1L5J


Conserved Protein Domain Family
AcnB_Swivel
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cd01576: AcnB_Swivel 
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Aconitase B swivel domain. Aconitate hydratase B is involved in energy metabolism as part of the TCA cycle. It catalyses the formation of cis-aconitate from citrate. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. The domain structure of Aconitase B is different from other Aconitases in that he swivel domain that is found at N-terminus of B family is normally found at C-terminus for other Aconitases. In most members of the family, there is also a HEAT domain before domain 4, which is believed to play a role in protein-protein interaction.
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Statistics
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PSSM-Id: 238808
Aligned: 9 rows
Threshold Bit Score: 182.289
Created: 16-Jul-2004
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
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substrate
Conserved site includes 3 residues -Click on image for an interactive view with Cn3D
Feature 1:substrate binding site [chemical binding site]
Evidence:
  • Structure:1L5J_A binds aconitase; contacts at 3.5A
  • Comment:These residues participate in the active site of the catalytic domain.
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Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
Feature 1                                                                                 ###   
1L5J_A      171 FKVTGETNTDDLSPAPDAWSRPDIPLHALAMLknaregiepdqpgvvgpikqiealqqkgfPLAYVGd-VVGTGSSRKSA 249  Escherichia coli
P74582      172 FKVPGETNTDDLSPAPHATTRPDIPLHALAMLeakmpeglgt----------iaelkqkghPVAYVGd-VVGTGSSRKSA 240  Synechocystis s...
CAB84989    171 FKVDGETNTDDLSPAPDAWSRPDIPLHALAMLknprdgitpdkpgevgpiklleelkakghPVAYVGd-VVGTGSSRKSA 249  Neisseria menin...
P56418      174 FKIDGETNTDDLSPASDAFTRSDIPLHAKAMLknrienyeqr----------ikaiktkgvPVAYVGd-VVGTGSSRKSA 242  Helicobacter py...
AAL45528    178 IAAEGDISTDLLSPGNQAHSRSDRQLHGQCMIspeaqaeiva----------lqqqhpdkrVMLIAEkgTMGVGSSRMSG 247  Agrobacterium t...
AAM71785    174 FKVPGETNTDDLSPASEAFTRSDIPMHALSMLrskmddpiat----------iaqlkekgyPLAYVGd-VVGTGSSRKSG 242  Chlorobium tepi...
ZP_00021985 171 FKVPGETNTDDLSPAPDATTRPDIPMHALAMLknkreg-----------------aafqpeEDGKRGpvKFIESLKDKGP 233  Wautersia metal...
ZP_00054840 171 FKVTGETNTDDLSPAPDAWSRPDIPLHALAMLknprpgieadepgnrgplkqleglakkgnLVAYVGd-VVGTGSSRKSA 249  Magnetospirillu...
ZP_00147947 170 FKVDGEINTDDFSPASAAWSRPDIPLHALEMGttrfpggiee----------iakwrgeghEVAFVAd-VVGTGSSRKSA 238  Methanococcoide...

Feature 1                                                                           
1L5J_A      250 TnSVLWFMGDDIPHVPNKr--GGGLCLGGKIAPIFFNTMEDAGaLPIEVdvsnl----nmgdVIDVYP 311  Escherichia coli
P74582      241 InSVLWHIGTDIPFVPNKr--AGGYILGGKIAPIFFNTAEDSGaLPIECdvnql----ntgdVITIYP 302  Synechocystis sp. PCC 6803
CAB84989    250 TnSVIWHTGEDIPFVPNKr--FGGVCLGGKIAPIFFNTQEDSGaLPIEVdvsal----kmgdVVDILP 311  Neisseria meningitidis Z2491
P56418      243 TnSIMWHFGKDIPFVPNKr--SGGIVIGGVIAPIFFATCEDSGaLPIVAdvkdl----kegdLIKIYP 304  Helicobacter pylori
AAL45528    248 VnNVALWTGKQASPYVPFvnyAPIVAGTNGISPIFATTVDVTGgIGINLknwvkklgedgkpILNNDG 315  Agrobacterium tumefaciens s...
AAM71785    243 InSVQWHLGEDIPAVPNKr--TAGVVIGGIIAPIFFNTAEDSGaLPIQAdvts------memGDVIDL 302  Chlorobium tepidum TLS
ZP_00021985 234 PgGLRWRCGRYRLQPQVGh--QLGAVVHWRRHPVRAEQAFRWR-VPGQQdc---------sdLLQHDG 289  Wautersia metallidurans
ZP_00054840 250 TnSVLWFTGEDIPFVPNKr--FGGVCLGTKIAPIFYNTMEDAGaLPIELdvnqm----nmgdVVELRP 311  Magnetospirillum magnetotac...
ZP_00147947 239 CnSVLWHIGKDIPHVPNKr--RDCVIIGTAIAPIFFNTAEDSGaLPLQMdiskl----qhgdIITINT 300  Methanococcoides burtonii D...

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