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Conserved domains on  [gi|1736059156|gb|KAA0541004|]
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hydroxymyristoyl-ACP dehydratase [Citrobacter portucalensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FabA super family cl42624
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 15-115 1.76e-06

3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and metabolism]; 3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase is part of the Pathway/BioSystem: Fatty acid biosynthesis


The actual alignment was detected with superfamily member COG0764:

Pssm-ID: 440527  Cd Length: 141  Bit Score: 43.65  E-value: 1.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059156  15 QAEIVLQLDPSLFWFSGHFSVQPLLPGV------AQLNWAMDYATTLLVPG---WRFHSIQNVKFQSPLLPEATVTLSLS 85
Cdd:COG0764    28 SIVAEKNVTPNEPFFQGHFPGDPVMPGVlileamAQLGGFLLLKSEGLEGKgrlVYFLGIDKVKFRGPVVPGDTLTLEVE 107

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1736059156  86 WQEARQ-MLSFSYQ-RHDGDVrhtASSGKIRL 115
Cdd:COG0764   108 IKRVRRgIGKADGKaTVDGKL---VAEAELTF 136
 
Name Accession Description Interval E-value
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 15-115 1.76e-06

3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and metabolism]; 3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440527  Cd Length: 141  Bit Score: 43.65  E-value: 1.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059156  15 QAEIVLQLDPSLFWFSGHFSVQPLLPGV------AQLNWAMDYATTLLVPG---WRFHSIQNVKFQSPLLPEATVTLSLS 85
Cdd:COG0764    28 SIVAEKNVTPNEPFFQGHFPGDPVMPGVlileamAQLGGFLLLKSEGLEGKgrlVYFLGIDKVKFRGPVVPGDTLTLEVE 107

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1736059156  86 WQEARQ-MLSFSYQ-RHDGDVrhtASSGKIRL 115
Cdd:COG0764   108 IKRVRRgIGKADGKaTVDGKL---VAEAELTF 136
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 23-78 1.67e-03

FabA-like domain; This enzyme domain has a HotDog fold.


Pssm-ID: 429766  Cd Length: 132  Bit Score: 35.72  E-value: 1.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1736059156  23 DPSLFWFSGHFSVQPLLPGV------AQLNWAMDYATTLLVPGWRFHSIQNVKFQSPLLPEA 78
Cdd:pfam07977  34 TPNEWFFQGHFPGDPVMPGVlgleamAQLMGFYAIWSGGGEGRGRARGVDEVKFRGQVTPGD 95
FabA_FabZ cd00493
FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct ...
 23-82 2.53e-03

FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct enzyme types of the dissociative, type II, fatty acid synthase system (found in bacteria and plants) required to complete successive cycles of fatty acid elongation. The third step of the elongation cycle, the dehydration of beta-hydroxyacyl-ACP to trans-2-acyl-ACP, is catalyzed by FabA or FabZ. FabA is bifunctional and catalyzes an additional isomerization reaction of trans-2-acyl-ACP to cis-3-acyl-ACP, an essential reaction to unsaturated fatty acid synthesis. FabZ is the primary dehydratase that participates in the elongation cycles of saturated as well as unsaturated fatty acid biosynthesis, whereas FabA is more active in the dehydration of beta-hydroxydecanoyl-ACP. The FabA structure is homodimeric with two independent active sites located at the dimer interface.


Pssm-ID: 238275  Cd Length: 131  Bit Score: 35.34  E-value: 2.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059156  23 DPSLFWFSGHFSVQPLLPGV------AQLN--WAMDYATTLLVPGWRFH--SIQNVKFQSPLLPEATVTL 82
Cdd:cd00493    28 TPNEPFFQGHFPGDPVMPGVlgieamAQAAaaLAGLLGLGKGNPPRLGYlaGVRKVKFRGPVLPGDTLTL 97
PRK13188 PRK13188
bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R) ...
 29-76 4.65e-03

bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase; Reviewed


Pssm-ID: 237296 [Multi-domain]  Cd Length: 464  Bit Score: 35.29  E-value: 4.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1736059156  29 FSGHFSVQPLLPGVAQLNwAMDYATTLLV------PGWR---FHSIQNVKFQSPLLP 76
Cdd:PRK13188  363 FQGHFPGNPVMPGVLQIE-AMAQTGGILVlntvpdPENYstyFMKIDKVKFRQKVVP 418
 
Name Accession Description Interval E-value
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 15-115 1.76e-06

3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and metabolism]; 3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440527  Cd Length: 141  Bit Score: 43.65  E-value: 1.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059156  15 QAEIVLQLDPSLFWFSGHFSVQPLLPGV------AQLNWAMDYATTLLVPG---WRFHSIQNVKFQSPLLPEATVTLSLS 85
Cdd:COG0764    28 SIVAEKNVTPNEPFFQGHFPGDPVMPGVlileamAQLGGFLLLKSEGLEGKgrlVYFLGIDKVKFRGPVVPGDTLTLEVE 107

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1736059156  86 WQEARQ-MLSFSYQ-RHDGDVrhtASSGKIRL 115
Cdd:COG0764   108 IKRVRRgIGKADGKaTVDGKL---VAEAELTF 136
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 23-78 1.67e-03

FabA-like domain; This enzyme domain has a HotDog fold.


Pssm-ID: 429766  Cd Length: 132  Bit Score: 35.72  E-value: 1.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1736059156  23 DPSLFWFSGHFSVQPLLPGV------AQLNWAMDYATTLLVPGWRFHSIQNVKFQSPLLPEA 78
Cdd:pfam07977  34 TPNEWFFQGHFPGDPVMPGVlgleamAQLMGFYAIWSGGGEGRGRARGVDEVKFRGQVTPGD 95
PS-DH pfam14765
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ...
 36-115 2.25e-03

Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. Structural analysis shows these DH domains are double hotdogs in which the active site contains a histidine from the N-terminal hotdog and an aspartate from the C-terminal hotdog. Studies have uncovered that a substrate tunnel formed between the DH domains may be essential for loading substrates and unloading products.


Pssm-ID: 434191  Cd Length: 296  Bit Score: 36.20  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059156  36 QPLLPGVAQLNWAMDyATTLLVPGWRFHSIQNVKFQSPL-LPEAT-----VTLSLSWQEARQMLSF---SYQRHDGD-VR 105
Cdd:pfam14765  38 TVVLPGAGYLEMALE-AARQLFGGSGAVALRDVSILKALvLPEDDpvevqTSLTPEEDGADSWWEFeifSRAGGGWEwTL 116

                          90
                  ....*....|
gi 1736059156 106 HtaSSGKIRL 115
Cdd:pfam14765 117 H--ATGTVRL 124
FabA_FabZ cd00493
FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct ...
 23-82 2.53e-03

FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct enzyme types of the dissociative, type II, fatty acid synthase system (found in bacteria and plants) required to complete successive cycles of fatty acid elongation. The third step of the elongation cycle, the dehydration of beta-hydroxyacyl-ACP to trans-2-acyl-ACP, is catalyzed by FabA or FabZ. FabA is bifunctional and catalyzes an additional isomerization reaction of trans-2-acyl-ACP to cis-3-acyl-ACP, an essential reaction to unsaturated fatty acid synthesis. FabZ is the primary dehydratase that participates in the elongation cycles of saturated as well as unsaturated fatty acid biosynthesis, whereas FabA is more active in the dehydration of beta-hydroxydecanoyl-ACP. The FabA structure is homodimeric with two independent active sites located at the dimer interface.


Pssm-ID: 238275  Cd Length: 131  Bit Score: 35.34  E-value: 2.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059156  23 DPSLFWFSGHFSVQPLLPGV------AQLN--WAMDYATTLLVPGWRFH--SIQNVKFQSPLLPEATVTL 82
Cdd:cd00493    28 TPNEPFFQGHFPGDPVMPGVlgieamAQAAaaLAGLLGLGKGNPPRLGYlaGVRKVKFRGPVLPGDTLTL 97
PRK13188 PRK13188
bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R) ...
 29-76 4.65e-03

bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase; Reviewed


Pssm-ID: 237296 [Multi-domain]  Cd Length: 464  Bit Score: 35.29  E-value: 4.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1736059156  29 FSGHFSVQPLLPGVAQLNwAMDYATTLLV------PGWR---FHSIQNVKFQSPLLP 76
Cdd:PRK13188  363 FQGHFPGNPVMPGVLQIE-AMAQTGGILVlntvpdPENYstyFMKIDKVKFRQKVVP 418
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 27-82 9.11e-03

FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily catalyzes the dehydration of beta-hydroxyacyl-ACP to trans-2-acyl-ACP, the third step in the elongation phase of the bacterial/ plastid, type II, fatty-acid biosynthesis pathway.


Pssm-ID: 238615  Cd Length: 131  Bit Score: 33.67  E-value: 9.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1736059156  27 FWFSGHFSVQPLLPGV------AQlnwAMDYATTLLVPGWR-----FHSIQNVKFQSPLLPEATVTL 82
Cdd:cd01288    33 PFFQGHFPGNPIMPGVliiealAQ---AAGILGLKSLEDFEgklvyFAGIDKARFRKPVVPGDQLIL 96
 
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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