEELRAEIDEIDRQLLELLAERAELAKEVGELKKEHGLPIYDPEREAEVLERLRELAEELgLDPEFVEAIFREIISES 84


                 ....*
gi 500472519  80 RRLER 84
Cdd:COG1605   85 IALQE 89
CM_2 pfam01817
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of ...
 7-84 2.27e-20

Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis. This enzyme is negatively regulated by tyrosine, tryptophan and phenylalanine.


Pssm-ID: 460345 [Multi-domain]  Cd Length: 79  Bit Score: 77.15  E-value: 2.27e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500472519   7 REQIDNLDSELLRIFNERANLALKIGEIKKGLALPVYDPSREKKIFKRMQEE-NPGPLDDQAIVRLFERVIDESRRLER 84
Cdd:pfam01817  1 RAEIDEIDREILELLAERMELAREIGEYKKENGLPVYDPEREEEVLERLRAGaEELGLDPDFIEAIFREIISESRALQK 79
PRK12595 PRK12595
bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed
 3-91 4.32e-19

bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed


Pssm-ID: 183614 [Multi-domain]  Cd Length: 360  Bit Score: 79.25  E-value: 4.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500472519   3 IDNLREQIDNLDSELLRIFNERANLALKIGEIKKGLALPVYDPSREKKIFKRMQEENPGPLDDQAIVRLFERVIDESRRL 82
Cdd:PRK12595   6 LEQLRKEIDEINLQLLELLSKRGELVQEIGEEKTKQGTKRYDPVREREMLDMIAENNEGPFEDSTIQHLFKEIFKASLEL 85


                 ....*....
gi 500472519  83 ERIMTSREL 91
Cdd:PRK12595  86 QEDDNRKAL 94
CM_2 smart00830
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ...
 7-84 1.93e-18

Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis. This enzyme is negatively regulated by tyrosine, tryptophan and phenylalanine..


Pssm-ID: 214841 [Multi-domain]  Cd Length: 79  Bit Score: 72.23  E-value: 1.93e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500472519    7 REQIDNLDSELLRIFNERANLALKIGEIKKGLALPVYDPSREKKIFKRMQEENPGP-LDDQAIVRLFERVIDESRRLER 84
Cdd:smart00830  1 RAEIDAIDDQILALLAERAALAREVARLKAKNGLPIRDPEREAEVLERLRALAEGPgLDPELVERIFREIIEASIALQK 79
CM_P2 TIGR01807
chorismate mutase domain of proteobacterial P-protein, clade 2; This model represents one of ...
 6-76 6.37e-16

chorismate mutase domain of proteobacterial P-protein, clade 2; This model represents one of two separate clades of the chorismate mutase domain of the gamma and beta and epsilon proteobacterial "P-protein" which contains an N-terminal chorismate mutase domain and a C-terminal prephenate dehydratase domain. It is also found in Aquifex aolicus. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130866 [Multi-domain]  Cd Length: 76  Bit Score: 65.93  E-value: 6.37e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500472519   6 LREQIDNLDSELLRIFNERANLALKIGEIKKGLA--LPVYDPSREKKIFKRMQEENPGPLDDQAIVRLFERVI 76
Cdd:TIGR01807  4 LRNKIDAIDDRILDLLSERATYAQAVGELKGSGAsgASFYRPEREAQVIRRLQNLNKGPLDQEAIARIFREIM 76
CM_A TIGR01801
chorismate mutase domain of gram positive AroA protein; This model represents a small clade of ...
 3-91 2.89e-12

chorismate mutase domain of gram positive AroA protein; This model represents a small clade of chorismate mutase domains N-terminally fused to the first enzyme in the chorismate pathway, 2-dehydro-3-deoxyphosphoheptanoate aldolase (DAHP synthetase, AroA) which are found in some gram positive species and Deinococcus. Only in Deinococcus, where this domain is the sole CM domain in the genome can a trusted assignment of function be made. In the other species there is at least one other trusted CM domain present. The similarity between the Deinococcus gene and the others in this clade is sufficiently strong (~44% identity), that the whole clade can be trusted to be functional. The possibility exists, however, that in the gram positive species the fusion to the first enzyme in the pathway has evolved a separate, regulatory role. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130860 [Multi-domain]  Cd Length: 102  Bit Score: 57.23  E-value: 2.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500472519    3 IDNLREQIDNLDSELLRIFNERANLALKIGEIKKGLALPVYDPSREKKIFKRMQEENPGPLDDQAIVRLFERVIDESRRL 82
Cdd:TIGR01801   6 LEDLRAEVDQLNRQILALISRRGEVVAQIGHAKSAQGPNHYDPAREEQMLNELIKINPGPFPTATIKGIFKEIFKASLAL 85


                  ....*....
gi 500472519   83 ERIMTSREL 91
Cdd:TIGR01801  86 QESNDKKQL 94
tyrA PRK11199
bifunctional chorismate mutase/prephenate dehydrogenase; Provisional
 3-83 3.20e-12

bifunctional chorismate mutase/prephenate dehydrogenase; Provisional


Pssm-ID: 183035 [Multi-domain]  Cd Length: 374  Bit Score: 60.28  E-value: 3.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500472519   3 IDNLREQIDNLDSELLRIFNERANLALKIGEIKKGLALPVYDPSREKKIF-KRMQE-ENPGpLDDQAIVRLFERVIDESR 80
Cdd:PRK11199   5 LTALRDQIDEVDKQLLELLAKRLELVAQVGEVKSRHGLPIYVPEREAAMLaSRRAEaEALG-VPPDLIEDVLRRVMRESY 83


                 ...
gi 500472519  81 RLE 83
Cdd:PRK11199  84 SSE 86
pheA PRK10622
bifunctional chorismate mutase/prephenate dehydratase; Provisional
 5-79 4.10e-10

bifunctional chorismate mutase/prephenate dehydratase; Provisional


Pssm-ID: 182594 [Multi-domain]  Cd Length: 386  Bit Score: 54.35  E-value: 4.10e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500472519   5 NLREQIDNLDSELLRIFNERANLALKIGEIKKGLALPVYDPSREKKIFKRMQEE-NPGPLDDQAIVRLFERVIDES 79
Cdd:PRK10622   9 ALREKISALDEKLLALLAERRELAVEVAKAKLLSHRPVRDIDRERDLLERLITLgKAHHLDAHYITRLFQLIIEDS 84
PRK07248 PRK07248
chorismate mutase;
1-84 5.55e-09

chorismate mutase;


Pssm-ID: 168880 [Multi-domain]  Cd Length: 87  Bit Score: 48.52  E-value: 5.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500472519  1 MNIDNLREQIDNLDSELLRIFNERANLALKIGEIKKGLALPVYDPSREKKIFKRMQEENPGPLDDQAIVRLFERVIDESR 80
Cdd:PRK07248  1 MDLEEIRQEIDQIDDQLVALLEKRMALVEQVVAYKKATGKPVLDTKREQVILDKVSSLVENKAYQETIVATFKDIMKRSR 80


                ....
gi 500472519 81 RLER 84
Cdd:PRK07248 81 DYQT 84
CM_mono_grmpos TIGR01805
monofunctional chorismate mutase, gram positive-type, clade 2; This model represents a clade ...
 3-83 1.34e-07

monofunctional chorismate mutase, gram positive-type, clade 2; This model represents a clade of chorismate mutase proteins/domains from gram positive species. The sequence from Enterococcus is fused to the C-terminus of an aparrent acetyltransferase, and the seuence from Clostridium acetobutylicum (but not perfringens) is fused to the N-terminus of shikimate-5-dehydrogenase, another enzyme of the chorismate pathway. All the other members of this clade are mono-functional. Members of this clade from Streptococcus and Lactococcus have been found which represent the sole chorismate mutase domain in their respective genomes which also exhibit evidence of the enzymes of both the upstream and downstream branches of the chorismate pathways. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130864 [Multi-domain]  Cd Length: 81  Bit Score: 44.77  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500472519   3 IDNLREQIDNLDSELLRIFNERANLALKIGEIKKGLALPVYDPSREKKIFKRMQEENPGPLDDQAIVRLFERVIDESRRL 82
Cdd:TIGR01805  1 LELIRKKIDEIDDKLVVLFEERMEVVKEIAAYKKKNGIPIFDSKREQEIIDKCTKNVENKEYRETIEEFFRNIMDISKEV 80


                 .
gi 500472519  83 E 83
Cdd:TIGR01805 81 Q 81
PRK06285 PRK06285
chorismate mutase; Provisional
 7-84 1.58e-06

chorismate mutase; Provisional


Pssm-ID: 180509 [Multi-domain]  Cd Length: 96  Bit Score: 42.33  E-value: 1.58e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500472519  7 REQIDNLDSELLRIFNERANLALKIGEIKKGLALPVYDPSREKKIFKRMQE-ENPGPLDDQAIVRLFERVIDESRRLER 84
Cdd:PRK06285 13 RKRIDEIDEQIIDLIAERTSLAKEIAELKKSLGMPIFDPEREDYIHEKIRKlCEEHNIDENIGLKIMKILMEHSKELQK 91
CM_M_hiGC-arch TIGR01808
monofunctional chorismate mutase, high GC gram positive type; This model represents the ...
 3-60 3.54e-06

monofunctional chorismate mutase, high GC gram positive type; This model represents the monofunctional chorismate mutase from high GC gram-positive bacteria and archaea. Trusted annotations from Corynebacterium and Pyrococcus are aparrently the sole chorismate mutase enzymes in their respective genomes. This is coupled with the presence in those genomes of the enzymes of the chorismate pathways both up- and downstream of chorismate mutase. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130867 [Multi-domain]  Cd Length: 74  Bit Score: 41.05  E-value: 3.54e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 500472519   3 IDNLREQIDNLDSELLRIFNERANLALKIGEIKKGLALPVYDPSREKKIFKRMQEENP 60
Cdd:TIGR01808  2 IDTLREEIDRLDAEILALVKRRAEISQAIGKARMASGGTRLVHSREMKVIERYSELGP 59
CM-like TIGR01803
chorismate mutase related enzymes; This subfamily includes two enzymes which are variants on ...
 3-83 4.13e-05

chorismate mutase related enzymes; This subfamily includes two enzymes which are variants on the mechanism of chorismate mutase and are likely to have evolved from an ancestral chorismate mutase enzyme. 4-amino-4-deoxy-chorismate mutase produces amino-deoxy-prephenate which is subsequently converted to para-dimethylamino-phenylalanine, a component of the natural product pristinamycin. Isochorismate-pyruvate lyase presumably catalyzes the same type of 2+2+2 cyclo-rearrangement as chorismate mutase, but acting on isochorismate, this results in two broken bonds instead of one broken and one made. The product of this reaction is salicylate (2-hydroxy-benzoate) which is also incorporated into various natural products.


Pssm-ID: 130862 [Multi-domain]  Cd Length: 82  Bit Score: 38.34  E-value: 4.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500472519   3 IDNLREQIDNLDSELLRIFNERANLALKIGEIKKGLALPVYDPSREKKIF---KRMQEENpgPLDDQAIVRLFERVIDES 79
Cdd:TIGR01803  1 LADIREAIDRIDLALVQALGRRMDYVKRASEFKRSHEAAIPAPERVAAVLpnaARWAEEN--GLDPPFVEGLFAQIIHWY 78


                 ....
gi 500472519  80 RRLE 83
Cdd:TIGR01803 79 IAEE 82
CM_archaeal TIGR01791
chorismate mutase, archaeal type; This model represents a clade of archaeal chorismate mutases. ...
 3-84 5.55e-05

chorismate mutase, archaeal type; This model represents a clade of archaeal chorismate mutases. Chorismate mutase catalyzes the conversion of chorismate into prephenate which is subsequently converted into either phenylalanine or tyrosine. In Sulfolobus this gene is found as a fusion with prephenate dehydrogenase (although the non-TIGR annotation contains a typographical error indicating it as a dehydratase OMNI|NTL02SS0274) which is the next enzyme in the tyrosine biosynthesis pathway. The Archaeoglobus gene contains an N-terminal prephenate dehydrogenase domain and a C-terminal prephenate dehydratase domain followed by a regulatory amino acid-binding ACT domain. The Thermoplasma volcanium gene is adjacent to prephenate dehydratase. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130851 [Multi-domain]  Cd Length: 83  Bit Score: 37.79  E-value: 5.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500472519   3 IDNLREQIDNLDSELLRIFNERANLALKIGEIKKGLALPVYDPSREKKIFKRMQEENPGP-LDDQAIVRLFERVIDESRR 81
Cdd:TIGR01791  1 IEELRQEIEEIDKSILDLIEKRIKIARKIGEIKHNNGLPITDEEREERVIERLRNTARNLgLDVLKLKEIFEILMSLSKE 80


                 ...
gi 500472519  82 LER 84
Cdd:TIGR01791 81 EQR 83
PRK06034 PRK06034
hypothetical protein; Provisional
 3-76 4.67e-04

hypothetical protein; Provisional


Pssm-ID: 235680 [Multi-domain]  Cd Length: 279  Bit Score: 37.00  E-value: 4.67e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500472519   3 IDNLREQIDNLDSELLRIFNERANLALKIGEIKK----GLALpvyDPSREKKIFKRMQEENPGPLDDQAIVRLFeRVI 76
Cdd:PRK06034  11 LAELRWEIDAIDEELHQLLMERGDIIDRLIAVKRtqevGSAF---RPGREADMMRRLVSRHRGILPLDTVESIW-RVI 84
PRK06443 PRK06443
chorismate mutase; Validated
 1-60 1.65e-03

chorismate mutase; Validated


Pssm-ID: 235801  Cd Length: 177  Bit Score: 35.27  E-value: 1.65e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 500472519   1 MNIDNLREQIDNLDSELLRIFNERANLALKIGEIKKGLALPVYDPSREKKIFKRMQEENP 60
Cdd:PRK06443   5 IDMEDLRSEILENTMDIIELIEKRRELARMIGIIKMRNGLSIRDSERENYVKNNLKSDNP 64
PRK07857 PRK07857
chorismate mutase;
2-58 2.27e-03

chorismate mutase;


Pssm-ID: 236117  Cd Length: 106  Bit Score: 34.28  E-value: 2.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 500472519   2 NIDNLREQIDNLDSELLRIFNERANLALKIGEIKKGLALPVYDPSREKKIFKRMQEE 58
Cdd:PRK07857  29 EIDELREEIDRLDAEILALVKRRTEVSQAIGKARMASGGTRLVHSREMKVIERYREE 85
PRK09239 PRK09239
chorismate mutase; Provisional
 6-57 2.62e-03

chorismate mutase; Provisional


Pssm-ID: 181719 [Multi-domain]  Cd Length: 104  Bit Score: 33.84  E-value: 2.62e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 500472519   6 LREQIDNLDSELLRIFNERANLALKIGEIKKGLALPVYDPSREKKIFKRMQE 57
Cdd:PRK09239  15 LRQSIDNIDAALIHMLAERFKCTQAVGVLKAEHGLPPADPAREAYQIERLRQ 66
 
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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