NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1488174791|gb|RKP32443|]
View 

hypothetical protein METBISCDRAFT_25677 [Metschnikowia bicuspidata]

Protein Classification

NAD(P)-dependent oxidoreductase( domain architecture ID 10591880)

NAD(P)-dependent oxidoreductase similar to Bacillus subtilis precorrin-2 dehydrogenase, which catalyzes the dehydrogenation of precorrin-2 to form sirohydrochlorin, a precursor in both siroheme and adenosylcobalamin biosynthesis

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
NAD_binding_7 pfam13241
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
 8-106 7.34e-20

Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.


:

Pssm-ID: 433055 [Multi-domain]  Cd Length: 104  Bit Score: 80.21  E-value: 7.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488174791   8 LAWQIKDKPCLVIGA-------VKSYVPEDLNMYEnasdlgISyKDITEEHFQRIT--KAVFEEH---FACVCCCIDDPE 75
Cdd:pfam13241   1 LFLDLRGKRVLVVGGgevaarkARKLLEAGAKVTV------VS-PEITPFLEGLLDliRREFEGDldgADLVIAATDDPE 73

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1488174791  76 LSARIYHQCKYLRISVNITDMPPMCDFYFGS 106
Cdd:pfam13241  74 LNERIAALARARGILVNVADDPELCDFYFPA 104
 
Name Accession Description Interval E-value
NAD_binding_7 pfam13241
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
 8-106 7.34e-20

Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.


Pssm-ID: 433055 [Multi-domain]  Cd Length: 104  Bit Score: 80.21  E-value: 7.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488174791   8 LAWQIKDKPCLVIGA-------VKSYVPEDLNMYEnasdlgISyKDITEEHFQRIT--KAVFEEH---FACVCCCIDDPE 75
Cdd:pfam13241   1 LFLDLRGKRVLVVGGgevaarkARKLLEAGAKVTV------VS-PEITPFLEGLLDliRREFEGDldgADLVIAATDDPE 73

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1488174791  76 LSARIYHQCKYLRISVNITDMPPMCDFYFGS 106
Cdd:pfam13241  74 LNERIAALARARGILVNVADDPELCDFYFPA 104
CysG2 COG1648
Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and ...
 8-122 2.59e-13

Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and metabolism]; Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 441254 [Multi-domain]  Cd Length: 211  Bit Score: 65.56  E-value: 2.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488174791   8 LAWQIKDKPCLVIGA-----------------VKSYVPE---DLNMYENASDLGISYKDITEEHFqritkavfeEHFACV 67
Cdd:COG1648     6 IFLDLEGRRVLVVGGgevaarkarlllkagarVTVVAPEfspELAALAEEGRIELIKRAFEPEDL---------DGAFLV 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1488174791  68 CCCIDDPELSARIYHQCKYLRISVNITDMPPMCDFYFGSMYTDDAVQIMISTNGK 122
Cdd:COG1648    77 IAATDDEEVNARVAAAARARGILVNVVDDPELCDFIVPAIVDRGPLVIAISTGGA 131
cysG_Nterm TIGR01470
siroheme synthase, N-terminal domain; This model represents a subfamily of CysG N-terminal ...
 72-121 2.15e-08

siroheme synthase, N-terminal domain; This model represents a subfamily of CysG N-terminal region-related sequences. All sequences in the seed alignment for this model are N-terminal regions of known or predicted siroheme synthases. The C-terminal region of each is uroporphyrin-III C-methyltransferase (EC 2.1.1.107), which catalyzes the first step committed to the biosynthesis of either siroheme or cobalamin (vitamin B12) rather than protoheme (heme). The region represented by this model completes the process of oxidation and iron insertion to yield siroheme. Siroheme is a cofactor for nitrite and sulfite reductases, so siroheme synthase is CysG of cysteine biosynthesis in some organisms. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 130536 [Multi-domain]  Cd Length: 205  Bit Score: 52.02  E-value: 2.15e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1488174791  72 DDPELSARIYHQCKYLRISVNITDMPPMCDFYFGSMYTDDAVQIMISTNG 121
Cdd:TIGR01470  78 DDEELNRRVAHAARARGVPVNVVDDPELCSFIFPSIVDRSPVVVAISSGG 127
 
Name Accession Description Interval E-value
NAD_binding_7 pfam13241
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
 8-106 7.34e-20

Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.


Pssm-ID: 433055 [Multi-domain]  Cd Length: 104  Bit Score: 80.21  E-value: 7.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488174791   8 LAWQIKDKPCLVIGA-------VKSYVPEDLNMYEnasdlgISyKDITEEHFQRIT--KAVFEEH---FACVCCCIDDPE 75
Cdd:pfam13241   1 LFLDLRGKRVLVVGGgevaarkARKLLEAGAKVTV------VS-PEITPFLEGLLDliRREFEGDldgADLVIAATDDPE 73

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1488174791  76 LSARIYHQCKYLRISVNITDMPPMCDFYFGS 106
Cdd:pfam13241  74 LNERIAALARARGILVNVADDPELCDFYFPA 104
CysG2 COG1648
Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and ...
 8-122 2.59e-13

Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and metabolism]; Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 441254 [Multi-domain]  Cd Length: 211  Bit Score: 65.56  E-value: 2.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488174791   8 LAWQIKDKPCLVIGA-----------------VKSYVPE---DLNMYENASDLGISYKDITEEHFqritkavfeEHFACV 67
Cdd:COG1648     6 IFLDLEGRRVLVVGGgevaarkarlllkagarVTVVAPEfspELAALAEEGRIELIKRAFEPEDL---------DGAFLV 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1488174791  68 CCCIDDPELSARIYHQCKYLRISVNITDMPPMCDFYFGSMYTDDAVQIMISTNGK 122
Cdd:COG1648    77 IAATDDEEVNARVAAAARARGILVNVVDDPELCDFIVPAIVDRGPLVIAISTGGA 131
cysG_Nterm TIGR01470
siroheme synthase, N-terminal domain; This model represents a subfamily of CysG N-terminal ...
 72-121 2.15e-08

siroheme synthase, N-terminal domain; This model represents a subfamily of CysG N-terminal region-related sequences. All sequences in the seed alignment for this model are N-terminal regions of known or predicted siroheme synthases. The C-terminal region of each is uroporphyrin-III C-methyltransferase (EC 2.1.1.107), which catalyzes the first step committed to the biosynthesis of either siroheme or cobalamin (vitamin B12) rather than protoheme (heme). The region represented by this model completes the process of oxidation and iron insertion to yield siroheme. Siroheme is a cofactor for nitrite and sulfite reductases, so siroheme synthase is CysG of cysteine biosynthesis in some organisms. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 130536 [Multi-domain]  Cd Length: 205  Bit Score: 52.02  E-value: 2.15e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1488174791  72 DDPELSARIYHQCKYLRISVNITDMPPMCDFYFGSMYTDDAVQIMISTNG 121
Cdd:TIGR01470  78 DDEELNRRVAHAARARGVPVNVVDDPELCSFIFPSIVDRSPVVVAISSGG 127
 
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