NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|502733126|ref|WP_012968110|]
View 

MULTISPECIES: formate dehydrogenase-N subunit gamma [Klebsiella]

Protein Classification

formate dehydrogenase-N subunit gamma( domain architecture ID 10013450)

formate dehydrogenase-N subunit gamma is the cytochrome b556 component of the formate dehydrogenase-N (nitrate-inducible), and also contains a menaquinone reduction site that receives electrons from the beta subunit (FdnH), through its hemes

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK10179 PRK10179
formate dehydrogenase-N subunit gamma; Provisional
1-217 2.51e-137

formate dehydrogenase-N subunit gamma; Provisional


:

Pssm-ID: 182289  Cd Length: 217  Bit Score: 383.43  E-value: 2.51e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502733126   1 MSKSKMIVRTTFIDRACHWTVVICFFLVALSGISFFFPTLQWLTETFGTPQMGRILHPFFGVLIFVALMFMFVRFVHHNI 80
Cdd:PRK10179   1 MSKSKMIVRTKFIDRACHWTVVICFFLVALSGISFFFPTLQWLTQTFGTPQMGRILHPFFGIAIFVALMFMFVRFVHHNI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502733126  81 PDKQDIPWLKGIVEVLKGNEHKVARVGKYNAGQKMMFWTIMSMIFVLLVTGMIIWRPYFADYFPMQVIRYSLLIHATSAI 160
Cdd:PRK10179  81 PDKKDIPWLLNIVEVLKGNEHKVADVGKYNAGQKMMFWSIMSMIFVLLVTGVIIWRPYFAQYFPMQVVRYSLLIHAAAGI 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 502733126 161 ILIHAILIHMYMAFWVKGSIKGMIEGKVSRRWAKKHHPRWYRDVERLEAMKESREGM 217
Cdd:PRK10179 161 ILIHAILIHMYMAFWVKGSIKGMIEGKVSRRWAKKHHPRWYREIEKAEAKKESEEGI 217
 
Name Accession Description Interval E-value
PRK10179 PRK10179
formate dehydrogenase-N subunit gamma; Provisional
1-217 2.51e-137

formate dehydrogenase-N subunit gamma; Provisional


Pssm-ID: 182289  Cd Length: 217  Bit Score: 383.43  E-value: 2.51e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502733126   1 MSKSKMIVRTTFIDRACHWTVVICFFLVALSGISFFFPTLQWLTETFGTPQMGRILHPFFGVLIFVALMFMFVRFVHHNI 80
Cdd:PRK10179   1 MSKSKMIVRTKFIDRACHWTVVICFFLVALSGISFFFPTLQWLTQTFGTPQMGRILHPFFGIAIFVALMFMFVRFVHHNI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502733126  81 PDKQDIPWLKGIVEVLKGNEHKVARVGKYNAGQKMMFWTIMSMIFVLLVTGMIIWRPYFADYFPMQVIRYSLLIHATSAI 160
Cdd:PRK10179  81 PDKKDIPWLLNIVEVLKGNEHKVADVGKYNAGQKMMFWSIMSMIFVLLVTGVIIWRPYFAQYFPMQVVRYSLLIHAAAGI 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 502733126 161 ILIHAILIHMYMAFWVKGSIKGMIEGKVSRRWAKKHHPRWYRDVERLEAMKESREGM 217
Cdd:PRK10179 161 ILIHAILIHMYMAFWVKGSIKGMIEGKVSRRWAKKHHPRWYREIEKAEAKKESEEGI 217
FdnI COG2864
Cytochrome b subunit of formate dehydrogenase [Energy production and conversion];
1-215 2.56e-81

Cytochrome b subunit of formate dehydrogenase [Energy production and conversion];


Pssm-ID: 442111  Cd Length: 217  Bit Score: 241.68  E-value: 2.56e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502733126   1 MSKSKMIVRTTFIDRACHWTVVICFFLVALSGISFFFPTLQWLTETFGTPQMGRILHPFFGVLIFVALMFMFVRFVHHNI 80
Cdd:COG2864    1 GRSGRKILRFSLFERINHWLVAISFILLALTGLALFFPKFFWLTPLFGGPQWARILHRFAGVVFFVGFVLHFVYWLRHNL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502733126  81 PDKQDIPWLKGIVEVLKGNEHKVARVGKYNAGQKMMFWTIMSMIFVLLVTGMIIWRPYFADYFPMQVIRYSLLIHATSAI 160
Cdd:COG2864   81 PNKKDLKWLKKIGGFLGGKEEEHPPAGKYNAGQKLDFWAVILGGLVLGVSGLILWFPYFAQYFPIWVMRIALLVHAIAAI 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 502733126 161 ILIHAILIHMYMA-FWVKGSIKGMIEGKVSRRWAKKHHPRWYRDVERLEAMKESRE 215
Cdd:COG2864  161 LLIAAIIVHIYAAtLGVEGALRAMFTGYVDEEWAKEHHPLWYEELKAKGKLEERSA 216
formate-DH-gamm TIGR01583
formate dehydrogenase, gamma subunit; This model represents the gamma chain of the gamma ...
7-206 6.90e-60

formate dehydrogenase, gamma subunit; This model represents the gamma chain of the gamma proteobacteria (and Aquifex aolicus) formate dehydrogenase. This subunit is integral to the cytoplasmic membrane, consisting of 4 transmembrane helices, and receives electrons from the beta subunit. The entire E. coli formate dehydrogenase N (nitrate-inducible form) has been crystallized. The gamma subunit contains two cytochromes, heme b(P) and heme b(C) near the periplasmic and cytoplasmic sides of the membrane respectively. The electron acceptor quinone binds at the cytoplasmic heme histidine ligand. NiFe-hydrogenase and thiosulfate reductase contain homologous gamma subunits, and these can be found scoring in the noise of this model. [Energy metabolism, Anaerobic, Energy metabolism, Electron transport]


Pssm-ID: 130645  Cd Length: 204  Bit Score: 186.55  E-value: 6.90e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502733126    7 IVRTTFIDRACHWTVVICFFLVALSGISFFFPTLQWLTETFGTPQMGRILHPFFGVLIFVALMFMFVRFVHHNIPDKQDI 86
Cdd:TIGR01583   2 IYRFSLFDRILHWIAAISFLILVFTGFVMMFGKFFWLGVILGELWVAKNLHPFAGILFFISIIPMFLKWWRRMIPAKYDI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502733126   87 PWLKGIVEVLKGNEHKVARVGKYNAGQKMMFWTIMSMIFVLLVTGMIIWRPYFADY-FPMQVIRYSLLIHATSAIILIHA 165
Cdd:TIGR01583  82 RWMMKVGGYLSKIKRPVPSAGKYNAGQKSWYWILVLGGFLMIITGIFMWFLDFPSTaFSIELLRISALIHNFSAIILAVG 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 502733126  166 ILIHMYMAFW-VKGSIKGMIEGKVSRRWAKKHHPRWYRDVER 206
Cdd:TIGR01583 162 FIVHIYMAVFgVKGSIHGMVSGKVEETWAKIHHPYWYREVVN 203
Ni_hydr_CYTB pfam01292
Prokaryotic cytochrome b561; This family includes cytochrome b561 and related proteins, in ...
9-186 2.06e-12

Prokaryotic cytochrome b561; This family includes cytochrome b561 and related proteins, in addition to the nickel-dependent hydrogenases b-type cytochrome subunit. Cytochrome b561 is a secretory vesicle-specific electron transport protein. It is an integral membrane protein, that binds two heme groups non-covalently. This is a prokaryotic family. Members of the 'eukaryotic cytochrome b561' family can be found in Pfam: PF03188.


Pssm-ID: 426183  Cd Length: 180  Bit Score: 62.93  E-value: 2.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502733126    9 RTTFIDRACHWTVVICFFLVALSGISFFFPTLQWLTETFgtpqmGRILHPFFGvLIFVALMFMFVRFVHHNIPDKQDIPW 88
Cdd:pfam01292   1 RYSLPVRLLHWLNALLVILLLLTGLLIAFPEPLALLGAA-----GRNLHKSLG-LVLLALLLLRLLWRPKARFPRSDLLR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502733126   89 LKGIVEVLKGNEHKVARVGKYNAGQKM--MFWTIMSMIFVLLVTGMIIWRPYFADYFP--MQVIRYSLLIHATSAIILIH 164
Cdd:pfam01292  75 FELLRYLYLLLRGPHPPPGKYNPGQKLalVHLLLYLLLILLPLTGLLLYFPASASGFGvdGGLAELARLLHELLAWALLA 154
                         170       180
                  ....*....|....*....|....*.
gi 502733126  165 AILIHMYMAFWV----KGSIKGMIEG 186
Cdd:pfam01292 155 LVVLHIYAALFHhfrgKGTLKRMLTG 180
 
Name Accession Description Interval E-value
PRK10179 PRK10179
formate dehydrogenase-N subunit gamma; Provisional
1-217 2.51e-137

formate dehydrogenase-N subunit gamma; Provisional


Pssm-ID: 182289  Cd Length: 217  Bit Score: 383.43  E-value: 2.51e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502733126   1 MSKSKMIVRTTFIDRACHWTVVICFFLVALSGISFFFPTLQWLTETFGTPQMGRILHPFFGVLIFVALMFMFVRFVHHNI 80
Cdd:PRK10179   1 MSKSKMIVRTKFIDRACHWTVVICFFLVALSGISFFFPTLQWLTQTFGTPQMGRILHPFFGIAIFVALMFMFVRFVHHNI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502733126  81 PDKQDIPWLKGIVEVLKGNEHKVARVGKYNAGQKMMFWTIMSMIFVLLVTGMIIWRPYFADYFPMQVIRYSLLIHATSAI 160
Cdd:PRK10179  81 PDKKDIPWLLNIVEVLKGNEHKVADVGKYNAGQKMMFWSIMSMIFVLLVTGVIIWRPYFAQYFPMQVVRYSLLIHAAAGI 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 502733126 161 ILIHAILIHMYMAFWVKGSIKGMIEGKVSRRWAKKHHPRWYRDVERLEAMKESREGM 217
Cdd:PRK10179 161 ILIHAILIHMYMAFWVKGSIKGMIEGKVSRRWAKKHHPRWYREIEKAEAKKESEEGI 217
FdnI COG2864
Cytochrome b subunit of formate dehydrogenase [Energy production and conversion];
1-215 2.56e-81

Cytochrome b subunit of formate dehydrogenase [Energy production and conversion];


Pssm-ID: 442111  Cd Length: 217  Bit Score: 241.68  E-value: 2.56e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502733126   1 MSKSKMIVRTTFIDRACHWTVVICFFLVALSGISFFFPTLQWLTETFGTPQMGRILHPFFGVLIFVALMFMFVRFVHHNI 80
Cdd:COG2864    1 GRSGRKILRFSLFERINHWLVAISFILLALTGLALFFPKFFWLTPLFGGPQWARILHRFAGVVFFVGFVLHFVYWLRHNL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502733126  81 PDKQDIPWLKGIVEVLKGNEHKVARVGKYNAGQKMMFWTIMSMIFVLLVTGMIIWRPYFADYFPMQVIRYSLLIHATSAI 160
Cdd:COG2864   81 PNKKDLKWLKKIGGFLGGKEEEHPPAGKYNAGQKLDFWAVILGGLVLGVSGLILWFPYFAQYFPIWVMRIALLVHAIAAI 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 502733126 161 ILIHAILIHMYMA-FWVKGSIKGMIEGKVSRRWAKKHHPRWYRDVERLEAMKESRE 215
Cdd:COG2864  161 LLIAAIIVHIYAAtLGVEGALRAMFTGYVDEEWAKEHHPLWYEELKAKGKLEERSA 216
PRK10639 PRK10639
formate dehydrogenase cytochrome b556 subunit;
1-213 4.67e-78

formate dehydrogenase cytochrome b556 subunit;


Pssm-ID: 182608  Cd Length: 211  Bit Score: 233.13  E-value: 4.67e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502733126   1 MSKSKMIVRTTFIDRACHWTVVICFFLVALSGISFFFPTLQWLTETFGTPQMGRILHPFFGVLIFVALMFMFVRFVHHNI 80
Cdd:PRK10639   1 MKRRDTIVRYTAPERINHWIVAFCFILAAVSGLGFFFPSFNWLMNILGTPQLARILHPFVGVVMFASFIIMFFRYWHHNL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502733126  81 PDKQDIPWLKGIVEVLKGNEhkVARVGKYNAGQKMMFWTIMSMIFVLLVTGMIIWRPYFADYFPMQVIRYSLLIHATSAI 160
Cdd:PRK10639  81 INRDDIFWAKNIRKIVVNEE--VGDTGRYNFGQKCVFWAAIIFLVLLLVSGVIIWRPYFAPAFSIPVIRFALMLHSFAAV 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 502733126 161 ILIHAILIHMYMAFWVKGSIKGMIEGKVSRRWAKKHHPRWYRDVERLEAMKES 213
Cdd:PRK10639 159 ALIVVIMVHIYAALWVKGTITAMVEGWVTSAWAKKHHPRWYREVRKTTEKKAE 211
formate-DH-gamm TIGR01583
formate dehydrogenase, gamma subunit; This model represents the gamma chain of the gamma ...
7-206 6.90e-60

formate dehydrogenase, gamma subunit; This model represents the gamma chain of the gamma proteobacteria (and Aquifex aolicus) formate dehydrogenase. This subunit is integral to the cytoplasmic membrane, consisting of 4 transmembrane helices, and receives electrons from the beta subunit. The entire E. coli formate dehydrogenase N (nitrate-inducible form) has been crystallized. The gamma subunit contains two cytochromes, heme b(P) and heme b(C) near the periplasmic and cytoplasmic sides of the membrane respectively. The electron acceptor quinone binds at the cytoplasmic heme histidine ligand. NiFe-hydrogenase and thiosulfate reductase contain homologous gamma subunits, and these can be found scoring in the noise of this model. [Energy metabolism, Anaerobic, Energy metabolism, Electron transport]


Pssm-ID: 130645  Cd Length: 204  Bit Score: 186.55  E-value: 6.90e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502733126    7 IVRTTFIDRACHWTVVICFFLVALSGISFFFPTLQWLTETFGTPQMGRILHPFFGVLIFVALMFMFVRFVHHNIPDKQDI 86
Cdd:TIGR01583   2 IYRFSLFDRILHWIAAISFLILVFTGFVMMFGKFFWLGVILGELWVAKNLHPFAGILFFISIIPMFLKWWRRMIPAKYDI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502733126   87 PWLKGIVEVLKGNEHKVARVGKYNAGQKMMFWTIMSMIFVLLVTGMIIWRPYFADY-FPMQVIRYSLLIHATSAIILIHA 165
Cdd:TIGR01583  82 RWMMKVGGYLSKIKRPVPSAGKYNAGQKSWYWILVLGGFLMIITGIFMWFLDFPSTaFSIELLRISALIHNFSAIILAVG 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 502733126  166 ILIHMYMAFW-VKGSIKGMIEGKVSRRWAKKHHPRWYRDVER 206
Cdd:TIGR01583 162 FIVHIYMAVFgVKGSIHGMVSGKVEETWAKIHHPYWYREVVN 203
Ni_hydr_CYTB pfam01292
Prokaryotic cytochrome b561; This family includes cytochrome b561 and related proteins, in ...
9-186 2.06e-12

Prokaryotic cytochrome b561; This family includes cytochrome b561 and related proteins, in addition to the nickel-dependent hydrogenases b-type cytochrome subunit. Cytochrome b561 is a secretory vesicle-specific electron transport protein. It is an integral membrane protein, that binds two heme groups non-covalently. This is a prokaryotic family. Members of the 'eukaryotic cytochrome b561' family can be found in Pfam: PF03188.


Pssm-ID: 426183  Cd Length: 180  Bit Score: 62.93  E-value: 2.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502733126    9 RTTFIDRACHWTVVICFFLVALSGISFFFPTLQWLTETFgtpqmGRILHPFFGvLIFVALMFMFVRFVHHNIPDKQDIPW 88
Cdd:pfam01292   1 RYSLPVRLLHWLNALLVILLLLTGLLIAFPEPLALLGAA-----GRNLHKSLG-LVLLALLLLRLLWRPKARFPRSDLLR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502733126   89 LKGIVEVLKGNEHKVARVGKYNAGQKM--MFWTIMSMIFVLLVTGMIIWRPYFADYFP--MQVIRYSLLIHATSAIILIH 164
Cdd:pfam01292  75 FELLRYLYLLLRGPHPPPGKYNPGQKLalVHLLLYLLLILLPLTGLLLYFPASASGFGvdGGLAELARLLHELLAWALLA 154
                         170       180
                  ....*....|....*....|....*.
gi 502733126  165 AILIHMYMAFWV----KGSIKGMIEG 186
Cdd:pfam01292 155 LVVLHIYAALFHhfrgKGTLKRMLTG 180
 
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