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Conserved domains on  [gi|503973757|ref|WP_014207751|]
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MULTISPECIES: globin domain-containing protein [Acinetobacter]

Protein Classification

NO-inducible flavohemoprotein( domain architecture ID 1001654)

NO-inducible flavohemoprotein such as nitric oxide dioxygenase, which catalyzes the conversion of NO, O2, and NAD(P)H to NO3-, NAD(P)+, and H+, and is involved NO detoxification and NO signaling

CATH:  1.10.490.10
EC:  1.14.12.17
Gene Ontology:  GO:0016491|GO:0008941|GO:0020037|GO:0051409|GO:0071949|GO:0019825
PubMed:  11751864|9724711|10922365

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13289 super family cl36224
NO-inducible flavohemoprotein;
1-251 6.23e-78

NO-inducible flavohemoprotein;


The actual alignment was detected with superfamily member PRK13289:

Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 240.47  E-value: 6.23e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757   1 MTPQQIELVKSTVPVLREHGVTLTTYFYKRMLNNNPELKNVFNLDDQTSLRQPRALAAAVLAYAENIENPTVLAKAVERI 80
Cdd:PRK13289   2 LSAQTIAIVKATVPLLEEHGEALTAHFYDRMFSHNPELKNIFNQSNQRNGDQPEALANAVLAYARNIDNLEALLPAVERI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757  81 TTKHVSLDIQPDQYAIVGDNLLHSISEVLNVPFESELIEAWKQAYLQLADILIGVEKQKYEQLESLKGGWAGWRSFEITQ 160
Cdd:PRK13289  82 AQKHVSLQIKPEHYPIVGEHLLAAIREVLGDAATDEVLDAWGEAYGVLADVFIGREAEIYEEAASKPGGWRGWRDFRVVK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757 161 IDPlESG--KRFTLKATDHEDVLTSPANAFISVKVQVPEQQLEQPKAFKFTEAQEDNSYHFEVQPEENHTefsVANILLE 238
Cdd:PRK13289 162 KVP-ESEviTSFYLEPVDGGPVADFKPGQYLGVRLDPEGEEYQEIRQYSLSDAPNGKYYRISVKREAGGK---VSNYLHD 237

                        250
                 ....*....|...
gi 503973757 239 HYRVGDQVQVSAP 251
Cdd:PRK13289 238 HVNVGDVLELAAP 250
 
Name Accession Description Interval E-value
PRK13289 PRK13289
NO-inducible flavohemoprotein;
1-251 6.23e-78

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 240.47  E-value: 6.23e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757   1 MTPQQIELVKSTVPVLREHGVTLTTYFYKRMLNNNPELKNVFNLDDQTSLRQPRALAAAVLAYAENIENPTVLAKAVERI 80
Cdd:PRK13289   2 LSAQTIAIVKATVPLLEEHGEALTAHFYDRMFSHNPELKNIFNQSNQRNGDQPEALANAVLAYARNIDNLEALLPAVERI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757  81 TTKHVSLDIQPDQYAIVGDNLLHSISEVLNVPFESELIEAWKQAYLQLADILIGVEKQKYEQLESLKGGWAGWRSFEITQ 160
Cdd:PRK13289  82 AQKHVSLQIKPEHYPIVGEHLLAAIREVLGDAATDEVLDAWGEAYGVLADVFIGREAEIYEEAASKPGGWRGWRDFRVVK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757 161 IDPlESG--KRFTLKATDHEDVLTSPANAFISVKVQVPEQQLEQPKAFKFTEAQEDNSYHFEVQPEENHTefsVANILLE 238
Cdd:PRK13289 162 KVP-ESEviTSFYLEPVDGGPVADFKPGQYLGVRLDPEGEEYQEIRQYSLSDAPNGKYYRISVKREAGGK---VSNYLHD 237

                        250
                 ....*....|...
gi 503973757 239 HYRVGDQVQVSAP 251
Cdd:PRK13289 238 HVNVGDVLELAAP 250
FHP_Ae-globin-like cd14779
Globin domain of Alcaligenes eutrophus flavohemoglobin (FHP) and related proteins; ...
 1-140 4.66e-64

Globin domain of Alcaligenes eutrophus flavohemoglobin (FHP) and related proteins; Flavohemoglobins (flavoHbs) function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. NO scavenging by flavoHb maintains Medicago truncatula-Sinorhizobium meliloti symbiosis. Alcaligenes eutrophus FHP contains a phospholipid-binding site.


Pssm-ID: 381287  Cd Length: 140  Bit Score: 196.51  E-value: 4.66e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757   1 MTPQQIELVKSTVPVLREHGVTLTTYFYKRMLNNNPELKNVFNLDDQTSLRQPRALAAAVLAYAENIENPTVLAKAVERI 80
Cdd:cd14779    1 LTEQQKDLVKATVPVLKEHGVALTKHFYQRMFEHNPELKNVFNMGHQESGKQQQALAMAVLAYAENIDDPEVLLPVLKLI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757  81 TTKHVSLDIQPDQYAIVGDNLLHSISEVLNVPFESELIEAWKQAYLQLADILIGVEKQKY 140
Cdd:cd14779   81 AHKHVSLGIRAEQYPIVGEHLLASIKEVLGDAATDELISAWAAAYGQLADILIGMESKLY 140
Hmp COG1017
Hemoglobin-like flavoprotein [Energy production and conversion];
1-138 3.97e-47

Hemoglobin-like flavoprotein [Energy production and conversion];


Pssm-ID: 440640 [Multi-domain]  Cd Length: 135  Bit Score: 153.00  E-value: 3.97e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757   1 MTPQQIELVKSTVPVLREHGVTLTTYFYKRMLNNNPELKNVFNlddQTSLRQPRALAAAVLAYAENIENPTVLAKAVERI 80
Cdd:COG1017    1 LSPETIALVKASFPLVAPHGEEITARFYERLFELHPELRPLFN---GDMGEQRKALAAALAAYARNLDNLEALLPALERL 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 503973757  81 TTKHVSLDIQPDQYAIVGDNLLHSISEVLNVPFESELIEAWKQAYLQLADILIGVEKQ 138
Cdd:COG1017   78 GRKHVSYGVKPEHYPIVGEALLAALREVLGDAWTPEVAAAWAEAYGLLADVMIAAEAE 135
Globin pfam00042
Globin;
27-132 9.21e-04

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 38.04  E-value: 9.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757   27 FYKRMLNNNPELKNVF-----NLDDQTS----LRQPRALAAAVLAYAENIENPTVLAKAVERITTKHV-SLDIQPDQYAI 96
Cdd:pfam00042   3 ILARLFTAYPDTKAYFprfekSADDLKGspkfKAHGKKVLAALGEAVKHLDDLAALNAALKKLGARHKeKRGVDPANFKL 82

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 503973757   97 VGDNLLHSISEVLNvPFESELIEAWKQAYLQLADIL 132
Cdd:pfam00042  83 FGEALLVVLAEHLG-EFTPETKAAWDKALDVIAAAL 117
 
Name Accession Description Interval E-value
PRK13289 PRK13289
NO-inducible flavohemoprotein;
1-251 6.23e-78

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 240.47  E-value: 6.23e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757   1 MTPQQIELVKSTVPVLREHGVTLTTYFYKRMLNNNPELKNVFNLDDQTSLRQPRALAAAVLAYAENIENPTVLAKAVERI 80
Cdd:PRK13289   2 LSAQTIAIVKATVPLLEEHGEALTAHFYDRMFSHNPELKNIFNQSNQRNGDQPEALANAVLAYARNIDNLEALLPAVERI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757  81 TTKHVSLDIQPDQYAIVGDNLLHSISEVLNVPFESELIEAWKQAYLQLADILIGVEKQKYEQLESLKGGWAGWRSFEITQ 160
Cdd:PRK13289  82 AQKHVSLQIKPEHYPIVGEHLLAAIREVLGDAATDEVLDAWGEAYGVLADVFIGREAEIYEEAASKPGGWRGWRDFRVVK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757 161 IDPlESG--KRFTLKATDHEDVLTSPANAFISVKVQVPEQQLEQPKAFKFTEAQEDNSYHFEVQPEENHTefsVANILLE 238
Cdd:PRK13289 162 KVP-ESEviTSFYLEPVDGGPVADFKPGQYLGVRLDPEGEEYQEIRQYSLSDAPNGKYYRISVKREAGGK---VSNYLHD 237

                        250
                 ....*....|...
gi 503973757 239 HYRVGDQVQVSAP 251
Cdd:PRK13289 238 HVNVGDVLELAAP 250
FHP_Ae-globin-like cd14779
Globin domain of Alcaligenes eutrophus flavohemoglobin (FHP) and related proteins; ...
 1-140 4.66e-64

Globin domain of Alcaligenes eutrophus flavohemoglobin (FHP) and related proteins; Flavohemoglobins (flavoHbs) function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. NO scavenging by flavoHb maintains Medicago truncatula-Sinorhizobium meliloti symbiosis. Alcaligenes eutrophus FHP contains a phospholipid-binding site.


Pssm-ID: 381287  Cd Length: 140  Bit Score: 196.51  E-value: 4.66e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757   1 MTPQQIELVKSTVPVLREHGVTLTTYFYKRMLNNNPELKNVFNLDDQTSLRQPRALAAAVLAYAENIENPTVLAKAVERI 80
Cdd:cd14779    1 LTEQQKDLVKATVPVLKEHGVALTKHFYQRMFEHNPELKNVFNMGHQESGKQQQALAMAVLAYAENIDDPEVLLPVLKLI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757  81 TTKHVSLDIQPDQYAIVGDNLLHSISEVLNVPFESELIEAWKQAYLQLADILIGVEKQKY 140
Cdd:cd14779   81 AHKHVSLGIRAEQYPIVGEHLLASIKEVLGDAATDELISAWAAAYGQLADILIGMESKLY 140
FHb-globin cd08922
Globin domain of flavohemoglobins (flavoHbs); FlavoHbs function primarily as nitric oxide ...
 1-140 9.67e-61

Globin domain of flavohemoglobins (flavoHbs); FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. NO scavenging by flavoHb attenuates the expression of the nitrosative stress response, affects the swarming behavior of Escherichia coli, and maintains squid-Vibrio fischeri and Medicago truncatula-Sinorhizobium meliloti symbioses. FlavoHb expression affects Aspergillus nidulans sexual development and mycotoxin production, and Dictyostelium discoideum development. This family also includes some single-domain goblins (SDgbs).


Pssm-ID: 381260  Cd Length: 140  Bit Score: 187.78  E-value: 9.67e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757   1 MTPQQIELVKSTVPVLREHGVTLTTYFYKRMLNNNPELKNVFNLDDQTSLRQPRALAAAVLAYAENIENPTVLAKAVERI 80
Cdd:cd08922    1 LSEETIAIVKATAPVLAEHGEEITTRFYKRMFAEHPELKNLFNMANQASGRQPKALAAAVLAYAANIDNLEVLLPAVERI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757  81 TTKHVSLDIQPDQYAIVGDNLLHSISEVLNVPFESELIEAWKQAYLQLADILIGVEKQKY 140
Cdd:cd08922   81 AHKHVSLGVKPEHYPIVGEYLLEAIKEVLGDAATPEVLDAWAEAYGFLADILIEREKQLY 140
Hmp COG1017
Hemoglobin-like flavoprotein [Energy production and conversion];
1-138 3.97e-47

Hemoglobin-like flavoprotein [Energy production and conversion];


Pssm-ID: 440640 [Multi-domain]  Cd Length: 135  Bit Score: 153.00  E-value: 3.97e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757   1 MTPQQIELVKSTVPVLREHGVTLTTYFYKRMLNNNPELKNVFNlddQTSLRQPRALAAAVLAYAENIENPTVLAKAVERI 80
Cdd:COG1017    1 LSPETIALVKASFPLVAPHGEEITARFYERLFELHPELRPLFN---GDMGEQRKALAAALAAYARNLDNLEALLPALERL 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 503973757  81 TTKHVSLDIQPDQYAIVGDNLLHSISEVLNVPFESELIEAWKQAYLQLADILIGVEKQ 138
Cdd:COG1017   78 GRKHVSYGVKPEHYPIVGEALLAALREVLGDAWTPEVAAAWAEAYGLLADVMIAAEAE 135
FHb-globin_3 cd14783
Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function ...
 1-140 6.95e-46

Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways.


Pssm-ID: 271316  Cd Length: 140  Bit Score: 150.30  E-value: 6.95e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757   1 MTPQQIELVKSTVPVLREHGVTLTTYFYKRMLNNNPELKNVFNLDDQTSLRQPRALAAAVLAYAENIENPTVLAKAVERI 80
Cdd:cd14783    1 LSQKTIDIVKSTAPILEENGETLTRHFYKRMFEHNPEVKPFFNPAHQHSGSQQRALAAAICAYAANIDNLEVLGNAVELI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757  81 TTKHVSLDIQPDQYAIVGDNLLHSISEVLNVPFESELIEAWKQAYLQLADILIGVEKQKY 140
Cdd:cd14783   81 AQKHASLGIKPEHYPIVGSNLLASIREVLGDAATDDIIEAWSEAYGFLADILIGREKQIY 140
FHb_fungal-globin cd19754
Globin domain of fungal flavohemoglobin; FlavoHbs function primarily as nitric oxide ...
 1-140 1.15e-44

Globin domain of fungal flavohemoglobin; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. NO scavenging by flavoHb attenuates the expression of the nitrosative stress response, affects the swarming behavior of Escherichia coli, and maintains squid-Vibrio fischeri and Medicago truncatula-Sinorhizobium meliloti symbioses. FlavoHb expression affects Aspergillus nidulans sexual development and mycotoxin production, and Dictyostelium discoideum development.


Pssm-ID: 381294  Cd Length: 141  Bit Score: 147.10  E-value: 1.15e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757   1 MTPQQIELVKSTVPVLREHGVTLTTYFYKRMLNNNPELKNVFNLDDQTSLRQPRALAAAVLAYAENIENPTVLAKAVERI 80
Cdd:cd19754    1 LTPAQIKIIKDSVPILESLGVKLTEKFYKYMLKRYPEVKPYFNETNQKLLRQPKILAFALLQYAKNIDDLTPLSGFVEQI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503973757  81 TTKHVSLDIQPDQYAIVGDNLLHSISEVLnvPFES---ELIEAWKQAYLQLADILIGVEKQKY 140
Cdd:cd19754   81 VSKHVGLQVKPEHYPIVGECLIETMKELL--PEAVatdEFIEAWTTAYGNLANILIDAEKKEY 141
VtHb-like_SDgb cd14778
Vitreoscilla stercoraria hemoglobin and related proteins; single-domain globins; VtHb is ...
 1-140 1.97e-44

Vitreoscilla stercoraria hemoglobin and related proteins; single-domain globins; VtHb is homodimeric, and may both transport oxygen to terminal respiratory oxidases, and provide resistance to nitrosative stress. It has medium oxygen affinity and displays cooperative ligand-binding properties. VHb has biotechnological application, its expression in heterologous hosts (bacteria and plants) has improved growth and productivity under microaerobic conditions. Another member of this subfamily Campylobacter jejuni hemoglobin (Cgb) is monomeric, and plays a role in detoxifying NO. Along with a truncated globin Ctb, it is up-regulated by the transcription factor NssR in response to nitrosative stress.


Pssm-ID: 381286 [Multi-domain]  Cd Length: 140  Bit Score: 146.42  E-value: 1.97e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757   1 MTPQQIELVKSTVPVLREHGVTLTTYFYKRMLNNNPELKNVFNLDDQTSLRQPRALAAAVLAYAENIENPTVLAKAVERI 80
Cdd:cd14778    1 LDQQTIEIIKSTVPVLKEHGVEITTEFYKNMFTEYPEVRPMFDMEKQKSGEQPKALAMTVLAAAQNIENLEKIRPAVEKI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757  81 TTKHVSLDIQPDQYAIVGDNLLHSISEVLNVPFESELIEAWKQAYLQLADILIGVEKQKY 140
Cdd:cd14778   81 GKTHVNLNVKPEHYPIVGACLLGAIKEVLGDTATDEILEAWEKAYGEIAKIFIDVEKKLY 140
HmpPa-globin-like cd14780
Globin domain of Pseudomonas aeruginosa flavohemoglobin (HmpPa) and related proteins; ...
 1-140 5.79e-44

Globin domain of Pseudomonas aeruginosa flavohemoglobin (HmpPa) and related proteins; Flavohemoglobins (flavoHbs) function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. The physiological role of HmpPa is thought to be detoxification of NO under aerobic conditions.


Pssm-ID: 381288  Cd Length: 140  Bit Score: 145.29  E-value: 5.79e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757   1 MTPQQIELVKSTVPVLREHGVTLTTYFYKRMLNNNPELKNVFNLDDQTSLRQPRALAAAVLAYAENIENPTVLAKAVERI 80
Cdd:cd14780    1 LSPHQIAIIKATVPALEAHGEAITTHFYPLMFEEYPEVRALFNQAHQASGAQPRALANAVLAYARHIDRLEVLGGAVSLI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757  81 TTKHVSLDIQPDQYAIVGDNLLHSISEVLNVPFESELIEAWKQAYLQLADILIGVEKQKY 140
Cdd:cd14780   81 VNKHVSLNILPEHYPIVGTCLLRAIREVLGDAATDEVIEAWGAAYQQLADLLIAAEEAVY 140
Yhb1-globin-like cd14777
Globin domain of Saccharomyces cerevisiae flavohemoglobin (Yhb1p) and related domains; ...
 1-140 9.75e-44

Globin domain of Saccharomyces cerevisiae flavohemoglobin (Yhb1p) and related domains; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. S. cerevisiae Yhb1p has been shown to protect against nitrosative stress and to control ferric reductase activity; it may participate in regulating the activity of plasma membrane ferric reductase(s). Also included in this subfamily is Dictyostelium discoideum FlavoHb, the expression of which affects D. discoideum development.


Pssm-ID: 381285  Cd Length: 140  Bit Score: 144.79  E-value: 9.75e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757   1 MTPQQIELVKSTVPVLREHGVTLTTYFYKRMLNNNPELKNVFNLDDQTSLRQPRALAAAVLAYAENIENPTVLAKAVERI 80
Cdd:cd14777    1 LSEKTIQIVKSTVPVLKEKGTEITKRFYKRMFEEHPELLNIFNQTNQKKGLQQTALANTVYAAAKHIDNLEVILPVVKQI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757  81 TTKHVSLDIQPDQYAIVGDNLLHSISEVLNVPFESELIEAWKQAYLQLADILIGVEKQKY 140
Cdd:cd14777   81 AHKHRALGVKPEHYPIVGENLLAAIKEVLGDAATDEILEAWEKAYGVIADVFIEVEKEMY 140
HmpEc-globin-like cd14776
Globin domain of Escherichia coli flavohemoglobin (Hmp) and related proteins; Flavohemoglobins ...
 1-140 3.96e-43

Globin domain of Escherichia coli flavohemoglobin (Hmp) and related proteins; Flavohemoglobins (flavoHbs) function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. This subfamily includes Vibrio fischeri Hmp and E.coli Hmp. NO scavenging by flavoHb affects the swarming behavior of Escherichia coli, and protects against NO during initiation of the squid-Vibrio symbiosis. E.coli Hmp can catalyze the reduction of several alkylhydroperoxide substrates into their corresponding alcohols using NADH as an electron donor, and it has been suggested that it participates in the repair of the lipid membrane oxidative damage generated during oxidative/nitrosative stress.


Pssm-ID: 271309  Cd Length: 138  Bit Score: 142.99  E-value: 3.96e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757   1 MTPQQIELVKSTVPVLREHGVTLTTYFYKRMLNNNPELKNVFNLDDQTSLRQPRALAAAVLAYAENIENPTVLAKAVERI 80
Cdd:cd14776    1 LSAETIRIVKATIPLLAAAGPALTQHFYQRMLTHNPELKNIFNLAHQRTGRQPKALFDAVAAYAQNIRNLQALLPAVERI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757  81 TTKHVSLDIQPDQYAIVGDNLLHSISEVLnvPFESELIEAWKQAYLQLADILIGVEKQKY 140
Cdd:cd14776   81 AQKHTSFNIQPEQYQIVGEHLLATIEELA--PPDKDVLAAWAKAYQFLADIFIDREGEIY 138
FHb-globin_1 cd14781
Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function ...
 1-140 8.22e-40

Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. This subfamily may contain some single-domain goblins (SDgbs).


Pssm-ID: 381289  Cd Length: 139  Bit Score: 134.53  E-value: 8.22e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757   1 MTPQQIELVKSTVPVLREHGVTLTTYFYKRMLNNnPELKNVFNLDDQTSLRQPRALAAAVLAYAENIENPTVLAKAVERI 80
Cdd:cd14781    1 LSPHTIAIVKATVPALEEHGVAITAAMYKRLFED-PEIKALFNQAAQKSGEQPRALAGAILAYAKNIDNLGALGSAVERI 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757  81 TTKHVSLDIQPDQYAIVGDNLLHSISEVLNVPFESELIEAWKQAYLQLADILIGVEKQKY 140
Cdd:cd14781   80 AQKHVGLHIKPEHYPHVATALLGAIKDVLGDAATDEVLEAWGEAYWFLADILINREKQLY 139
FHb-globin_2 cd14782
Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function ...
 1-140 4.84e-28

Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways.


Pssm-ID: 381290  Cd Length: 143  Bit Score: 104.40  E-value: 4.84e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757   1 MTPQQIELVKSTVPVLREHGVTLTTYFYKRMLNNNPEL-KNVFNLDDQTSLRQPRALAAAVLAYAENIENPTV--LAKAV 77
Cdd:cd14782    1 LSAESAEVIRATLPVVGEHIEEITPLFYRRMFGEHPELlRNLFNRGNQASGEQQKALAASVAAFATHLVDPDAppPDSVL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503973757  78 ERITTKHVSLDIQPDQYAIVGDNLLHSISEVLNVPFESELIEAWKQAYLQLADILIGVEKQKY 140
Cdd:cd14782   81 SRIAHKHASLGITPEQYTIVHRHLFAAIAEVLGAAVTPEVAAAWDEVYWLMADQLIATEARLY 143
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 9-132 2.16e-13

myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) and single-domain globins: FHbs, Ngbs/neuroglobins, Cygb/cytoglobins, GbE/avian eye specific globin E, GbX/globin X, amphibian GbY/globin Y, Mb/myoglobin, HbA/hemoglobin-alpha, HbB/hemoglobin-beta, SDgbs/single-domain globins related to FHbs, and Adgb/androglobin. The M family exhibits the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments (named A through H). In Adgbs, the globin domain is split into two: helices C-H are followed by helices A-B and the two parts are separated by the IQ motif. Although rearranged, the globin domain of most Adgbs contains a number of conserved residues which play critical roles in heme-coordination and gas ligand binding. Adgbs have been omitted from this A-H helix cd.


Pssm-ID: 381254  Cd Length: 133  Bit Score: 65.17  E-value: 2.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757   9 VKSTVPVLREHGVTLTTYFYKRMLNNNPELKNVFNLDDQTSLRQPRALAAAVLAYA---------ENIENPTVLAKAVER 79
Cdd:cd01040    1 VKSSWARVKKDKEEFGVAIFLRLFEANPELKKLFPKFAGVDLDLKGSPEFKAHAKRvvgaldsliDNLDDPEALDALLRK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 503973757  80 ITTKHVSLDIQPDQYAIVGDNLLHSISEVLNVPFESELIEAWKQAYLQLADIL 132
Cdd:cd01040   81 LGKRHKRRGVTPEHFEVFGEALLETLEEVLGEAFTPEVEAAWRKLLDYIANAI 133
HGbI-like cd12131
Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a ...
 5-133 3.29e-13

Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a single-domain heme-containing protein isolated from Methylacidiphilum infernorum, an aerobic acidophilic and thermophilic methanotroph. M. infernorum grows optimally at pH 2.0 and 60C and its home is New Zealand's Hell's Gate geothermal park. The physiological role of HGbI has yet to be determined. It has an extremely strong resistance to auto-oxidation, and has fast oxygen-binding/slow release characteristics. Its CO on-rate is comparable to the O2 on-rate, and it is able to bind acetate with high affinity in the ferric state. The coordination of the heme iron changes in the ferrous form from pentacoordinate at low pH to predominantly hexacoordinate at high pH; in the ferric form, it is predominantly hexacoordinate at all pH.


Pssm-ID: 381269 [Multi-domain]  Cd Length: 128  Bit Score: 64.49  E-value: 3.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757   5 QIELVKSTVPVLREHGVTLTTYFYKRMLNNNPELKNVFNLDDQTSlrQPRALAAAVLAYAENIENPTVLAKAVERITTKH 84
Cdd:cd12131    1 QIELVQQSFAKVEPIADEAAALFYERLFELDPELKPLFKGTDMEE--QGRKLMAMLVLVVKGLDDLEALLPALQDLGRRH 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 503973757  85 VSLDIQPDQYAIVGDNLLHSISEVLNVPFESELIEAWKQAYLQLADILI 133
Cdd:cd12131   79 VKYGVKPEHYPLVGEALLWTLEEGLGDEWTPEVKQAWTDAYGILAGTMI 127
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 148-251 1.49e-12

FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain containing a B-type heme fused with a ferredoxin reductase-like FAD/NAD-binding domain. Flavohemoglobins detoxify nitric oxide (NO) via an NO dioxygenase reaction. The hemoglobin domain adopts a globin fold with an embedded heme molecule. Flavohemoglobins also have a C-terminal reductase domain with bindiing sites for FAD and NAD(P)H. This domain catalyzes the conversion of NO + O2 + NAD(P)H to NO3- + NAD(P)+. Instead of the oxygen transport function of hemoglobins, flavohemoglobins seem to act in NO dioxygenation and NO signalling.


Pssm-ID: 99781  Cd Length: 247  Bit Score: 65.27  E-value: 1.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757 148 GGWAGWRSFEITQIDPlESG--KRFTLKATDHEDVLTSPANAFISVKVQVPEQQLEQPKAFKFTEAQEDNSYHFEVQPEE 225
Cdd:cd06184    1 GGWRGFRPFVVARKVA-ESEdiTSFYLEPADGGPLPPFLPGQYLSVRVKLPGLGYRQIRQYSLSDAPNGDYYRISVKREP 79

                         90       100
                 ....*....|....*....|....*.
gi 503973757 226 NHTefsVANILLEHYRVGDQVQVSAP 251
Cdd:cd06184   80 GGL---VSNYLHDNVKVGDVLEVSAP 102
Mb-like_oxidoreductase cd19753
Globin domain of uncharacterized oxidoreductases containing a FAD/NADH binding domain; This ...
 9-125 1.04e-05

Globin domain of uncharacterized oxidoreductases containing a FAD/NADH binding domain; This subfamily is composed of uncharacterized proteins containing an N-terminal myoglobin-like (M family globin) domain and a C-terminal oxygenase reductase FAD/NADH binding domain belonging to the ferredoxin reductase (FNR) family and is usually part of multi-component bacterial oxygenases which oxidize hydrocarbons using oxygen as the oxidant. The domain architecture of this subfamily is similar to flavohemoglobins, which function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. NO scavenging by flavoHb attenuates the expression of the nitrosative stress response, affects the swarming behavior of Escherichia coli, and maintains squid-Vibrio fischeri and Medicago truncatula-Sinorhizobium meliloti symbioses.


Pssm-ID: 381293 [Multi-domain]  Cd Length: 121  Bit Score: 43.77  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757   9 VKSTVPVLREHGVTLTTYFYKRMLNNNPELKNVFNLDDQTslrQPRALAAAVLAYAENIENPTVLAKAVERITTKHVSLD 88
Cdd:cd19753    1 LRASLAAVEDGPDELARRFYARLFAEAPELRDLFPADMDA---QRDRLARALTHVVENLDDPDGLVPFLAQLGRDHRKYG 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 503973757  89 IQPDQYAIVGDNLLHSISEVLNVPFESELIEAWKQAY 125
Cdd:cd19753   78 VAPEHYPAVGAALLAALRHFAGEAWTPELEAAWAEAY 114
GbX cd12137
Globin_X (GbX); Zebrafish globin X (GbX) is expressed at low levels in neurons of the central ...
 1-123 1.96e-04

Globin_X (GbX); Zebrafish globin X (GbX) is expressed at low levels in neurons of the central nervous system, and appears to be associated with the sensory system. GbX is likely to be attached to the cell membrane via S-palmitoylation and N-myristoylation. It's unlikely to have a true respiratory function as it is membrane-associated. It has been suggested that it may protect the lipids in the cell membrane from oxidation or act as a redox-sensing or signaling protein. Zebrafish GbX is hexacoordinate, and displays cooperative O2 binding.


Pssm-ID: 271287  Cd Length: 145  Bit Score: 40.36  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757   1 MTPQQIELVKSTVPVLREHGVTLTTYFYKRMLNNNPELKNVF------NLDDQTSLRQPRALAAAVLAYAENI-----EN 69
Cdd:cd12137    1 LTERQKQLIESSWSILQEDIAKVGVIMFVRLFETHPDCKDAFfpfrdvDLEDLRHSKELRAHGLRVLSFVEKSlarlhQP 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 503973757  70 PTVLAKAVErITTKHVSLDIQPDQYAIVGDNLLHSISEVLNVPFESELIEAWKQ 123
Cdd:cd12137   81 DKLEELLHE-LGRKHYRYNAKVKYVDLVGQQFIFAIEPVLKEQWTPELEEAWKT 133
Globin pfam00042
Globin;
27-132 9.21e-04

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 38.04  E-value: 9.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757   27 FYKRMLNNNPELKNVF-----NLDDQTS----LRQPRALAAAVLAYAENIENPTVLAKAVERITTKHV-SLDIQPDQYAI 96
Cdd:pfam00042   3 ILARLFTAYPDTKAYFprfekSADDLKGspkfKAHGKKVLAALGEAVKHLDDLAALNAALKKLGARHKeKRGVDPANFKL 82

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 503973757   97 VGDNLLHSISEVLNvPFESELIEAWKQAYLQLADIL 132
Cdd:pfam00042  83 FGEALLVVLAEHLG-EFTPETKAAWDKALDVIAAAL 117
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
151-251 1.09e-03

Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 39.39  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757 151 AGWRSFEITQIDPLESG-KRFTLKATDHEDVLTSPANAFISVKVQVPEQqlEQPKAFKFTEAQEDNSYHFEVQPEENHtE 229
Cdd:COG1018    1 AGFRPLRVVEVRRETPDvVSFTLEPPDGAPLPRFRPGQFVTLRLPIDGK--PLRRAYSLSSAPGDGRLEITVKRVPGG-G 77

                         90       100
                 ....*....|....*....|..
gi 503973757 230 FSvaNILLEHYRVGDQVQVSAP 251
Cdd:COG1018   78 GS--NWLHDHLKVGDTLEVSGP 97
class1-2_nsHbs_Lbs cd08923
Class1 nonsymbiotic hemoglobins (nsHbs), class II nsHbs, leghemoglobins (Lbs,) and related ...
 2-129 5.04e-03

Class1 nonsymbiotic hemoglobins (nsHbs), class II nsHbs, leghemoglobins (Lbs,) and related proteins; Class1 nsHbs include the dimeric hexacoordinate Trema tomentosa nsHb and the dimeric hexacoordinate nsHb from monocot barley. Also belonging to this family is ParaHb, a dimeric pentacoordinate Hb from the root nodules of Parasponia andersonii, a non-legume capable of symbiotic nitrogen fixation. ParaHb is unusual in that it has different heme redox potentials for each subunit; it may have evolved from class1 nsHbs. Lbs are pentacoordinate, and facilitate the diffusion of O2 to the respiring Rhizobium bacteroids within root nodules. They may have evolved from class 2 nonsymbiotic hemoglobins (class2 nsHb).


Pssm-ID: 381261  Cd Length: 147  Bit Score: 36.31  E-value: 5.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757   2 TPQQIELVKSTVPVLREHGVTLTTYFYKRMLNNNPELKNVFN-LDDQTSLRQ--PRALAAAVLAYAENIENPTVLAKA-- 76
Cdd:cd08923    2 TEKQEALVKSSWEVLKKNIPQLSLRFFLLILEIAPAAKDMFSfLKDSDEIPEnnPKLKAHAMKVFKMTCESAIQLRKKgk 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503973757  77 -------VERITTKHVSLDIQPDQYAIVGDNLLHSISEVLNVPFESELIEAWKQAYLQLA 129
Cdd:cd08923   82 vvvadttLKRLGSVHLKKGVADPHFEVVKEALLKTIKEAVGDKWSEEMKCAWGEAYDQLA 141
 
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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