NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15597389|ref|NP_250883|]
View 

hydrogen cyanide synthase subunit HcnA [Pseudomonas aeruginosa PAO1]

Protein Classification

(2Fe-2S)-binding protein( domain architecture ID 10607402)

(2Fe-2S)-binding protein such as Pseudomonas aeruginosa hydrogen cyanide synthase subunit HcnA, part of a three-component membrane-bound flavoenzyme that catalyzes the formation of hydrogen cyanide, a secondary metabolite, by transfer of electrons to a cyanide-resistant branch of the aerobic respiratory chain

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Fer2_4 pfam13510
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
19-95 2.34e-22

2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which a beta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated. This cluster appears within sarcosine oxidase proteins.


:

Pssm-ID: 433268 [Multi-domain]  Cd Length: 82  Bit Score: 82.59  E-value: 2.34e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597389    19 TIHLNGQPVAAAAGETVLNVLNAVGLRRLARNDHGQASGAFCGMGVCHCCLVAIDGRPKRRACQTVVRPGMRVETES 95
Cdd:pfam13510   5 TFTFDGRPVTAPEGDTIAAALLANGVRVPRSCKYGRPRGIFCAMGECRNCLVEVDGVPNVRACTTPVREGMVVRTQN 81
 
Name Accession Description Interval E-value
Fer2_4 pfam13510
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
19-95 2.34e-22

2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which a beta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated. This cluster appears within sarcosine oxidase proteins.


Pssm-ID: 433268 [Multi-domain]  Cd Length: 82  Bit Score: 82.59  E-value: 2.34e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597389    19 TIHLNGQPVAAAAGETVLNVLNAVGLRRLARNDHGQASGAFCGMGVCHCCLVAIDGRPKRRACQTVVRPGMRVETES 95
Cdd:pfam13510   5 TFTFDGRPVTAPEGDTIAAALLANGVRVPRSCKYGRPRGIFCAMGECRNCLVEVDGVPNVRACTTPVREGMVVRTQN 81
NuoG COG1034
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ...
18-95 2.93e-08

NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440657 [Multi-domain]  Cd Length: 453  Bit Score: 49.45  E-value: 2.93e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597389  18 MTIHLNGQPVAAAAGETVLNVLNAVGL---RrlarndhgqasgaFC---GMGV---CHCCLVAIDGRPKRR-ACQTVVRP 87
Cdd:COG1034   2 VTITIDGKEVEVPKGTTVLQAAEKAGIeipR-------------FCyhpKLSIagaCRMCLVEVEGAPKPVaSCATPVTD 68

                ....*...
gi 15597389  88 GMRVETES 95
Cdd:COG1034  69 GMVVKTDS 76
PRK08493 PRK08493
NADH-quinone oxidoreductase subunit G;
17-103 2.69e-06

NADH-quinone oxidoreductase subunit G;


Pssm-ID: 236277 [Multi-domain]  Cd Length: 819  Bit Score: 43.93  E-value: 2.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597389   17 DMTIHLNGQPVAAAAGETVLNVlnavglrrlARndhgqASGAF----CGMG------VCHCCLVAIDGrpKR-RACQTVV 85
Cdd:PRK08493   1 MITITINGKECEAQEGEYILNV---------AR-----RNGIFipaiCYLSgcsptlACRLCMVEADG--KRvYSCNTKA 64
                         90
                 ....*....|....*...
gi 15597389   86 RPGMRVETESNRFDQEER 103
Cdd:PRK08493  65 KEGMNILTNTPNLMDERN 82
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
19-92 1.17e-04

2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 37.37  E-value: 1.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597389  19 TIHLNGQPVAAAAGETVLNVLNAVGLRRLArndhgqasgaFCGMGVCHCCLVAID-----------------GRPKRRAC 81
Cdd:cd00207   4 NVPGSGVEVEVPEGETLLDAAREAGIDIPY----------SCRAGACGTCKVEVVegevdqsdpslldeeeaEGGYVLAC 73
                        90
                ....*....|.
gi 15597389  82 QTVVRPGMRVE 92
Cdd:cd00207  74 QTRVTDGLVIE 84
 
Name Accession Description Interval E-value
Fer2_4 pfam13510
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
19-95 2.34e-22

2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which a beta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated. This cluster appears within sarcosine oxidase proteins.


Pssm-ID: 433268 [Multi-domain]  Cd Length: 82  Bit Score: 82.59  E-value: 2.34e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597389    19 TIHLNGQPVAAAAGETVLNVLNAVGLRRLARNDHGQASGAFCGMGVCHCCLVAIDGRPKRRACQTVVRPGMRVETES 95
Cdd:pfam13510   5 TFTFDGRPVTAPEGDTIAAALLANGVRVPRSCKYGRPRGIFCAMGECRNCLVEVDGVPNVRACTTPVREGMVVRTQN 81
NuoG COG1034
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ...
18-95 2.93e-08

NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440657 [Multi-domain]  Cd Length: 453  Bit Score: 49.45  E-value: 2.93e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597389  18 MTIHLNGQPVAAAAGETVLNVLNAVGL---RrlarndhgqasgaFC---GMGV---CHCCLVAIDGRPKRR-ACQTVVRP 87
Cdd:COG1034   2 VTITIDGKEVEVPKGTTVLQAAEKAGIeipR-------------FCyhpKLSIagaCRMCLVEVEGAPKPVaSCATPVTD 68

                ....*...
gi 15597389  88 GMRVETES 95
Cdd:COG1034  69 GMVVKTDS 76
PRK08493 PRK08493
NADH-quinone oxidoreductase subunit G;
17-103 2.69e-06

NADH-quinone oxidoreductase subunit G;


Pssm-ID: 236277 [Multi-domain]  Cd Length: 819  Bit Score: 43.93  E-value: 2.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597389   17 DMTIHLNGQPVAAAAGETVLNVlnavglrrlARndhgqASGAF----CGMG------VCHCCLVAIDGrpKR-RACQTVV 85
Cdd:PRK08493   1 MITITINGKECEAQEGEYILNV---------AR-----RNGIFipaiCYLSgcsptlACRLCMVEADG--KRvYSCNTKA 64
                         90
                 ....*....|....*...
gi 15597389   86 RPGMRVETESNRFDQEER 103
Cdd:PRK08493  65 KEGMNILTNTPNLMDERN 82
CutS COG2080
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ...
15-93 1.27e-05

Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and conversion]; Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 441683 [Multi-domain]  Cd Length: 155  Bit Score: 41.23  E-value: 1.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597389  15 RADMTIHLNGQP--VAAAAGETVLNVLnavglrrlaRNDHGQAS---GafCGMGVCHCCLVAIDGRPkRRACQT-VVR-P 87
Cdd:COG2080   1 MMMITLTVNGKPveVDVDPDTPLLDVL---------RDDLGLTGtkfG--CGHGQCGACTVLVDGKA-VRSCLTlAVQaD 68

                ....*.
gi 15597389  88 GMRVET 93
Cdd:COG2080  69 GKEITT 74
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
41-92 3.21e-05

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 40.89  E-value: 3.21e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597389   41 AVGLRRL-ARNDHGQASGAFCGMGVCHCCLVAIDGRPkRRACQTVV-------RPGMRVE 92
Cdd:PRK12576  38 TEALRRIkEEQDPTLSYRASCHMAVCGSCGMKINGEP-RLACKTLVldvakkyNSVITIE 96
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
19-92 1.17e-04

2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 37.37  E-value: 1.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597389  19 TIHLNGQPVAAAAGETVLNVLNAVGLRRLArndhgqasgaFCGMGVCHCCLVAID-----------------GRPKRRAC 81
Cdd:cd00207   4 NVPGSGVEVEVPEGETLLDAAREAGIDIPY----------SCRAGACGTCKVEVVegevdqsdpslldeeeaEGGYVLAC 73
                        90
                ....*....|.
gi 15597389  82 QTVVRPGMRVE 92
Cdd:cd00207  74 QTRVTDGLVIE 84
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
18-103 1.30e-04

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 39.33  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597389   18 MTIHLNGQPVAAAAGETVLNVLNAVGLR--RLARNDHGQASGAfcgmgvCHCCLVAIDGrpKRR---ACQTVVRPGMRVE 92
Cdd:PRK12814   4 ISLTINGRSVTAAPGTSILEAAASAGITipTLCFHQELEATGS------CWMCIVEIKG--KNRfvpACSTAVSEGMVIE 75
                         90
                 ....*....|.
gi 15597389   93 TESNRFDQEER 103
Cdd:PRK12814  76 TENAELHAMRR 86
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
27-86 5.41e-04

2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which abeta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated.


Pssm-ID: 432963 [Multi-domain]  Cd Length: 107  Bit Score: 36.06  E-value: 5.41e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597389    27 VAAAAGETVLNVLNAVglrrlarNDHGQASGAF---CGMGVCHCCLVAIDGRPkRRACQTVVR 86
Cdd:pfam13085  23 VPYEEGMTVLDALNKI-------KEEQDPTLAFrrsCREGICGSCAMNINGKP-RLACKTLID 77
ThiS COG2104
Sulfur carrier protein ThiS (thiamine biosynthesis) [Coenzyme transport and metabolism]; ...
18-92 1.00e-03

Sulfur carrier protein ThiS (thiamine biosynthesis) [Coenzyme transport and metabolism]; Sulfur carrier protein ThiS (thiamine biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 441707 [Multi-domain]  Cd Length: 66  Bit Score: 34.66  E-value: 1.00e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597389  18 MTIHLNGQPVAAAAGETVLNVLNAVGL--RRLArndhgqasgafcgmgvchcclVAIDGR--PKRRACQTVVRPGMRVE 92
Cdd:COG2104   1 MKITVNGEPREVPEGTTLADLLEELGLdpKGVA---------------------VAVNGEivPRSQWASTVLKEGDRVE 58
Fdx COG0633
Ferredoxin [Energy production and conversion];
19-93 1.95e-03

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 34.44  E-value: 1.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597389  19 TIHLNGQPVAAAAGETVLNVLNAVGLRRLARndhgqasgafCGMGVCHCCLVAI-DGRPKRR----------------AC 81
Cdd:COG0633   5 TFIPEGHTVEVPAGESLLEAALRAGIDLPYS----------CRSGACGTCHVRVlEGEVDHReedalsdeeraagsrlAC 74
                        90
                ....*....|..
gi 15597389  82 QTVVRPGMRVET 93
Cdd:COG0633  75 QARPTSDLVVEL 86
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
27-86 1.97e-03

Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440247 [Multi-domain]  Cd Length: 230  Bit Score: 35.49  E-value: 1.97e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597389  27 VAAAAGETVLNVLNAVglrrlarNDHGQASGAF---CGMGVCHCCLVAIDGRPkRRACQTVVR 86
Cdd:COG0479  25 VPVSPGMTVLDALDYI-------KEEQDPTLAFrrsCREGICGSCAMVINGRP-RLACQTHVR 79
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH