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Conserved domains on  [gi|37956444|gb|AAP15391|]
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NifD, partial [Desulfuromonas michiganensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Oxidoreductase_nitrogenase super family cl02775
The nitrogenase enzyme system catalyzes the ATP-dependent reduction of dinitrogen to ammonia. ...
 5-151 5.03e-94

The nitrogenase enzyme system catalyzes the ATP-dependent reduction of dinitrogen to ammonia. This group contains both alpha and beta subunits of component 1 of the three known genetically distinct types of nitrogenase systems: a molybdenum-dependent nitrogenase (Mo-nitrogenase), a vanadium-dependent nitrogenase (V-nitrogenase), and an iron-only nitrogenase (Fe-nitrogenase) and, both subunits of Protochlorophyllide (Pchlide) reductase and chlorophyllide (chlide) reductase. The nitrogenase systems consist of component 1 (MoFe protein, VFe protein or, FeFe protein respectively) and, component 2 (Fe protein). The most widespread and best characterized nitrogenase is the Mo-nitrogenase. MoFe is an alpha2beta2 tetramer, the alternative nitrogenases are alpha2beta2delta2 hexamers whose alpha and beta subunits are similar to the alpha and beta subunits of MoFe. For MoFe, each alphabeta pair contains one P-cluster (at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein contains a single [4Fe-4S] cluster from which, electrons are transferred to the P-cluster of the MoFe and in turn, to FeMoCo at the site of substrate reduction. The V-nitrogenase requires an iron-vanadium cofactor (FeVco), the iron only-nitrogenase an iron only cofactor (FeFeco). These cofactors are analogous to the FeMoco. The V-nitrogenase has P clusters identical to those of MoFe. Pchlide reductase and chlide reductase participate in the Mg-branch of the tetrapyrrole biosynthetic pathway. Pchlide reductase catalyzes the reduction of the D-ring of Pchlide during the synthesis of chlorophylls (Chl) and bacteriochlorophylls (BChl). Chlide-a reductase catalyzes the reduction of the B-ring of Chlide-a during the synthesis of BChl-a. The Pchlide reductase NB complex is a an N2B2 heterotetramer resembling nitrogenase FeMo, N and B proteins are homologous to the FeMo alpha and beta subunits respectively. The NB complex may serve as a catalytic site for Pchlide reduction and, the ZY complex as a site of chlide reduction, similar to MoFe for nitrogen reduction.


The actual alignment was detected with superfamily member TIGR01282:

Pssm-ID: 445915  Cd Length: 466  Bit Score: 279.63  E-value: 5.03e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37956444     5 FFGPTKIEESLRAIGERFDDTIKANVEKVIAKYEPVMQAVLDEYKPRLEGKTAMLFVGGLRPRHTVGAYEDLGIQITGSG 84
Cdd:TIGR01282 286 FFGPTKIAESLRKIAEFFDDEIKEKAEEVIAKYQPAVDAVIAKYRPRLEGKTVMLYVGGLRPRHVIGAFEDLGMEVIGTG 365

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37956444    85 YEFAHQDDYDRTAPEMAKGTIIYDDVSEFELEKFVEEFKPDLVGSGIKEKYVFQKSGIPFRQMHSWD 151
Cdd:TIGR01282 366 YEFAHNDDYERTTKYMKDGTLIYDDVTHYEFEEFVEKLKPDLVGSGIKEKYVFQKMGVPFRQMHSWD 432
 
Name Accession Description Interval E-value
nifD TIGR01282
nitrogenase molybdenum-iron protein alpha chain; Nitrogenase consists of alpha (NifD) and beta ...
 5-151 5.03e-94

nitrogenase molybdenum-iron protein alpha chain; Nitrogenase consists of alpha (NifD) and beta (NifK) subunits of the molybdenum-iron protein and an ATP-binding iron-sulfur protein (NifH). This model describes a large clade of NifD proteins, but excludes a lineage that contains putative NifD and NifD homologs from species with vanadium-dependent nitrogenases. [Central intermediary metabolism, Nitrogen fixation]


Pssm-ID: 162284  Cd Length: 466  Bit Score: 279.63  E-value: 5.03e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37956444     5 FFGPTKIEESLRAIGERFDDTIKANVEKVIAKYEPVMQAVLDEYKPRLEGKTAMLFVGGLRPRHTVGAYEDLGIQITGSG 84
Cdd:TIGR01282 286 FFGPTKIAESLRKIAEFFDDEIKEKAEEVIAKYQPAVDAVIAKYRPRLEGKTVMLYVGGLRPRHVIGAFEDLGMEVIGTG 365

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37956444    85 YEFAHQDDYDRTAPEMAKGTIIYDDVSEFELEKFVEEFKPDLVGSGIKEKYVFQKSGIPFRQMHSWD 151
Cdd:TIGR01282 366 YEFAHNDDYERTTKYMKDGTLIYDDVTHYEFEEFVEKLKPDLVGSGIKEKYVFQKMGVPFRQMHSWD 432
Nitrogenase_MoFe_alpha cd01976
Nitrogenase_MoFe_alpha_II: Nitrogenase MoFe protein, beta subunit. A group of proteins similar ...
 5-151 8.32e-94

Nitrogenase_MoFe_alpha_II: Nitrogenase MoFe protein, beta subunit. A group of proteins similar to the alpha subunit of the MoFe protein of the molybdenum (Mo-) nitrogenase. The nitrogenase enzyme catalyzes the ATP-dependent reduction of dinitrogen to ammonia. The Mo-nitrogenase is the most widespread and best characterized of these systems. Mo-nitrogenase consists of the MoFe protein (component 1) and the Fe protein (component 2). MoFe is an alpha2beta2 tetramer. Each alphabeta pair of MoFe contains one P-cluster (at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein contains a single [4Fe-4S] cluster. Electrons are transferred from the [4Fe-4S] cluster of the Fe protein to the P-cluster of the MoFe and in turn to FeMoCo, the site of substrate reduction.


Pssm-ID: 238935 [Multi-domain]  Cd Length: 421  Bit Score: 277.68  E-value: 8.32e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37956444   5 FFGPTKIEESLRAIGERFDDTIKANVEKVIAKYEPVMQAVLDEYKPRLEGKTAMLFVGGLRPRHTVGAYEDLGIQITGSG 84
Cdd:cd01976 251 FFGPTKIAESLRKIAAYFDDEITAKTEEVIAEYKPAMEAVIAKYRPRLEGKTVMLYVGGLRPRHYIGAYEDLGMEVVGTG 330

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37956444  85 YEFAHQDDYDRTAPEMAKGTIIYDDVSEFELEKFVEEFKPDLVGSGIKEKYVFQKSGIPFRQMHSWD 151
Cdd:cd01976 331 YEFAHRDDYERTEVIPKEGTLLYDDVTHYELEEFVKRLKPDLIGSGIKEKYVFQKMGIPFRQMHSWD 397
NifD/CfbD COG2710
Nitrogenase Mo-Fe protein NifD/coenzyme F430 biosynthesis subunit CfbD [Coenzyme transport and ...
 5-151 2.31e-41

Nitrogenase Mo-Fe protein NifD/coenzyme F430 biosynthesis subunit CfbD [Coenzyme transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 442027 [Multi-domain]  Cd Length: 416  Bit Score: 142.18  E-value: 2.31e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37956444   5 FFGPTKIEESLRAIGERFDDTIkanvEKVIAKYEPVMQAVLDEYKPRLEGKTAMLFVGGLRPRHTVGAYEDLGIQITGSG 84
Cdd:COG2710 238 PIGLEATDEFLRKLAELFGKPV----PEVIARERGRLVDALADYHFYLGGKKVAIYGDPDLLWGLASFLLELGMEPVAAV 313

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37956444  85 YEFAHQDDYDRTAPEMAKGTI--IYDDVSEFELEKFVEEFKPDLVGSGIKEKYVFQKSGIPFRQMHSWD 151
Cdd:COG2710 314 TTTGSPEDYERIKELLEELPEgtVIDDGDLEELEELLKELKPDLLIGGSKGKYLARKLGIPLLRVGFPI 382
Oxidored_nitro pfam00148
Nitrogenase component 1 type Oxidoreductase;
3-144 4.98e-29

Nitrogenase component 1 type Oxidoreductase;


Pssm-ID: 395096 [Multi-domain]  Cd Length: 398  Bit Score: 109.26  E-value: 4.98e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37956444     3 STFFGPTKIEESLRAIGERFDdtiKANVEKVIAKYEPVMQAVLDEYKPRLEGKTAMLFVGGLRPRHTVGAYEDLGIQITG 82
Cdd:pfam00148 223 GAPIGLEATDRFLRALAKLFG---KEVAPEVIARERGRLLDAMVDYHEYLAGKRVAIYGDPDLVLGLARFLLELGMEPVA 299

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37956444    83 SGYEFAHQDDYDRTAPEMAKGT-IIYDDVSEFELEKFVEEFKPDLVGSGIKEKYVFQKSGIPF 144
Cdd:pfam00148 300 VGTGTGHPDDYERLKAELEEGDpEVIDGADLEELEELIKELKPDLLLGNSKGRYIARKLGIPL 362
PRK14477 PRK14477
bifunctional nitrogenase molybdenum-cofactor biosynthesis protein NifE/NifN; Provisional
 4-144 2.83e-22

bifunctional nitrogenase molybdenum-cofactor biosynthesis protein NifE/NifN; Provisional


Pssm-ID: 172952 [Multi-domain]  Cd Length: 917  Bit Score: 91.73  E-value: 2.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37956444    4 TFFGPTKIEESLRAIGERFDD--------TIKANVEKVIAKYEPVMQAVLDEYKPRLEGKTAMLFVGGLRPRHTVGAYED 75
Cdd:PRK14477 262 SFYGMTDTAKALRDIARELDDaggglekrVLQDRVEKLIAEEEAKCRAALAPYRARLEGKRVVLFTGGVKTWSMVNALRE 341

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37956444   76 LGIQITGSGYEFAHQDDYDRTAPEMAKGTIIYDDVSEFELEKFVEEFKPDLVGSGIKEKYVFQKSGIPF 144
Cdd:PRK14477 342 LGVEVLAAGTQNSTLEDFARMKALMHKDAHIIEDTSTAGLLRVMREKMPDLIVAGGKTKFLALKTRTPF 410
 
Name Accession Description Interval E-value
nifD TIGR01282
nitrogenase molybdenum-iron protein alpha chain; Nitrogenase consists of alpha (NifD) and beta ...
 5-151 5.03e-94

nitrogenase molybdenum-iron protein alpha chain; Nitrogenase consists of alpha (NifD) and beta (NifK) subunits of the molybdenum-iron protein and an ATP-binding iron-sulfur protein (NifH). This model describes a large clade of NifD proteins, but excludes a lineage that contains putative NifD and NifD homologs from species with vanadium-dependent nitrogenases. [Central intermediary metabolism, Nitrogen fixation]


Pssm-ID: 162284  Cd Length: 466  Bit Score: 279.63  E-value: 5.03e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37956444     5 FFGPTKIEESLRAIGERFDDTIKANVEKVIAKYEPVMQAVLDEYKPRLEGKTAMLFVGGLRPRHTVGAYEDLGIQITGSG 84
Cdd:TIGR01282 286 FFGPTKIAESLRKIAEFFDDEIKEKAEEVIAKYQPAVDAVIAKYRPRLEGKTVMLYVGGLRPRHVIGAFEDLGMEVIGTG 365

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37956444    85 YEFAHQDDYDRTAPEMAKGTIIYDDVSEFELEKFVEEFKPDLVGSGIKEKYVFQKSGIPFRQMHSWD 151
Cdd:TIGR01282 366 YEFAHNDDYERTTKYMKDGTLIYDDVTHYEFEEFVEKLKPDLVGSGIKEKYVFQKMGVPFRQMHSWD 432
Nitrogenase_MoFe_alpha cd01976
Nitrogenase_MoFe_alpha_II: Nitrogenase MoFe protein, beta subunit. A group of proteins similar ...
 5-151 8.32e-94

Nitrogenase_MoFe_alpha_II: Nitrogenase MoFe protein, beta subunit. A group of proteins similar to the alpha subunit of the MoFe protein of the molybdenum (Mo-) nitrogenase. The nitrogenase enzyme catalyzes the ATP-dependent reduction of dinitrogen to ammonia. The Mo-nitrogenase is the most widespread and best characterized of these systems. Mo-nitrogenase consists of the MoFe protein (component 1) and the Fe protein (component 2). MoFe is an alpha2beta2 tetramer. Each alphabeta pair of MoFe contains one P-cluster (at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein contains a single [4Fe-4S] cluster. Electrons are transferred from the [4Fe-4S] cluster of the Fe protein to the P-cluster of the MoFe and in turn to FeMoCo, the site of substrate reduction.


Pssm-ID: 238935 [Multi-domain]  Cd Length: 421  Bit Score: 277.68  E-value: 8.32e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37956444   5 FFGPTKIEESLRAIGERFDDTIKANVEKVIAKYEPVMQAVLDEYKPRLEGKTAMLFVGGLRPRHTVGAYEDLGIQITGSG 84
Cdd:cd01976 251 FFGPTKIAESLRKIAAYFDDEITAKTEEVIAEYKPAMEAVIAKYRPRLEGKTVMLYVGGLRPRHYIGAYEDLGMEVVGTG 330

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37956444  85 YEFAHQDDYDRTAPEMAKGTIIYDDVSEFELEKFVEEFKPDLVGSGIKEKYVFQKSGIPFRQMHSWD 151
Cdd:cd01976 331 YEFAHRDDYERTEVIPKEGTLLYDDVTHYELEEFVKRLKPDLIGSGIKEKYVFQKMGIPFRQMHSWD 397
Nitrogenase_MoFe_alpha_like cd01967
Nitrogenase_MoFe_alpha_like: Nitrogenase MoFe protein, alpha subunit_like. The nitrogenase ...
 4-151 5.77e-65

Nitrogenase_MoFe_alpha_like: Nitrogenase MoFe protein, alpha subunit_like. The nitrogenase enzyme catalyzes the ATP-dependent reduction of dinitrogen to ammonia. Three genetically distinct types of nitrogenase systems are known to exist: a molybdenum-dependent nitrogenase (Mo-nitrogenase), a vanadium dependent nitrogenase (V-nitrogenase), and an iron-only nitrogenase (Fe-nitrogenase). These nitrogenase systems consist of component 1 (MoFe protein, VFe protein or, FeFe protein respectively) and, component 2 (Fe protein). This group contains the alpha subunit of component 1 of all three different forms. The most widespread and best characterized of these systems is the Mo-nitrogenase. MoFe is an alpha2beta2 tetramer, the alternative nitrogenases are alpha2beta2delta2 hexamers having alpha and beta subunits similar to the alpha and beta subunits of MoFe. The role of the delta subunit is unknown. For MoFe, each alphabeta pair of subunits contains one P-cluster (located at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein is a homodimer which contains, a single [4Fe-4S] cluster from which electrons are transferred to the P-cluster of the MoFe and in turn, to FeMoCo the site of substrate reduction. The V-nitrogenase requires an iron-vanadium cofactor (FeVco), the iron only-nitrogenase an iron only cofactor (FeFeco). These cofactors are analogous to the FeMoco. The V-nitrogenase has P clusters identical to those of MoFe. In addition to N2, nitrogenase also catalyzes the reduction of a variety of other substrates such as acetylene The V-nitrogenase differs from the Mo- nitrogenase in that it produces free hydrazine, as a minor product during dinitrogen reduction and, ethane as a minor product during acetylene reduction.


Pssm-ID: 238929 [Multi-domain]  Cd Length: 406  Bit Score: 203.22  E-value: 5.77e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37956444   4 TFFGPTKIEESLRAIGERFDDtiKANVEKVIAKYEPVMQAVLDEYKPRLEGKTAMLFVGGLRPRHTVGAYEDLGIQITGS 83
Cdd:cd01967 238 NFYGFEDTSESLRKIAKFFGD--EEKAEEVIAEEEARIKPELEKYRERLKGKKVIIYTGGARSWHVIAALRELGMEVVAA 315

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37956444  84 GYEFAHQDDYDRTAPEMAKGTIIYDDVSEFELEKFVEEFKPDLVGSGIKEKYVFQKSGIPFRQMHSWD 151
Cdd:cd01967 316 GYEFGHDDDYERIRKILDEGTLLVDDYNDLELEELVEKLKPDLILSGIKEKYVAQKLGIPFLDLHSER 383
N2-ase-Ialpha TIGR01862
nitrogenase component I, alpha chain; This model represents the alpha chain of all three ...
 5-151 9.72e-59

nitrogenase component I, alpha chain; This model represents the alpha chain of all three varieties (Mo-Fe, V-Fe, and Fe-Fe) of component I of nitrogenase. [Central intermediary metabolism, Nitrogen fixation]


Pssm-ID: 273838  Cd Length: 443  Bit Score: 188.04  E-value: 9.72e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37956444     5 FFGPTKIEESLRAIGERFDDTIKAnvEKVIAKYEPVMQAVLDEYKPRLEGKTAMLFVGGLRPRHTVG-AYEDLGIQITGS 83
Cdd:TIGR01862 270 FFGFTYTAESLRAIAAFFGIEKRA--EEVIAEEKAKWKPELDYYKERLQGKRVCLYIGGSRLWHWIGsAEEDLGMEVVAV 347

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37956444    84 GYEFAHQDDYDRTAPEMAKGTIIYDDVSEFELEKFVEEFKPDLVGSGIKEKYVFQKSGIPFRQMHSWD 151
Cdd:TIGR01862 348 GYEFAHEDDYEKTMKRMGEGTLLIDDPNELEFEEILEKLKPDIIFSGIKEKFVAQKLGVPYRQMHSYD 415
NifD/CfbD COG2710
Nitrogenase Mo-Fe protein NifD/coenzyme F430 biosynthesis subunit CfbD [Coenzyme transport and ...
 5-151 2.31e-41

Nitrogenase Mo-Fe protein NifD/coenzyme F430 biosynthesis subunit CfbD [Coenzyme transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 442027 [Multi-domain]  Cd Length: 416  Bit Score: 142.18  E-value: 2.31e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37956444   5 FFGPTKIEESLRAIGERFDDTIkanvEKVIAKYEPVMQAVLDEYKPRLEGKTAMLFVGGLRPRHTVGAYEDLGIQITGSG 84
Cdd:COG2710 238 PIGLEATDEFLRKLAELFGKPV----PEVIARERGRLVDALADYHFYLGGKKVAIYGDPDLLWGLASFLLELGMEPVAAV 313

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37956444  85 YEFAHQDDYDRTAPEMAKGTI--IYDDVSEFELEKFVEEFKPDLVGSGIKEKYVFQKSGIPFRQMHSWD 151
Cdd:COG2710 314 TTTGSPEDYERIKELLEELPEgtVIDDGDLEELEELLKELKPDLLIGGSKGKYLARKLGIPLLRVGFPI 382
Oxidoreductase_nitrogenase cd00316
The nitrogenase enzyme system catalyzes the ATP-dependent reduction of dinitrogen to ammonia. ...
 4-151 3.12e-40

The nitrogenase enzyme system catalyzes the ATP-dependent reduction of dinitrogen to ammonia. This group contains both alpha and beta subunits of component 1 of the three known genetically distinct types of nitrogenase systems: a molybdenum-dependent nitrogenase (Mo-nitrogenase), a vanadium-dependent nitrogenase (V-nitrogenase), and an iron-only nitrogenase (Fe-nitrogenase) and, both subunits of Protochlorophyllide (Pchlide) reductase and chlorophyllide (chlide) reductase. The nitrogenase systems consist of component 1 (MoFe protein, VFe protein or, FeFe protein respectively) and, component 2 (Fe protein). The most widespread and best characterized nitrogenase is the Mo-nitrogenase. MoFe is an alpha2beta2 tetramer, the alternative nitrogenases are alpha2beta2delta2 hexamers whose alpha and beta subunits are similar to the alpha and beta subunits of MoFe. For MoFe, each alphabeta pair contains one P-cluster (at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein contains a single [4Fe-4S] cluster from which, electrons are transferred to the P-cluster of the MoFe and in turn, to FeMoCo at the site of substrate reduction. The V-nitrogenase requires an iron-vanadium cofactor (FeVco), the iron only-nitrogenase an iron only cofactor (FeFeco). These cofactors are analogous to the FeMoco. The V-nitrogenase has P clusters identical to those of MoFe. Pchlide reductase and chlide reductase participate in the Mg-branch of the tetrapyrrole biosynthetic pathway. Pchlide reductase catalyzes the reduction of the D-ring of Pchlide during the synthesis of chlorophylls (Chl) and bacteriochlorophylls (BChl). Chlide-a reductase catalyzes the reduction of the B-ring of Chlide-a during the synthesis of BChl-a. The Pchlide reductase NB complex is a an N2B2 heterotetramer resembling nitrogenase FeMo, N and B proteins are homologous to the FeMo alpha and beta subunits respectively. The NB complex may serve as a catalytic site for Pchlide reduction and, the ZY complex as a site of chlide reduction, similar to MoFe for nitrogen reduction.


Pssm-ID: 238193 [Multi-domain]  Cd Length: 399  Bit Score: 138.95  E-value: 3.12e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37956444   4 TFFGPTKIEESLRAIGERFDdtIKANVEKVIAKYEPVMQAVLDEYKPRLEGKTAMLFVGGLRPRHTVGAYEDLGIQITGS 83
Cdd:cd00316 231 NPIGLEATDAFLRKLAELFG--IEKEVPEVIARERARLLDALADYHEYLGGKKVAIFGDGDLLLALARFLLELGMEVVAA 308

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37956444  84 GYEFAHQDDYDRTAPEMAKGTIIYDDVSEFELEKFVEEFKPDLVGSGIKEKYVFQKSGIPFRQMHSWD 151
Cdd:cd00316 309 GTTFGHKADYERREELLGEGTEVVDDGDLEELEELIRELKPDLIIGGSKGRYIAKKLGIPLVRIGFPI 376
Nitrogenase_NifE_I cd01968
Nitrogenase_NifE_I: a subgroup of the NifE subunit of the NifEN complex: NifE forms an ...
 5-144 1.26e-30

Nitrogenase_NifE_I: a subgroup of the NifE subunit of the NifEN complex: NifE forms an alpha2beta2 tetramer with NifN. NifE and NifN are structurally homologous to nitrogenase MoFe protein alpha and beta subunits respectively. NifEN participates in the synthesis of the iron-molybdenum cofactor (FeMoco) of the MoFe protein. NifB-co (an iron and sulfur containing precursor of the FeMoco) from NifB is transferred to the NifEN complex where it is further processed to FeMoco. The NifEN bound precursor of FeMoco has been identified as a molybdenum-free, iron- and sulfur- containing analog of FeMoco. It has been suggested that this NifEN bound precursor also acts as a cofactor precursor in nitrogenase systems which require a cofactor other than FeMoco: i.e. iron-vanadium cofactor (FeVco) or iron only cofactor (FeFeco).


Pssm-ID: 238930 [Multi-domain]  Cd Length: 410  Bit Score: 113.57  E-value: 1.26e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37956444   5 FFGPTKIEESLRAIGERFDDT-IKANVEKVIAKYEPVMQAVLDEYKPRLEGKTAMLFVGGLRPRHTVGAYEDLGIQITGS 83
Cdd:cd01968 237 FYGIRDTSKSLRNIAELLGDEeLIERTEELIAREEARLRPELAPYRARLEGKKAALYTGGVKSWSLVSALQDLGMEVVAT 316

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37956444  84 GYEFAHQDDYDRTAPEMAKGTIIYDDVSEFELEKFVEEFKPDLVGSGIKEKYVFQKSGIPF 144
Cdd:cd01968 317 GTQKGTKEDYERIKELLGEGTVIVDDANPRELKKLLKEKKADLLVAGGKERYLALKLGIPF 377
nifE TIGR01283
nitrogenase molybdenum-iron cofactor biosynthesis protein NifE; This protein is part of the ...
 2-144 2.37e-30

nitrogenase molybdenum-iron cofactor biosynthesis protein NifE; This protein is part of the NifEN complex involved in biosynthesis of the molybdenum-iron cofactor used by the homologous NifDK complex of nitrogenase. In a few species, the protein is found as a NifEN fusion protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Central intermediary metabolism, Nitrogen fixation]


Pssm-ID: 188126 [Multi-domain]  Cd Length: 453  Bit Score: 113.61  E-value: 2.37e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37956444     2 NSTFFGPTKIEESLRAIGERF-DDTIKANVEKVIAKYEPVMQAVLDEYKPRLEGKTAMLFVGGLRPRHTVGAYEDLGIQI 80
Cdd:TIGR01283 270 EGSFYGIEDTSKALRDIADLFgDPELLKRTEELIAREEAKIRPALEPYRERLKGKKAAIYTGGVKSWSVVSALQDLGMEV 349

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37956444    81 TGSGYEFAHQDDYDRTAPEMAKGTIIYDDVSEFELEKFVEEFKPDLVGSGIKEKYVFQKSGIPF 144
Cdd:TIGR01283 350 VATGTQKSTEEDYARIRELMGEGTVMLDDANPRELLKLLLEYKADILIAGGRERYTALKLGIPF 413
Oxidored_nitro pfam00148
Nitrogenase component 1 type Oxidoreductase;
3-144 4.98e-29

Nitrogenase component 1 type Oxidoreductase;


Pssm-ID: 395096 [Multi-domain]  Cd Length: 398  Bit Score: 109.26  E-value: 4.98e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37956444     3 STFFGPTKIEESLRAIGERFDdtiKANVEKVIAKYEPVMQAVLDEYKPRLEGKTAMLFVGGLRPRHTVGAYEDLGIQITG 82
Cdd:pfam00148 223 GAPIGLEATDRFLRALAKLFG---KEVAPEVIARERGRLLDAMVDYHEYLAGKRVAIYGDPDLVLGLARFLLELGMEPVA 299

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37956444    83 SGYEFAHQDDYDRTAPEMAKGT-IIYDDVSEFELEKFVEEFKPDLVGSGIKEKYVFQKSGIPF 144
Cdd:pfam00148 300 VGTGTGHPDDYERLKAELEEGDpEVIDGADLEELEELIKELKPDLLLGNSKGRYIARKLGIPL 362
Nitrogenase_VFe_alpha cd01977
Nitrogenase_VFe_alpha -like: Nitrogenase VFe protein, alpha subunit like. This group contains ...
 5-150 6.06e-27

Nitrogenase_VFe_alpha -like: Nitrogenase VFe protein, alpha subunit like. This group contains proteins similar to the alpha subunits of, the VFe protein of the vanadium-dependent (V-) nitrogenase and the FeFe protein of the iron only (Fe-) nitrogenase Nitrogenase catalyzes the ATP-dependent reduction of dinitrogen (N2) to ammonia. In addition to V- and Fe- nitrogenases there is a molybdenum (Mo)-dependent nitrogenase which is the most widespread and best characterized of these systems. These systems consist of component 1 (VFe protein, FeFe protein or, MoFe protein respectively) and, component 2 (Fe protein). MoFe is an alpha2beta2 tetramer, V-and Fe- nitrogenases are alpha2beta2delta2 hexamers. The alpha and beta subunits of VFe and FeFe are similar to the alpha and beta subunits of MoFe. For MoFe each alphabeta pair contains one P-cluster (at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein which has a practically identical structure in all three systems, it contains a single [4Fe-4S] cluster. Electrons are transferred from the [4Fe-4S] cluster of the Fe protein to the P-cluster of the MoFe and in turn to FeMoCo, the site of substrate reduction. The V-nitrogenase requires an iron-vanadium cofactor (FeVco), the iron only-nitrogenase an iron only cofactor (FeFeco). These cofactors are analogous to the FeMoco. The V-nitrogenase has P clusters identical to those of MoFe. In addition to N2, nitrogenase also catalyzes the reduction of a variety of other substrates such as acetylene The V-nitrogenase differs from the Mo-nitrogenase in that it produces free hydrazine, as a minor product during dinitrogen reduction and, ethane as a minor product during acetylene reduction.


Pssm-ID: 238936 [Multi-domain]  Cd Length: 415  Bit Score: 103.67  E-value: 6.06e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37956444   5 FFGPTKIEESLRAIGERF--DDTIKANVEKVIAKYEPVmqavLDEYKPRLEGKTAMLFVGGLRPRHTVGAYED-LGIQIT 81
Cdd:cd01977 241 GFGFEYCAESLRKIGAFFgiEDRAEAVIAEEMAKWKPE----LDWYKERLKGKKVCIWTGGPKLWHWTKVIEDeLGMQVV 316

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37956444  82 GSGYEFAHQDDYDRTAPEMAKGTIIYDDVSEFELEKFVEEFKPDLVGSGIKEKYVFQKSGIPFRQMHSW 150
Cdd:cd01977 317 AMSSKFGHQEDFEKVIARGGEGTIYIDDPNELEFFEILEMLKPDIILTGPRVGELVKKLHVPYVNIHAY 385
PRK14477 PRK14477
bifunctional nitrogenase molybdenum-cofactor biosynthesis protein NifE/NifN; Provisional
 4-144 2.83e-22

bifunctional nitrogenase molybdenum-cofactor biosynthesis protein NifE/NifN; Provisional


Pssm-ID: 172952 [Multi-domain]  Cd Length: 917  Bit Score: 91.73  E-value: 2.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37956444    4 TFFGPTKIEESLRAIGERFDD--------TIKANVEKVIAKYEPVMQAVLDEYKPRLEGKTAMLFVGGLRPRHTVGAYED 75
Cdd:PRK14477 262 SFYGMTDTAKALRDIARELDDaggglekrVLQDRVEKLIAEEEAKCRAALAPYRARLEGKRVVLFTGGVKTWSMVNALRE 341

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37956444   76 LGIQITGSGYEFAHQDDYDRTAPEMAKGTIIYDDVSEFELEKFVEEFKPDLVGSGIKEKYVFQKSGIPF 144
Cdd:PRK14477 342 LGVEVLAAGTQNSTLEDFARMKALMHKDAHIIEDTSTAGLLRVMREKMPDLIVAGGKTKFLALKTRTPF 410
 
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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