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Conserved domains on  [gi|499329768|ref|WP_011020260|]
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3-isopropylmalate dehydratase small subunit [Methanosarcina acetivorans]

Protein Classification

3-isopropylmalate dehydratase small subunit( domain architecture ID 10011439)

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
leuD PRK00439
3-isopropylmalate dehydratase small subunit; Reviewed
 2-162 1.95e-105

3-isopropylmalate dehydratase small subunit; Reviewed


:

Pssm-ID: 234762 [Multi-domain]  Cd Length: 163  Bit Score: 298.28  E-value: 1.95e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768   2 EGRAWKFGDDVDTDAVIPGRYLIFNTPGELAKYTFEGVRPDFAKKVHENDIVVAGSNFGCGSSREHAPLALKGSKVSCVI 81
Cdd:PRK00439   1 KGRVWKFGDNIDTDVIIPARYLNTSDPQELAKHCMEDLDPEFAKKVKPGDIIVAGKNFGCGSSREHAPIALKAAGVSAVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768  82 AKSFARIFFRNAINIGVPVLECPNT-DRIDDGDELEVDLSTGDIQNITKGETYQATPLPDFVREIVDEGGLIEYARKLVS 160
Cdd:PRK00439  81 AKSFARIFYRNAINIGLPVLECDEAvDKIEDGDEVEVDLETGVITNLTTGEEYKFKPIPEFMLEILKAGGLIEYLKKKGR 160


                 ..
gi 499329768 161 ER 162
Cdd:PRK00439 161 FP 162
 
Name Accession Description Interval E-value
leuD PRK00439
3-isopropylmalate dehydratase small subunit; Reviewed
 2-162 1.95e-105

3-isopropylmalate dehydratase small subunit; Reviewed


Pssm-ID: 234762 [Multi-domain]  Cd Length: 163  Bit Score: 298.28  E-value: 1.95e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768   2 EGRAWKFGDDVDTDAVIPGRYLIFNTPGELAKYTFEGVRPDFAKKVHENDIVVAGSNFGCGSSREHAPLALKGSKVSCVI 81
Cdd:PRK00439   1 KGRVWKFGDNIDTDVIIPARYLNTSDPQELAKHCMEDLDPEFAKKVKPGDIIVAGKNFGCGSSREHAPIALKAAGVSAVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768  82 AKSFARIFFRNAINIGVPVLECPNT-DRIDDGDELEVDLSTGDIQNITKGETYQATPLPDFVREIVDEGGLIEYARKLVS 160
Cdd:PRK00439  81 AKSFARIFYRNAINIGLPVLECDEAvDKIEDGDEVEVDLETGVITNLTTGEEYKFKPIPEFMLEILKAGGLIEYLKKKGR 160


                 ..
gi 499329768 161 ER 162
Cdd:PRK00439 161 FP 162
leud TIGR02084
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 3-157 2.69e-78

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 members of the seed for this model are those sequences which are gene clustered with other genes involved in leucine biosynthesis and include some archaea. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 131139 [Multi-domain]  Cd Length: 156  Bit Score: 229.29  E-value: 2.69e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768    3 GRAWKFGDDVDTDAVIPGRYLIFNTPGELAKYTFEGVRPDFAKKVHENDIVVAGSNFGCGSSREHAPLALKGSKVSCVIA 82
Cdd:TIGR02084   1 GKVHKYGDNVDTDVIIPARYLNTSDPKELAKHCMEDLDKDFVKKVKEGDIIVAGENFGCGSSREHAPIAIKASGISCVIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499329768   83 KSFARIFFRNAINIGVPVLECPN-TDRIDDGDELEVDLSTGDIQNITKGETYQATPLPDFVREIVDEGGLIEYARK 157
Cdd:TIGR02084  81 KSFARIFYRNAINIGLPIVESEEaVDEIEEGDEVEVDLEKGIIKNLTKGKEYKATPFPEFLQKIMKAGGLLNYVKK 156
HacB2_Meth NF040625
homoaconitase small subunit;
1-154 4.32e-68

homoaconitase small subunit;


Pssm-ID: 468597 [Multi-domain]  Cd Length: 161  Bit Score: 203.79  E-value: 4.32e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768   1 MEGRAWKFGDDVDTDAVIPGRYLIFNTPGELAKYTFEGVRPDFAKKVHENDIVVAGSNFGCGSSREHAPLALKGSKVSCV 80
Cdd:NF040625   4 IKGKVWKFGDNIDTDVIIPGRYLRTFNPDDLASHVMEGERPDFTKNVQKGDIIVAGWNFGCGSSREQAPVAIKHAGVSAI 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499329768  81 IAKSFARIFFRNAINIGVPVLecpnTDRI--DDGDELEVDLSTGDIQNITKGETYQATPLPDFVREIVDEGGLIEY 154
Cdd:NF040625  84 IAKSFARIFYRNAINIGLPVI----VADIeaDDGDILSIDLEKGIIKNKTTGEEFKIQPFKEFMLEILEDGGLVNH 155
LeuD COG0066
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ...
 1-158 5.51e-63

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: 191.92  E-value: 5.51e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768   1 MEGRAWKF-GDDVDTDAVIPGRYLIFNTPGELAKYTFEGVR------PDF---AKKVHENDIVVAGSNFGCGSSREHAPL 70
Cdd:COG0066    6 LTGRAVPLdGDNIDTDQIIPARFLKTIDREGLGKHLFEDWRydrspdPDFvlnQPRYQGADILVAGRNFGCGSSREHAPW 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768  71 ALKGSKVSCVIAKSFARIFFRNAINIGVPVLECPN--TDRI------DDGDELEVDLSTGDIQNITkGETYQATpLPDFV 142
Cdd:COG0066   86 ALKDYGFRAVIAPSFADIFYRNAINNGLLPIELPEeaVDALfaaieaNPGDELTVDLEAGTVTNGT-GETYPFE-IDPFR 163

                        170
                 ....*....|....*.
gi 499329768 143 REIVDEgGLIEYARKL 158
Cdd:COG0066  164 RECLLN-GLDDIGLTL 178
IPMI_Swivel cd01577
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ...
 7-119 1.02e-38

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: 126.93  E-value: 1.02e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768   7 KFGDDVDTDAVIPGRYLifntpgelakytfegvrpdfakkvheNDIVVAGSNFGCGSSREHAPLALKGSKVSCVIAKSFA 86
Cdd:cd01577    1 LFGDNIDTDQIIPARFL--------------------------GDIIVAGKNFGCGSSREHAPWALKDAGIRAVIAESFA 54

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 499329768  87 RIFFRNAINIGV-PVLECP---NTDRIDDGDELEVDL 119
Cdd:cd01577   55 RIFFRNAINNGLlPVTLADedvEEVEAKPGDEVEVDL 91
Aconitase_C pfam00694
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ...
 8-105 2.57e-18

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: 75.87  E-value: 2.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768    8 FGDDVDTDAVIPGRYL-IFNTPGeLAKYTFEGVRPDFAK-----------------KVHENDIVV-AGSNFGCGSSREHA 68
Cdd:pfam00694  15 FNSNVDTDLIIPKQFLgTIANIG-IGNINFEGWRYGKVRylpdgenpdfydaamryKQHGAPIVViGGKNFGCGSSREHA 93

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 499329768   69 PLALKGSKVSCVIAKSFARIFFRNAINIGVPVLECPN 105
Cdd:pfam00694  94 AWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPE 130
 
Name Accession Description Interval E-value
leuD PRK00439
3-isopropylmalate dehydratase small subunit; Reviewed
 2-162 1.95e-105

3-isopropylmalate dehydratase small subunit; Reviewed


Pssm-ID: 234762 [Multi-domain]  Cd Length: 163  Bit Score: 298.28  E-value: 1.95e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768   2 EGRAWKFGDDVDTDAVIPGRYLIFNTPGELAKYTFEGVRPDFAKKVHENDIVVAGSNFGCGSSREHAPLALKGSKVSCVI 81
Cdd:PRK00439   1 KGRVWKFGDNIDTDVIIPARYLNTSDPQELAKHCMEDLDPEFAKKVKPGDIIVAGKNFGCGSSREHAPIALKAAGVSAVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768  82 AKSFARIFFRNAINIGVPVLECPNT-DRIDDGDELEVDLSTGDIQNITKGETYQATPLPDFVREIVDEGGLIEYARKLVS 160
Cdd:PRK00439  81 AKSFARIFYRNAINIGLPVLECDEAvDKIEDGDEVEVDLETGVITNLTTGEEYKFKPIPEFMLEILKAGGLIEYLKKKGR 160


                 ..
gi 499329768 161 ER 162
Cdd:PRK00439 161 FP 162
leud TIGR02084
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 3-157 2.69e-78

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 members of the seed for this model are those sequences which are gene clustered with other genes involved in leucine biosynthesis and include some archaea. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 131139 [Multi-domain]  Cd Length: 156  Bit Score: 229.29  E-value: 2.69e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768    3 GRAWKFGDDVDTDAVIPGRYLIFNTPGELAKYTFEGVRPDFAKKVHENDIVVAGSNFGCGSSREHAPLALKGSKVSCVIA 82
Cdd:TIGR02084   1 GKVHKYGDNVDTDVIIPARYLNTSDPKELAKHCMEDLDKDFVKKVKEGDIIVAGENFGCGSSREHAPIAIKASGISCVIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499329768   83 KSFARIFFRNAINIGVPVLECPN-TDRIDDGDELEVDLSTGDIQNITKGETYQATPLPDFVREIVDEGGLIEYARK 157
Cdd:TIGR02084  81 KSFARIFYRNAINIGLPIVESEEaVDEIEEGDEVEVDLEKGIIKNLTKGKEYKATPFPEFLQKIMKAGGLLNYVKK 156
LEUD_arch TIGR02087
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ...
 3-157 7.86e-76

3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the 3-isopropylmalate dehydratase, small subunits which form TIGR00171. This subfamily includes the members of TIGR02084 which are gene clustered with other genes of leucine biosynthesis. The rest of the subfamily includes mainly archaeal species which exhibit two hits to this model. In these cases it is possible that one or the other of the hits does not have a 3-isopropylmalate dehydratase activity but rather one of the other related aconitase-like activities.


Pssm-ID: 273961 [Multi-domain]  Cd Length: 154  Bit Score: 223.07  E-value: 7.86e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768    3 GRAWKFGDDVDTDAVIPGRYLIFNTPGELAKYTFEGVRPDFAKKVHENDIVVAGSNFGCGSSREHAPLALKGSKVSCVIA 82
Cdd:TIGR02087   1 GRVWKFGDDIDTDEIIPGRYLRTTDPDELASHAMEGIDPEFAKKVRPGDVIVAGKNFGCGSSREQAALALKAAGIAAVIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499329768   83 KSFARIFFRNAINIGVPVLECPnTDRIDDGDELEVDLSTGDIQnITKGETYQATPLPDFVREIVDEGGLIEYARK 157
Cdd:TIGR02087  81 ESFARIFYRNAINIGLPLIEAK-TEGIKDGDEVTVDLETGEIR-VNGNEEYKGEPLPDFLLEILREGGLLEYLKK 153
HacB2_Meth NF040625
homoaconitase small subunit;
1-154 4.32e-68

homoaconitase small subunit;


Pssm-ID: 468597 [Multi-domain]  Cd Length: 161  Bit Score: 203.79  E-value: 4.32e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768   1 MEGRAWKFGDDVDTDAVIPGRYLIFNTPGELAKYTFEGVRPDFAKKVHENDIVVAGSNFGCGSSREHAPLALKGSKVSCV 80
Cdd:NF040625   4 IKGKVWKFGDNIDTDVIIPGRYLRTFNPDDLASHVMEGERPDFTKNVQKGDIIVAGWNFGCGSSREQAPVAIKHAGVSAI 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499329768  81 IAKSFARIFFRNAINIGVPVLecpnTDRI--DDGDELEVDLSTGDIQNITKGETYQATPLPDFVREIVDEGGLIEY 154
Cdd:NF040625  84 IAKSFARIFYRNAINIGLPVI----VADIeaDDGDILSIDLEKGIIKNKTTGEEFKIQPFKEFMLEILEDGGLVNH 155
LeuD COG0066
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ...
 1-158 5.51e-63

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: 191.92  E-value: 5.51e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768   1 MEGRAWKF-GDDVDTDAVIPGRYLIFNTPGELAKYTFEGVR------PDF---AKKVHENDIVVAGSNFGCGSSREHAPL 70
Cdd:COG0066    6 LTGRAVPLdGDNIDTDQIIPARFLKTIDREGLGKHLFEDWRydrspdPDFvlnQPRYQGADILVAGRNFGCGSSREHAPW 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768  71 ALKGSKVSCVIAKSFARIFFRNAINIGVPVLECPN--TDRI------DDGDELEVDLSTGDIQNITkGETYQATpLPDFV 142
Cdd:COG0066   86 ALKDYGFRAVIAPSFADIFYRNAINNGLLPIELPEeaVDALfaaieaNPGDELTVDLEAGTVTNGT-GETYPFE-IDPFR 163

                        170
                 ....*....|....*.
gi 499329768 143 REIVDEgGLIEYARKL 158
Cdd:COG0066  164 RECLLN-GLDDIGLTL 178
PRK14023 PRK14023
homoaconitate hydratase small subunit; Provisional
 4-157 1.55e-57

homoaconitate hydratase small subunit; Provisional


Pssm-ID: 184460 [Multi-domain]  Cd Length: 166  Bit Score: 177.30  E-value: 1.55e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768   4 RAWKFGDDVDTDAVIPGRYLIFNT-PGELAKYTFEGVRPDFAKKVHENDIVVAGSNFGCGSSREHAPLALKGSKVSCVIA 82
Cdd:PRK14023   3 RVWKFGDNINTDDILPGKYAPFMVgEDRFHNYAFAHLRPEFASTVRPGDILVAGRNFGLGSSREYAPEALKMLGIGAIIA 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499329768  83 KSFARIFFRNAINIGVPVLECPN-TDRIDDGDELEVDLSTGDIqnITKGETYQATPLPDFVREIVDEGGLIEYARK 157
Cdd:PRK14023  83 KSYARIFYRNLVNLGIPPFESEEvVDALEDGDEVELDLETGVL--TRGGETFQLRPPPEFLLEALKEGSILEYYRK 156
IPMI_Swivel cd01577
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ...
 7-119 1.02e-38

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: 126.93  E-value: 1.02e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768   7 KFGDDVDTDAVIPGRYLifntpgelakytfegvrpdfakkvheNDIVVAGSNFGCGSSREHAPLALKGSKVSCVIAKSFA 86
Cdd:cd01577    1 LFGDNIDTDQIIPARFL--------------------------GDIIVAGKNFGCGSSREHAPWALKDAGIRAVIAESFA 54

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 499329768  87 RIFFRNAINIGV-PVLECP---NTDRIDDGDELEVDL 119
Cdd:cd01577   55 RIFFRNAINNGLlPVTLADedvEEVEAKPGDEVEVDL 91
PLN00072 PLN00072
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
 3-157 2.78e-34

3-isopropylmalate isomerase/dehydratase small subunit; Provisional


Pssm-ID: 177701 [Multi-domain]  Cd Length: 246  Bit Score: 120.35  E-value: 2.78e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768   3 GRAWKFGDDVDTDAVIPGRY--LIFNTPGE---LAKYTFEGVrPDFAKK--VHEND------IVVAGSNFGCGSSREHAP 69
Cdd:PLN00072  71 GLCFVVGDNIDTDQIIPAEYltLVPSKPDEyekLGSYALIGL-PAFYKTrfVEPGEmktkysIIIGGENFGCGSSREHAP 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768  70 LALKGSKVSCVIAKSFARIFFRNAINIGvPVLECPNTDRIDD----GDELEVDLSTGDIQNITKGETYQATPLPDfVREI 145
Cdd:PLN00072 150 VALGAAGAKAVVAESYARIFFRNSVATG-EVYPLESEVRICEecktGDVVTVELGNSVLINHTTGKEYKLKPIGD-AGPV 227

                        170
                 ....*....|..
gi 499329768 146 VDEGGLIEYARK 157
Cdd:PLN00072 228 IDAGGIFAYARK 239
PRK07229 PRK07229
aconitate hydratase; Validated
 7-157 1.58e-30

aconitate hydratase; Validated


Pssm-ID: 235974 [Multi-domain]  Cd Length: 646  Bit Score: 115.63  E-value: 1.58e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768   7 KFGDDVDTDAVIPG--RYLIF--NTPgELAKYTFEGVRPDFAKKVHEND--IVVAGSNFGCGSSREHAPLALK--GSKVs 78
Cdd:PRK07229 476 KVGDNITTDHIMPAgaKWLPYrsNIP-NISEFVFEGVDNTFPERAKEQGggIVVGGENYGQGSSREHAALAPRylGVKA- 553

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768  79 cVIAKSFARIFFRNAINIGVPVLECPNT---DRIDDGDELEVD-----LSTGDIQ--NITKGETYQAT-PLPDFVREIVD 147
Cdd:PRK07229 554 -VLAKSFARIHKANLINFGILPLTFADPadyDKIEEGDVLEIEdlrefLPGGPLTvvNVTKDEEIEVRhTLSERQIEILL 632

                        170
                 ....*....|
gi 499329768 148 EGGLIEYARK 157
Cdd:PRK07229 633 AGGALNLIKK 642
leuD PRK01641
3-isopropylmalate dehydratase small subunit;
9-144 5.75e-27

3-isopropylmalate dehydratase small subunit;


Pssm-ID: 179314 [Multi-domain]  Cd Length: 200  Bit Score: 100.20  E-value: 5.75e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768   9 GDDVDTDAVIPGRYLIFNTPGELAKYTFEGVR--------PDF---------AKkvhendIVVAGSNFGCGSSREHAPLA 71
Cdd:PRK01641  16 RANVDTDQIIPKQFLKRITRTGFGKGLFDDWRylddgqpnPDFvlnqpryqgAS------ILLAGDNFGCGSSREHAPWA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768  72 LKGSKVSCVIAKSFARIFFRNAINIGVP--VLECPNTDRI------DDGDELEVDLSTgdiQNITKGETYQATPLPDFVR 143
Cdd:PRK01641  90 LADYGFRAVIAPSFADIFYNNCFKNGLLpiVLPEEDVDELfklveaNPGAELTVDLEA---QTVTAPDKTFPFEIDPFRR 166


                 .
gi 499329768 144 E 144
Cdd:PRK01641 167 H 167
AcnA_Bact_Swivel cd01579
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ...
 7-119 2.07e-26

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: 96.35  E-value: 2.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768   7 KFGDDVDTDAVIPG--RYLIF--NTPgELAKYTFEGVRPDFAKKVHEND--IVVAGSNFGCGSSREHAPLALKGSKVSCV 80
Cdd:cd01579    1 KVGDNITTDHIMPAgaKVLPLrsNIP-AISEFVFHRVDPTFAERAKAAGpgFIVGGENYGQGSSREHAALAPMYLGVRAV 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 499329768  81 IAKSFARIFFRNAINIGVPVLECPNT---DRIDDGDELEVDL 119
Cdd:cd01579   80 LAKSFARIHRANLINFGILPLTFADEddyDRFEQGDQLELPL 121
Homoaconitase_Swivel cd01674
Homoaconitase swivel domain. This family includes homoaconitase and other uncharacterized ...
 10-104 5.12e-24

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: 90.81  E-value: 5.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768  10 DDVDTDAVIPGRYLIFN--TPGELAKYTFEGVRPDFAKKVHENDIVVAGSNFGCGSSREHAPLALKGSKVSCVIAKSFAR 87
Cdd:cd01674    4 DNLNTDGIYPGKYTYQDdiTPEKMAEVCMENYDSEFSTKTKQGDILVSGFNFGTGSSREQAATALLAKGIPLVVSGSFGN 83

                         90
                 ....*....|....*..
gi 499329768  88 IFFRNAINIGVPVLECP 104
Cdd:cd01674   84 IFSRNSINNALLSIELP 100
Aconitase_swivel cd00404
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ...
 51-118 1.61e-18

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: 75.20  E-value: 1.61e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499329768  51 DIVVAGSNFGCGSSREHAPLALKGSKVSCVIAKSFARIFFRNAINIGVPVLECP---NTDRIDDGDELEVD 118
Cdd:cd00404   17 GVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFAdpeDYLKLHTGDELDIY 87
Aconitase_C pfam00694
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ...
 8-105 2.57e-18

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: 75.87  E-value: 2.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768    8 FGDDVDTDAVIPGRYL-IFNTPGeLAKYTFEGVRPDFAK-----------------KVHENDIVV-AGSNFGCGSSREHA 68
Cdd:pfam00694  15 FNSNVDTDLIIPKQFLgTIANIG-IGNINFEGWRYGKVRylpdgenpdfydaamryKQHGAPIVViGGKNFGCGSSREHA 93

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 499329768   69 PLALKGSKVSCVIAKSFARIFFRNAINIGVPVLECPN 105
Cdd:pfam00694  94 AWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPE 130
leuD TIGR00171
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 11-136 1.52e-17

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: 75.62  E-value: 1.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768   11 DVDTDAVIPGRYLIFNTPGELAKYTFEGVR----------PDFAKKV---HENDIVVAGSNFGCGSSREHAPLALKGSKV 77
Cdd:TIGR00171  18 NVDTDAIIPKQFLKRITRTGFGKHLFFDWRfldangkepnPDFVLNQpqyQGASILLARENFGCGSSREHAPWALDDYGF 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499329768   78 SCVIAKSFARIFFRNAINIGVPVLECPNTDRID-------DGDELEVDLSTgdiQNITKGETYQAT 136
Cdd:TIGR00171  98 KVIIAPSFADIFYNNSFKNGLLPIRLSYDEVKElfgqvenQGLQMTVDLEN---QLIHDSEGKVYS 160
PTZ00092 PTZ00092
aconitate hydratase-like protein; Provisional
 8-161 7.28e-10

aconitate hydratase-like protein; Provisional


Pssm-ID: 240263 [Multi-domain]  Cd Length: 898  Bit Score: 56.56  E-value: 7.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768   8 FGDDVDTDAVIP----------GRYLI--------FNTPGE-------LAKYTFEGVR----------------P----- 41
Cdd:PTZ00092 678 LGDSITTDHISPagniaknspaAKYLMergverkdFNTYGArrgndevMVRGTFANIRlinklcgkvgpntvhvPtgekm 757

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768  42 ---DFAKKVHEND---IVVAGSNFGCGSSREHA---PlALKGskVSCVIAKSFARIFFRNAINIGVPVLECPNTDRID-- 110
Cdd:PTZ00092 758 siyDAAEKYKQEGvplIVLAGKEYGSGSSRDWAakgP-YLQG--VKAVIAESFERIHRSNLVGMGILPLQFLNGENADsl 834

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499329768 111 --DGDEL-EVDLSTGDI---QNIT----KGETYQATPLPDFVREI--VDEGGLIEYA-RKLVSE 161
Cdd:PTZ00092 835 glTGKEQfSIDLNSGELkpgQDVTvktdTGKTFDTILRIDTEVEVeyFKHGGILQYVlRKLVKG 898
AcnA COG1048
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ...
 52-130 6.20e-09

Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: Lysine biosynthesisTCA cycle


Pssm-ID: 440669 [Multi-domain]  Cd Length: 891  Bit Score: 53.57  E-value: 6.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768  52 IVVAGSNFGCGSSREHAplAlKGSK---VSCVIAKSFARIFFRNAINIGVPVLECPNTDRID----DGDElevdlsTGDI 124
Cdd:COG1048  763 VVLAGKEYGTGSSRDWA--A-KGTRllgVKAVIAESFERIHRSNLVGMGVLPLQFPEGESAEslglTGDE------TFDI 833


                 ....*.
gi 499329768 125 QNITKG 130
Cdd:COG1048  834 EGLDEG 839
acnA PRK12881
aconitate hydratase AcnA;
52-125 4.51e-07

aconitate hydratase AcnA;


Pssm-ID: 237246 [Multi-domain]  Cd Length: 889  Bit Score: 48.39  E-value: 4.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768  52 IVVAGSNFGCGSSREhapLALKGSK---VSCVIAKSFARIFFRNAINIGVPVLECPNTD-----RIDDGDELEVDLSTGD 123
Cdd:PRK12881 762 VVIAGEEYGTGSSRD---WAAKGTRllgVKAVIAESFERIHRSNLVGMGVLPLQFKGGDsrqslGLTGGETFDIEGLPGE 838


                 ..
gi 499329768 124 IQ 125
Cdd:PRK12881 839 IK 840
AcnA_Mitochon_Swivel cd01578
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ...
 35-118 1.35e-06

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: 45.54  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768  35 TFEGVrPDFAKKVHENDI---VVAGSNFGCGSSREHAPLALKGSKVSCVIAKSFARIFFRNAINIGVPVLECPNT---DR 108
Cdd:cd01578   53 EYGPV-PDTARDYKAHGIkwvVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPadyDK 131

                         90
                 ....*....|
gi 499329768 109 IDDGDELEVD 118
Cdd:cd01578  132 IHPDDKVDIL 141
AcnA_IRP_Swivel cd01580
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ...
 7-105 2.34e-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: 44.96  E-value: 2.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768   7 KFGDDVDTDAVIP----------GRYLI--------FNTPGE-------LAKYTFEGVRP-------------------- 41
Cdd:cd01580    1 LLGDSVTTDHISPagsiakdspaGKYLAergvkprdFNSYGSrrgndevMMRGTFANIRLrnklvpgteggtthhpptge 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499329768  42 -----DFAKKVHEND---IVVAGSNFGCGSSREhapLALKGSK---VSCVIAKSFARIFFRNAINIGVPVLECPN 105
Cdd:cd01580   81 vmsiyDAAMRYKEEGvplVILAGKEYGSGSSRD---WAAKGPFllgVKAVIAESFERIHRSNLVGMGILPLQFPP 152
PRK09277 PRK09277
aconitate hydratase AcnA;
52-114 9.32e-05

aconitate hydratase AcnA;


Pssm-ID: 236445 [Multi-domain]  Cd Length: 888  Bit Score: 41.65  E-value: 9.32e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768  52 IVVAGSNFGCGSSREHAplAlKGSK---VSCVIAKSFARIFFRNAINIGVPVLECPNTDRID----DGDE 114
Cdd:PRK09277 761 VVIAGKEYGTGSSRDWA--A-KGTRllgVKAVIAESFERIHRSNLVGMGVLPLQFKPGESRKtlglDGTE 827
PLN00070 PLN00070
aconitate hydratase
 7-98 1.10e-04

aconitate hydratase


Pssm-ID: 215047 [Multi-domain]  Cd Length: 936  Bit Score: 41.33  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768   7 KFGDDVDTDAVIP----------GRYLI--------FNTPGE-------LAKYTFEGVR-----------PdfaKKVH-- 48
Cdd:PLN00070 712 NFGDSITTDHISPagsihkdspaAKYLMergvdrkdFNSYGSrrgndeiMARGTFANIRivnkllkgevgP---KTVHip 788

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499329768  49 ------------------ENDIVVAGSNFGCGSSREHA---PLaLKGskVSCVIAKSFARIFFRNAINIGV 98
Cdd:PLN00070 789 tgeklsvfdaamkyksegHDTIILAGAEYGSGSSRDWAakgPM-LLG--VKAVIAKSFERIHRSNLVGMGI 856
PRK14812 PRK14812
hypothetical protein; Provisional
 62-148 2.99e-03

hypothetical protein; Provisional


Pssm-ID: 173273 [Multi-domain]  Cd Length: 119  Bit Score: 35.85  E-value: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329768  62 GSSREHAPLALKGSKVSCVIAKSFARIFFRNAINIGVPVLECPNTDR-----IDDGDELEVDLSTGDIqnitkgetyqAT 136
Cdd:PRK14812   3 GSSREHAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPREVReklaqLKPTDQVTVDLEQQKI----------IS 72

                         90
                 ....*....|..
gi 499329768 137 PLPDFVREIVDE 148
Cdd:PRK14812  73 PVEEFTFEIDSE 84
 
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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