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Conserved domains on  [gi|2190839825|gb|UKP28230|]
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3-isopropylmalate dehydratase small subunit [Streptococcus pneumoniae]

Protein Classification

3-isopropylmalate dehydratase small subunit( domain architecture ID 10014895)

3-isopropylmalate dehydratase small subunit catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK14812 PRK14812
hypothetical protein; Provisional
 1-119 2.39e-83

hypothetical protein; Provisional


:

Pssm-ID: 173273 [Multi-domain]  Cd Length: 119  Bit Score: 238.85  E-value: 2.39e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190839825   1 MAGSSREYAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPREVREKLAQLKPTDQVTVDLEQQKIISPVEEFTFE 80
Cdd:PRK14812    1 MAGSSREHAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPREVREKLAQLKPTDQVTVDLEQQKIISPVEEFTFE 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2190839825  81 IDSEWKHKLLNSLDDIGITLQYEELIAAYEKQRPAYWQD 119
Cdd:PRK14812   81 IDSEWKHKLLNSLDDIGITLQYEELIAAYEKQRPAYWQD 119
 
Name Accession Description Interval E-value
PRK14812 PRK14812
hypothetical protein; Provisional
 1-119 2.39e-83

hypothetical protein; Provisional


Pssm-ID: 173273 [Multi-domain]  Cd Length: 119  Bit Score: 238.85  E-value: 2.39e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190839825   1 MAGSSREYAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPREVREKLAQLKPTDQVTVDLEQQKIISPVEEFTFE 80
Cdd:PRK14812    1 MAGSSREHAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPREVREKLAQLKPTDQVTVDLEQQKIISPVEEFTFE 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2190839825  81 IDSEWKHKLLNSLDDIGITLQYEELIAAYEKQRPAYWQD 119
Cdd:PRK14812   81 IDSEWKHKLLNSLDDIGITLQYEELIAAYEKQRPAYWQD 119
LeuD COG0066
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ...
 3-116 1.22e-54

3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; 3-isopropylmalate dehydratase small subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439836 [Multi-domain]  Cd Length: 195  Bit Score: 168.81  E-value: 1.22e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190839825   3 GSSREYAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPREVREKLAQL---KPTDQVTVDLEQQKIISP-VEEFT 78
Cdd:COG0066    77 GSSREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIELPEEAVDALFAAieaNPGDELTVDLEAGTVTNGtGETYP 156

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2190839825  79 FEIDSEWKHKLLNSLDDIGITLQYEELIAAYEKQRPAY 116
Cdd:COG0066   157 FEIDPFRRECLLNGLDDIGLTLKHADAIAAFEAKRPAW 194
leuD TIGR00171
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 3-106 1.29e-38

3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. The candidate archaeal leuD proteins are not included in the seed alignment for this model and score below the trusted cutoff. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 129275 [Multi-domain]  Cd Length: 188  Bit Score: 128.01  E-value: 1.29e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190839825   3 GSSREYAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQP-REVREKLAQLK-PTDQVTVDLEQQKI-ISPVEEFTF 79
Cdd:TIGR00171  82 GSSREHAPWALDDYGFKVIIAPSFADIFYNNSFKNGLLPIRLSyDEVKELFGQVEnQGLQMTVDLENQLIhDSEGKVYSF 161

                          90       100
                  ....*....|....*....|....*..
gi 2190839825  80 EIDSEWKHKLLNSLDDIGITLQYEELI 106
Cdd:TIGR00171 162 EIDPFRKHCLINGLDEIGLTLQHEDEI 188
IPMI_Swivel cd01577
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ...
 3-65 1.58e-26

Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.


Pssm-ID: 238809 [Multi-domain]  Cd Length: 91  Bit Score: 94.19  E-value: 1.58e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2190839825   3 GSSREYAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPREVREKLAQlKPTDQVTVDL 65
Cdd:cd01577    30 GSSREHAPWALKDAGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEVEA-KPGDEVEVDL 91
Aconitase_C pfam00694
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ...
 2-47 3.87e-22

Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This domain undergoes conformational change in the enzyme mechanism.


Pssm-ID: 459908 [Multi-domain]  Cd Length: 131  Bit Score: 84.34  E-value: 3.87e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2190839825   2 AGSSREYAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPRE 47
Cdd:pfam00694  86 CGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
 
Name Accession Description Interval E-value
PRK14812 PRK14812
hypothetical protein; Provisional
 1-119 2.39e-83

hypothetical protein; Provisional


Pssm-ID: 173273 [Multi-domain]  Cd Length: 119  Bit Score: 238.85  E-value: 2.39e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190839825   1 MAGSSREYAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPREVREKLAQLKPTDQVTVDLEQQKIISPVEEFTFE 80
Cdd:PRK14812    1 MAGSSREHAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPREVREKLAQLKPTDQVTVDLEQQKIISPVEEFTFE 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2190839825  81 IDSEWKHKLLNSLDDIGITLQYEELIAAYEKQRPAYWQD 119
Cdd:PRK14812   81 IDSEWKHKLLNSLDDIGITLQYEELIAAYEKQRPAYWQD 119
leuD PRK01641
3-isopropylmalate dehydratase small subunit;
3-118 8.28e-68

3-isopropylmalate dehydratase small subunit;


Pssm-ID: 179314 [Multi-domain]  Cd Length: 200  Bit Score: 202.28  E-value: 8.28e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190839825   3 GSSREYAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPREVREKLAQL---KPTDQVTVDLEQQKIISPVEEFTF 79
Cdd:PRK01641   80 GSSREHAPWALADYGFRAVIAPSFADIFYNNCFKNGLLPIVLPEEDVDELFKLveaNPGAELTVDLEAQTVTAPDKTFPF 159

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2190839825  80 EIDSEWKHKLLNSLDDIGITLQYEELIAAYEKQRPAYWQ 118
Cdd:PRK01641  160 EIDPFRRHCLLNGLDDIGLTLQHEDAIAAYEAKRPAFRP 198
LeuD COG0066
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ...
 3-116 1.22e-54

3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; 3-isopropylmalate dehydratase small subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439836 [Multi-domain]  Cd Length: 195  Bit Score: 168.81  E-value: 1.22e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190839825   3 GSSREYAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPREVREKLAQL---KPTDQVTVDLEQQKIISP-VEEFT 78
Cdd:COG0066    77 GSSREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIELPEEAVDALFAAieaNPGDELTVDLEAGTVTNGtGETYP 156

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2190839825  79 FEIDSEWKHKLLNSLDDIGITLQYEELIAAYEKQRPAY 116
Cdd:COG0066   157 FEIDPFRRECLLNGLDDIGLTLKHADAIAAFEAKRPAW 194
leuD TIGR00171
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 3-106 1.29e-38

3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. The candidate archaeal leuD proteins are not included in the seed alignment for this model and score below the trusted cutoff. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 129275 [Multi-domain]  Cd Length: 188  Bit Score: 128.01  E-value: 1.29e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190839825   3 GSSREYAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQP-REVREKLAQLK-PTDQVTVDLEQQKI-ISPVEEFTF 79
Cdd:TIGR00171  82 GSSREHAPWALDDYGFKVIIAPSFADIFYNNSFKNGLLPIRLSyDEVKELFGQVEnQGLQMTVDLENQLIhDSEGKVYSF 161

                          90       100
                  ....*....|....*....|....*..
gi 2190839825  80 EIDSEWKHKLLNSLDDIGITLQYEELI 106
Cdd:TIGR00171 162 EIDPFRKHCLINGLDEIGLTLQHEDEI 188
IPMI_Swivel cd01577
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ...
 3-65 1.58e-26

Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.


Pssm-ID: 238809 [Multi-domain]  Cd Length: 91  Bit Score: 94.19  E-value: 1.58e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2190839825   3 GSSREYAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPREVREKLAQlKPTDQVTVDL 65
Cdd:cd01577    30 GSSREHAPWALKDAGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEVEA-KPGDEVEVDL 91
Aconitase_C pfam00694
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ...
 2-47 3.87e-22

Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This domain undergoes conformational change in the enzyme mechanism.


Pssm-ID: 459908 [Multi-domain]  Cd Length: 131  Bit Score: 84.34  E-value: 3.87e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2190839825   2 AGSSREYAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPRE 47
Cdd:pfam00694  86 CGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
leuD PRK00439
3-isopropylmalate dehydratase small subunit; Reviewed
 3-81 1.69e-15

3-isopropylmalate dehydratase small subunit; Reviewed


Pssm-ID: 234762 [Multi-domain]  Cd Length: 163  Bit Score: 67.93  E-value: 1.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190839825   3 GSSREYAAWALADYGFKVVIAGSFGDIHYNNELNNGmLPIVQPREVREKLAQlkpTDQVTVDLEQQKIIS---------- 72
Cdd:PRK00439   61 GSSREHAPIALKAAGVSAVIAKSFARIFYRNAINIG-LPVLECDEAVDKIED---GDEVEVDLETGVITNlttgeeykfk 136


                  ....*....
gi 2190839825  73 PVEEFTFEI 81
Cdd:PRK00439  137 PIPEFMLEI 145
PRK14023 PRK14023
homoaconitate hydratase small subunit; Provisional
 3-102 4.41e-12

homoaconitate hydratase small subunit; Provisional


Pssm-ID: 184460 [Multi-domain]  Cd Length: 166  Bit Score: 59.05  E-value: 4.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190839825   3 GSSREYAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIvqprEVREKLAQLKPTDQVTVDLEQQKIISPVEEFTFEID 82
Cdd:PRK14023   62 GSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPPF----ESEEVVDALEDGDEVELDLETGVLTRGGETFQLRPP 137

                          90       100
                  ....*....|....*....|
gi 2190839825  83 SEWkhkLLNSLDDIGITLQY 102
Cdd:PRK14023  138 PEF---LLEALKEGSILEYY 154
Aconitase_swivel cd00404
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ...
 3-64 4.14e-10

Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. The aconitase family contains the following proteins: - Iron-responsive element binding protein (IRE-BP). IRE-BP is a cytosolic protein that binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5'UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'UTR of transferrin receptor mRNA. IRE-BP also express aconitase activity. - 3-isopropylmalate dehydratase (isopropylmalate isomerase), the enzyme that catalyzes the second step in the biosynthesis of leucine. - Homoaconitase (homoaconitate hydratase), an enzyme that participates in the alpha-aminoadipate pathway of lysine biosynthesis and that converts cis-homoaconitate into homoisocitric acid.


Pssm-ID: 238236 [Multi-domain]  Cd Length: 88  Bit Score: 52.09  E-value: 4.14e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2190839825   3 GSSREYAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPreVREKLAQLKPTDQVTVD 64
Cdd:cd00404    28 GSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFA--DPEDYLKLHTGDELDIY 87
PRK07229 PRK07229
aconitate hydratase; Validated
 3-43 7.17e-08

aconitate hydratase; Validated


Pssm-ID: 235974 [Multi-domain]  Cd Length: 646  Bit Score: 48.99  E-value: 7.17e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2190839825   3 GSSREYAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIV 43
Cdd:PRK07229  536 GSSREHAALAPRYLGVKAVLAKSFARIHKANLINFGILPLT 576
AcnA_Bact_Swivel cd01579
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ...
 3-42 6.75e-07

Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism. This distinct subfamily is found only in bacteria and archea. Its exact characteristics are not known.


Pssm-ID: 238811 [Multi-domain]  Cd Length: 121  Bit Score: 44.74  E-value: 6.75e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2190839825   3 GSSREYAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPI 42
Cdd:cd01579    61 GSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPL 100
Homoaconitase_Swivel cd01674
Homoaconitase swivel domain. This family includes homoaconitase and other uncharacterized ...
 3-50 2.13e-06

Homoaconitase swivel domain. This family includes homoaconitase and other uncharacterized proteins of the Aconitase family. Homoaconitase is part of an unusual lysine biosynthesis pathway found only in filamentous fungi, in which lysine is synthesized via the alpha-aminoadipate pathway. In this pathway, homoaconitase catalyzes the conversion of cis-homoaconitic acid into homoisocitric acid. The reaction mechanism is believed to be similar to that of other aconitases. This is the swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.


Pssm-ID: 238837 [Multi-domain]  Cd Length: 129  Bit Score: 43.43  E-value: 2.13e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2190839825   3 GSSREYAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPREVRE 50
Cdd:cd01674    58 GSSREQAATALLAKGIPLVVSGSFGNIFSRNSINNALLSIELPFLVQK 105
AcnA_IRP_Swivel cd01580
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ...
 2-65 2.31e-06

Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.


Pssm-ID: 238812 [Multi-domain]  Cd Length: 171  Bit Score: 43.80  E-value: 2.31e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2190839825   2 AGSSREYAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPI-VQPREVREKLAqLKPTDQVTVDL 65
Cdd:cd01580   108 SGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLqFPPGENADSLG-LTGEETYDIIG 171
PLN00072 PLN00072
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
 3-71 1.66e-05

3-isopropylmalate isomerase/dehydratase small subunit; Provisional


Pssm-ID: 177701 [Multi-domain]  Cd Length: 246  Bit Score: 42.15  E-value: 1.66e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190839825   3 GSSREYAAWALADYGFKVVIAGSFGDIHYNNELNNGMlpiVQPREVREKLA-QLKPTDQVTVDLEQQKII 71
Cdd:PLN00072  142 GSSREHAPVALGAAGAKAVVAESYARIFFRNSVATGE---VYPLESEVRICeECKTGDVVTVELGNSVLI 208
PTZ00092 PTZ00092
aconitate hydratase-like protein; Provisional
 3-70 1.60e-04

aconitate hydratase-like protein; Provisional


Pssm-ID: 240263 [Multi-domain]  Cd Length: 898  Bit Score: 39.61  E-value: 1.60e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2190839825   3 GSSREYAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPI-VQPREVREKLAqLKPTDQVTVDLEQQKI 70
Cdd:PTZ00092  784 GSSRDWAAKGPYLQGVKAVIAESFERIHRSNLVGMGILPLqFLNGENADSLG-LTGKEQFSIDLNSGEL 851
AcnA_Mitochon_Swivel cd01578
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ...
 3-42 3.74e-04

Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.


Pssm-ID: 238810 [Multi-domain]  Cd Length: 149  Bit Score: 37.83  E-value: 3.74e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2190839825   3 GSSREYAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPI 42
Cdd:cd01578    82 GSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPL 121
acnA PRK12881
aconitate hydratase AcnA;
3-64 5.81e-04

aconitate hydratase AcnA;


Pssm-ID: 237246 [Multi-domain]  Cd Length: 889  Bit Score: 37.99  E-value: 5.81e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2190839825   3 GSSREYAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPREVREKLAQLKPTDQVTVD 64
Cdd:PRK12881  772 GSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFKGGDSRQSLGLTGGETFDIE 833
PLN00070 PLN00070
aconitate hydratase
 2-83 1.09e-03

aconitate hydratase


Pssm-ID: 215047 [Multi-domain]  Cd Length: 936  Bit Score: 37.09  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2190839825   2 AGSSREYAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIV-QPREVREKLAqLKPTDQVTVDLEQQ-KIISPVEEFTF 79
Cdd:PLN00070  819 SGSSRDWAAKGPMLLGVKAVIAKSFERIHRSNLVGMGIIPLCfKSGEDADTLG-LTGHERYTIDLPSNiSEIKPGQDVTV 897


                  ....
gi 2190839825  80 EIDS 83
Cdd:PLN00070  898 TTDN 901
 
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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