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Conserved domains on  [gi|1039027902|gb|ANM72615|]
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nitrogenase protein alpha chain, partial [Bradyrhizobium sp. CPI234]

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. ...
 1-172 2.86e-125

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: 360.14  E-value: 2.86e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902   1 EATPKAKLNILHCYRSMNYISRHMEEKFGIPWCEYNFFGPSKIAESLRKIAGYFDDRIKEGAERVIAKYQPLVDAVVAKY 80
Cdd:TIGR01282 250 ENAPKAKLNLIHCYRSMNYISRHMEEKYGIPWMEYNFFGPTKIAESLRKIAEFFDDEIKEKAEEVIAKYQPAVDAVIAKY 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902  81 RPRLEGKTVMLFVGGLRPRHVIGAYEDLGMEVIGTGYEFGHNDDYQRTaQHYVKDGTLIYDDVNGYEFERFVEKMQPDLV 160
Cdd:TIGR01282 330 RPRLEGKTVMLYVGGLRPRHVIGAFEDLGMEVIGTGYEFAHNDDYERT-TKYMKDGTLIYDDVTHYEFEEFVEKLKPDLV 408

                         170
                  ....*....|..
gi 1039027902 161 GSGIKEKYVFQK 172
Cdd:TIGR01282 409 GSGIKEKYVFQK 420
 
Name Accession Description Interval E-value
nifD TIGR01282
nitrogenase molybdenum-iron protein alpha chain; Nitrogenase consists of alpha (NifD) and beta ...
 1-172 2.86e-125

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: 360.14  E-value: 2.86e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902   1 EATPKAKLNILHCYRSMNYISRHMEEKFGIPWCEYNFFGPSKIAESLRKIAGYFDDRIKEGAERVIAKYQPLVDAVVAKY 80
Cdd:TIGR01282 250 ENAPKAKLNLIHCYRSMNYISRHMEEKYGIPWMEYNFFGPTKIAESLRKIAEFFDDEIKEKAEEVIAKYQPAVDAVIAKY 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902  81 RPRLEGKTVMLFVGGLRPRHVIGAYEDLGMEVIGTGYEFGHNDDYQRTaQHYVKDGTLIYDDVNGYEFERFVEKMQPDLV 160
Cdd:TIGR01282 330 RPRLEGKTVMLYVGGLRPRHVIGAFEDLGMEVIGTGYEFAHNDDYERT-TKYMKDGTLIYDDVTHYEFEEFVEKLKPDLV 408

                         170
                  ....*....|..
gi 1039027902 161 GSGIKEKYVFQK 172
Cdd:TIGR01282 409 GSGIKEKYVFQK 420
Nitrogenase_MoFe_alpha cd01976
Nitrogenase_MoFe_alpha_II: Nitrogenase MoFe protein, beta subunit. A group of proteins similar ...
 1-172 1.02e-116

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: 336.61  E-value: 1.02e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902   1 EATPKAKLNILHCYRSMNYISRHMEEKFGIPWCEYNFFGPSKIAESLRKIAGYFDDRIKEGAERVIAKYQPLVDAVVAKY 80
Cdd:cd01976   215 ENAHKAKLNLIHCYRSMNYIARMMEEKYGIPWMEYNFFGPTKIAESLRKIAAYFDDEITAKTEEVIAEYKPAMEAVIAKY 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902  81 RPRLEGKTVMLFVGGLRPRHVIGAYEDLGMEVIGTGYEFGHNDDYQRTaQHYVKDGTLIYDDVNGYEFERFVEKMQPDLV 160
Cdd:cd01976   295 RPRLEGKTVMLYVGGLRPRHYIGAYEDLGMEVVGTGYEFAHRDDYERT-EVIPKEGTLLYDDVTHYELEEFVKRLKPDLI 373

                         170
                  ....*....|..
gi 1039027902 161 GSGIKEKYVFQK 172
Cdd:cd01976   374 GSGIKEKYVFQK 385
NifD/CfbD COG2710
Nitrogenase Mo-Fe protein NifD/coenzyme F430 biosynthesis subunit CfbD [Coenzyme transport and ...
 1-172 8.42e-53

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: 172.99  E-value: 8.42e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902   1 EATPKAKLNILHCYRSMNYISRHMEEKFGIPWCE-YNFFGPSKIAESLRKIAGYFDDRIkegaERVIAKYQPLVDAVVAK 79
Cdd:COG2710   201 ADAGRAKLNLVLCSRSGNYAARYLEEKYGIPYLEfVSPIGLEATDEFLRKLAELFGKPV----PEVIARERGRLVDALAD 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902  80 YRPRLEGKTVMLFVGGLRPRHVIGAYEDLGMEVIGTGYEFGHNDDYQRTAQHY--VKDGTlIYDDVNGYEFERFVEKMQP 157
Cdd:COG2710   277 YHFYLGGKKVAIYGDPDLLWGLASFLLELGMEPVAAVTTTGSPEDYERIKELLeeLPEGT-VIDDGDLEELEELLKELKP 355

                         170
                  ....*....|....*
gi 1039027902 158 DLVGSGIKEKYVFQK 172
Cdd:COG2710   356 DLLIGGSKGKYLARK 370
Oxidored_nitro pfam00148
Nitrogenase component 1 type Oxidoreductase;
1-172 9.26e-40

Nitrogenase component 1 type Oxidoreductase;


Pssm-ID: 395096 [Multi-domain]  Cd Length: 398  Bit Score: 138.53  E-value: 9.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902   1 EATPKAKLNILHCYRSMNYISRHMEEKFGIPWCEY-NFFGPSKIAESLRKIAGYFDdrIKEGAERVIAKYQPLVDAVVAk 79
Cdd:pfam00148 188 RAAGNAAANLVLCPFSGEYAAEMLEEKFGVPYIRLgAPIGLEATDRFLRALAKLFG--KEVAPEVIARERGRLLDAMVD- 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902  80 YRPRLEGKTVMLFVGGLRPRHVIGAYEDLGMEVIGTGYEFGHNDDYQRTAQHYVKDGTLIYDDVNGYEFERFVEKMQPDL 159
Cdd:pfam00148 265 YHEYLAGKRVAIYGDPDLVLGLARFLLELGMEPVAVGTGTGHPDDYERLKAELEEGDPEVIDGADLEELEELIKELKPDL 344

                         170
                  ....*....|...
gi 1039027902 160 VGSGIKEKYVFQK 172
Cdd:pfam00148 345 LLGNSKGRYIARK 357
PRK14477 PRK14477
bifunctional nitrogenase molybdenum-cofactor biosynthesis protein NifE/NifN; Provisional
 5-169 2.81e-32

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


Pssm-ID: 172952 [Multi-domain]  Cd Length: 917  Bit Score: 121.39  E-value: 2.81e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902   5 KAKLNILHCYRSMNYISRHMEEKFGIPWCEYNFFGPSKIAESLRKIAGYFDDR--------IKEGAERVIAKYQPLVDAV 76
Cdd:PRK14477  231 RAKLNVIICSKSLTNLARKMEKRYGIPYLEESFYGMTDTAKALRDIARELDDAggglekrvLQDRVEKLIAEEEAKCRAA 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902  77 VAKYRPRLEGKTVMLFVGGLRPRHVIGAYEDLGMEVIGTGYEFGHNDDYQRTAQHYVKDGTlIYDDVNGYEFERFVEKMQ 156
Cdd:PRK14477  311 LAPYRARLEGKRVVLFTGGVKTWSMVNALRELGVEVLAAGTQNSTLEDFARMKALMHKDAH-IIEDTSTAGLLRVMREKM 389

                         170
                  ....*....|...
gi 1039027902 157 PDLVGSGIKEKYV 169
Cdd:PRK14477  390 PDLIVAGGKTKFL 402
 
Name Accession Description Interval E-value
nifD TIGR01282
nitrogenase molybdenum-iron protein alpha chain; Nitrogenase consists of alpha (NifD) and beta ...
 1-172 2.86e-125

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: 360.14  E-value: 2.86e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902   1 EATPKAKLNILHCYRSMNYISRHMEEKFGIPWCEYNFFGPSKIAESLRKIAGYFDDRIKEGAERVIAKYQPLVDAVVAKY 80
Cdd:TIGR01282 250 ENAPKAKLNLIHCYRSMNYISRHMEEKYGIPWMEYNFFGPTKIAESLRKIAEFFDDEIKEKAEEVIAKYQPAVDAVIAKY 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902  81 RPRLEGKTVMLFVGGLRPRHVIGAYEDLGMEVIGTGYEFGHNDDYQRTaQHYVKDGTLIYDDVNGYEFERFVEKMQPDLV 160
Cdd:TIGR01282 330 RPRLEGKTVMLYVGGLRPRHVIGAFEDLGMEVIGTGYEFAHNDDYERT-TKYMKDGTLIYDDVTHYEFEEFVEKLKPDLV 408

                         170
                  ....*....|..
gi 1039027902 161 GSGIKEKYVFQK 172
Cdd:TIGR01282 409 GSGIKEKYVFQK 420
Nitrogenase_MoFe_alpha cd01976
Nitrogenase_MoFe_alpha_II: Nitrogenase MoFe protein, beta subunit. A group of proteins similar ...
 1-172 1.02e-116

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: 336.61  E-value: 1.02e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902   1 EATPKAKLNILHCYRSMNYISRHMEEKFGIPWCEYNFFGPSKIAESLRKIAGYFDDRIKEGAERVIAKYQPLVDAVVAKY 80
Cdd:cd01976   215 ENAHKAKLNLIHCYRSMNYIARMMEEKYGIPWMEYNFFGPTKIAESLRKIAAYFDDEITAKTEEVIAEYKPAMEAVIAKY 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902  81 RPRLEGKTVMLFVGGLRPRHVIGAYEDLGMEVIGTGYEFGHNDDYQRTaQHYVKDGTLIYDDVNGYEFERFVEKMQPDLV 160
Cdd:cd01976   295 RPRLEGKTVMLYVGGLRPRHYIGAYEDLGMEVVGTGYEFAHRDDYERT-EVIPKEGTLLYDDVTHYELEEFVKRLKPDLI 373

                         170
                  ....*....|..
gi 1039027902 161 GSGIKEKYVFQK 172
Cdd:cd01976   374 GSGIKEKYVFQK 385
Nitrogenase_MoFe_alpha_like cd01967
Nitrogenase_MoFe_alpha_like: Nitrogenase MoFe protein, alpha subunit_like. The nitrogenase ...
 1-172 8.29e-81

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: 244.82  E-value: 8.29e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902   1 EATPKAKLNILHCYRSMNYISRHMEEKFGIPWCEYNFFGPSKIAESLRKIAGYFDDRIKegAERVIAKYQPLVDAVVAKY 80
Cdd:cd01967   203 RRAHRAKLNLVHCSRSMNYLAREMEERYGIPYMEVNFYGFEDTSESLRKIAKFFGDEEK--AEEVIAEEEARIKPELEKY 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902  81 RPRLEGKTVMLFVGGLRPRHVIGAYEDLGMEVIGTGYEFGHNDDYQRTaQHYVKDGTLIYDDVNGYEFERFVEKMQPDLV 160
Cdd:cd01967   281 RERLKGKKVIIYTGGARSWHVIAALRELGMEVVAAGYEFGHDDDYERI-RKILDEGTLLVDDYNDLELEELVEKLKPDLI 359

                         170
                  ....*....|..
gi 1039027902 161 GSGIKEKYVFQK 172
Cdd:cd01967   360 LSGIKEKYVAQK 371
N2-ase-Ialpha TIGR01862
nitrogenase component I, alpha chain; This model represents the alpha chain of all three ...
 1-172 1.56e-78

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: 240.04  E-value: 1.56e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902   1 EATPKAKLNILHCYRSMNYISRHMEEKFGIPWCEYNFFGPSKIAESLRKIAGYFDdrIKEGAERVIAKYQPLVDAVVAKY 80
Cdd:TIGR01862 234 RLMHKAKLNLVHCARSANYIANELEERYGIPWMKIDFFGFTYTAESLRAIAAFFG--IEKRAEEVIAEEKAKWKPELDYY 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902  81 RPRLEGKTVMLFVGGLRPRHVIG-AYEDLGMEVIGTGYEFGHNDDYQRTAQHyVKDGTLIYDDVNGYEFERFVEKMQPDL 159
Cdd:TIGR01862 312 KERLQGKRVCLYIGGSRLWHWIGsAEEDLGMEVVAVGYEFAHEDDYEKTMKR-MGEGTLLIDDPNELEFEEILEKLKPDI 390

                         170
                  ....*....|...
gi 1039027902 160 VGSGIKEKYVFQK 172
Cdd:TIGR01862 391 IFSGIKEKFVAQK 403
NifD/CfbD COG2710
Nitrogenase Mo-Fe protein NifD/coenzyme F430 biosynthesis subunit CfbD [Coenzyme transport and ...
 1-172 8.42e-53

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: 172.99  E-value: 8.42e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902   1 EATPKAKLNILHCYRSMNYISRHMEEKFGIPWCE-YNFFGPSKIAESLRKIAGYFDDRIkegaERVIAKYQPLVDAVVAK 79
Cdd:COG2710   201 ADAGRAKLNLVLCSRSGNYAARYLEEKYGIPYLEfVSPIGLEATDEFLRKLAELFGKPV----PEVIARERGRLVDALAD 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902  80 YRPRLEGKTVMLFVGGLRPRHVIGAYEDLGMEVIGTGYEFGHNDDYQRTAQHY--VKDGTlIYDDVNGYEFERFVEKMQP 157
Cdd:COG2710   277 YHFYLGGKKVAIYGDPDLLWGLASFLLELGMEPVAAVTTTGSPEDYERIKELLeeLPEGT-VIDDGDLEELEELLKELKP 355

                         170
                  ....*....|....*
gi 1039027902 158 DLVGSGIKEKYVFQK 172
Cdd:COG2710   356 DLLIGGSKGKYLARK 370
Oxidoreductase_nitrogenase cd00316
The nitrogenase enzyme system catalyzes the ATP-dependent reduction of dinitrogen to ammonia. ...
 1-172 1.11e-49

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: 164.37  E-value: 1.11e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902   1 EATPKAKLNILHCYRSMNYISRHMEEKFGIPWCEYNFFGPSKIAESLRKIAGYFDDRIKegAERVIAKYQPLVDAVVAKY 80
Cdd:cd00316   196 RELGNAKLNLVLCRESGLYLARYLEEKYGIPYILINPIGLEATDAFLRKLAELFGIEKE--VPEVIARERARLLDALADY 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902  81 RPRLEGKTVMLFVGGLRPRHVIGAYEDLGMEVIGTGYEFGHNDDYQRTAQhYVKDGTLIYDDVNGYEFERFVEKMQPDLV 160
Cdd:cd00316   274 HEYLGGKKVAIFGDGDLLLALARFLLELGMEVVAAGTTFGHKADYERREE-LLGEGTEVVDDGDLEELEELIRELKPDLI 352

                         170
                  ....*....|..
gi 1039027902 161 GSGIKEKYVFQK 172
Cdd:cd00316   353 IGGSKGRYIAKK 364
nifE TIGR01283
nitrogenase molybdenum-iron cofactor biosynthesis protein NifE; This protein is part of the ...
 4-169 3.15e-49

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: 164.45  E-value: 3.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902   4 PKAKLNILHCYRSMNYISRHMEEKFGIPWCEYNFFGPSKIAESLRKIAGYF-DDRIKEGAERVIAKYQPLVDAVVAKYRP 82
Cdd:TIGR01283 240 HRAKLNMVQCSKAMINLARKMEEKYGIPYFEGSFYGIEDTSKALRDIADLFgDPELLKRTEELIAREEAKIRPALEPYRE 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902  83 RLEGKTVMLFVGGLRPRHVIGAYEDLGMEVIGTGYEFGHNDDYQRTAQHyVKDGTLIYDDVNGYEFERFVEKMQPDLVGS 162
Cdd:TIGR01283 320 RLKGKKAAIYTGGVKSWSVVSALQDLGMEVVATGTQKSTEEDYARIREL-MGEGTVMLDDANPRELLKLLLEYKADILIA 398


                  ....*..
gi 1039027902 163 GIKEKYV 169
Cdd:TIGR01283 399 GGRERYT 405
Nitrogenase_NifE_I cd01968
Nitrogenase_NifE_I: a subgroup of the NifE subunit of the NifEN complex: NifE forms an ...
 4-169 3.93e-46

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: 155.56  E-value: 3.93e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902   4 PKAKLNILHCYRSMNYISRHMEEKFGIPWCEYNFFGPSKIAESLRKIAGYFDDR-IKEGAERVIAKYQPLVDAVVAKYRP 82
Cdd:cd01968   204 HRAKLNVVQCSKSMIYLARKMEEKYGIPYIEVSFYGIRDTSKSLRNIAELLGDEeLIERTEELIAREEARLRPELAPYRA 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902  83 RLEGKTVMLFVGGLRPRHVIGAYEDLGMEVIGTGYEFGHNDDYQRTAQHyVKDGTLIYDDVNGYEFERFVEKMQPDLVGS 162
Cdd:cd01968   284 RLEGKKAALYTGGVKSWSLVSALQDLGMEVVATGTQKGTKEDYERIKEL-LGEGTVIVDDANPRELKKLLKEKKADLLVA 362


                  ....*..
gi 1039027902 163 GIKEKYV 169
Cdd:cd01968   363 GGKERYL 369
Oxidored_nitro pfam00148
Nitrogenase component 1 type Oxidoreductase;
1-172 9.26e-40

Nitrogenase component 1 type Oxidoreductase;


Pssm-ID: 395096 [Multi-domain]  Cd Length: 398  Bit Score: 138.53  E-value: 9.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902   1 EATPKAKLNILHCYRSMNYISRHMEEKFGIPWCEY-NFFGPSKIAESLRKIAGYFDdrIKEGAERVIAKYQPLVDAVVAk 79
Cdd:pfam00148 188 RAAGNAAANLVLCPFSGEYAAEMLEEKFGVPYIRLgAPIGLEATDRFLRALAKLFG--KEVAPEVIARERGRLLDAMVD- 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902  80 YRPRLEGKTVMLFVGGLRPRHVIGAYEDLGMEVIGTGYEFGHNDDYQRTAQHYVKDGTLIYDDVNGYEFERFVEKMQPDL 159
Cdd:pfam00148 265 YHEYLAGKRVAIYGDPDLVLGLARFLLELGMEPVAVGTGTGHPDDYERLKAELEEGDPEVIDGADLEELEELIKELKPDL 344

                         170
                  ....*....|...
gi 1039027902 160 VGSGIKEKYVFQK 172
Cdd:pfam00148 345 LLGNSKGRYIARK 357
Nitrogenase_VFe_alpha cd01977
Nitrogenase_VFe_alpha -like: Nitrogenase VFe protein, alpha subunit like. This group contains ...
 5-172 1.57e-38

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: 135.65  E-value: 1.57e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902   5 KAKLNILHCYRSMNYISRHMEEKFGIPWCEYNFFGPSKIAESLRKIAGYFDdrIKEGAERVI----AKYQPLVDAvvakY 80
Cdd:cd01977   209 RAKLNVVNCARSAGYIANELKKRYGIPRLDVDGFGFEYCAESLRKIGAFFG--IEDRAEAVIaeemAKWKPELDW----Y 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902  81 RPRLEGKTVMLFVGGLRPRHVIGAYED-LGMEVIGTGYEFGHNDDYQRtAQHYVKDGTLIYDDVNGYEFERFVEKMQPDL 159
Cdd:cd01977   283 KERLKGKKVCIWTGGPKLWHWTKVIEDeLGMQVVAMSSKFGHQEDFEK-VIARGGEGTIYIDDPNELEFFEILEMLKPDI 361

                         170
                  ....*....|...
gi 1039027902 160 VGSGIKEKYVFQK 172
Cdd:cd01977   362 ILTGPRVGELVKK 374
PRK14477 PRK14477
bifunctional nitrogenase molybdenum-cofactor biosynthesis protein NifE/NifN; Provisional
 5-169 2.81e-32

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


Pssm-ID: 172952 [Multi-domain]  Cd Length: 917  Bit Score: 121.39  E-value: 2.81e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902   5 KAKLNILHCYRSMNYISRHMEEKFGIPWCEYNFFGPSKIAESLRKIAGYFDDR--------IKEGAERVIAKYQPLVDAV 76
Cdd:PRK14477  231 RAKLNVIICSKSLTNLARKMEKRYGIPYLEESFYGMTDTAKALRDIARELDDAggglekrvLQDRVEKLIAEEEAKCRAA 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902  77 VAKYRPRLEGKTVMLFVGGLRPRHVIGAYEDLGMEVIGTGYEFGHNDDYQRTAQHYVKDGTlIYDDVNGYEFERFVEKMQ 156
Cdd:PRK14477  311 LAPYRARLEGKRVVLFTGGVKTWSMVNALRELGVEVLAAGTQNSTLEDFARMKALMHKDAH-IIEDTSTAGLLRVMREKM 389

                         170
                  ....*....|...
gi 1039027902 157 PDLVGSGIKEKYV 169
Cdd:PRK14477  390 PDLIVAGGKTKFL 402
PRK02910 PRK02910
ferredoxin:protochlorophyllide reductase (ATP-dependent) subunit B;
4-160 1.38e-04

ferredoxin:protochlorophyllide reductase (ATP-dependent) subunit B;


Pssm-ID: 235085 [Multi-domain]  Cd Length: 519  Bit Score: 41.02  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902   4 PKAKLNILhCYRSMNYIS-RHMEEKFGIPWCEYNFFGPSKIAESLRKIAG-------YFDDRIKEGAERV--IAKYQPLV 73
Cdd:PRK02910  208 PAAWFNVV-LYREIGESAaRYLEREFGQPYVKTVPIGVGATARFIREVAEllnldgaDLEAFILDGLSAPsrLPWFSRSV 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902  74 DAVVakyrprLEGKTVMLFVGGlrpRHVIGA----YEDLGMEVIGTG-YEFGHNDDYQRTAQHYVkDGTLIYDDVNgyEF 148
Cdd:PRK02910  287 DSTY------LTGKRVFVFGDA---THAVAAarilSDELGFEVVGAGtYLREDARWVRAAAKEYG-DEALITDDYL--EV 354

                         170
                  ....*....|..
gi 1039027902 149 ERFVEKMQPDLV 160
Cdd:PRK02910  355 EDAIAEAAPELV 366
Nitrogenase_VnfE_like cd01972
Nitrogenase_VnfE_like: VnfE subunit of the VnfEN complex_like. This group in addition to VnfE ...
 4-160 3.79e-04

Nitrogenase_VnfE_like: VnfE subunit of the VnfEN complex_like. This group in addition to VnfE contains a subset of the alpha subunit of the nitrogenase MoFe protein and NifE-like proteins. The nitrogenase enzyme system catalyzes the ATP-dependent reduction of dinitrogen to ammonia. NifEN participates in the synthesis of the iron-molybdenum cofactor (FeMoco) of MoFe protein of the molybdenum(Mo)-nitrogenase. NifB-co (an iron and sulfur containing precursor of the FeMoco) from NifB is transferred to NifEN where it is further processed to FeMoco. VnfEN may similarly be a scaffolding protein for the iron-vanadium cofactor (FeVco) of the vanadium-dependent (V)-nitrogenase. NifE and NifN are essential for the Mo-nitrogenase, VnfE and VnfN are not essential for the V-nitrogenase. NifE and NifN can substitute when the vnfEN genes are inactivated.


Pssm-ID: 238932 [Multi-domain]  Cd Length: 426  Bit Score: 39.71  E-value: 3.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902   4 PKAKLNILHCYRSMNYISRHMEEKFGIPwceYNF----FGPSKIAESLRKIAGYFDdrIKEGAERVIAKYQPLVDAVVAK 79
Cdd:cd01972   212 SEAAANVTLCLDLGYYLGAALEQRFGVP---EIKapqpYGIEATDKWLREIAKVLG--MEAEAEAVIEREHERVAPEIEE 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902  80 YRPRLEGKTVMLfVGGLRPRHVIGAY--EDLGMEVIGTgYEFGHNDDYQR--TAQHYVKDGTLIYDDV------NG--YE 147
Cdd:cd01972   287 LRKALKGKKAIV-ETGAAYGHLLIAVlrELGFGEVPVV-LVFHHDPTYDRgdSEKDLLEHGVDPEIDItkytvsNGqyYQ 364

                         170
                  ....*....|...
gi 1039027902 148 FERFVEKMQPDLV 160
Cdd:cd01972   365 FYNLLKRVKPDFI 377
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 26-113 1.16e-03

ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 38.06  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902  26 EKFGIPWCEYNFFGPSKIAESLRKIAGYFDDriKEGAERVIAKYQPLVDAVVAKYRPRLEGKTVMLFVGGLRPRHVIGA- 104
Cdd:COG0614    80 EKIGIPVVVLDPRSLEDLYESIRLLGELLGR--EERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPLYTAGGg 157

                          90
                  ....*....|....*
gi 1039027902 105 ------YEDLGMEVI 113
Cdd:COG0614   158 sfigelLELAGGRNV 172
Nitrogenase_VnfN_like cd01971
Nitrogenase_vnfN_like: VnfN subunit of the VnfEN complex-like. This group in addition to VnfN ...
 2-83 5.94e-03

Nitrogenase_vnfN_like: VnfN subunit of the VnfEN complex-like. This group in addition to VnfN contains a subset of the beta subunit of the nitrogenase MoFe protein and NifN-like proteins. The nitrogenase enzyme system catalyzes the ATP-dependent reduction of dinitrogen to ammonia. NifEN participates in the synthesis of the iron-molybdenum cofactor (FeMoco) of MoFe protein of the molybdenum(Mo)-nitrogenase. NifB-co (an iron and sulfur containing precursor of the FeMoco) from NifB is transferred to NifEN where it is further processed to FeMoco. VnfEN may similarly be a scaffolding protien for the iron-vanadium cofactor (FeVco) of the vanadium-dependent (V)-nitrogenase. NifE and NifN are essential for the Mo-nitrogenase, VnfE and VnfN are not essential for the V-nitrogenase. NifE and NifN can substitute when the vnfEN genes are inactivated.


Pssm-ID: 238931 [Multi-domain]  Cd Length: 427  Bit Score: 36.24  E-value: 5.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039027902   2 ATPKAKLNILHCYRSMNYISRHMEEKFGIPWCEYNFF--GPSKIAESLRKIAGYF-------DDRIKEGAERVIAKYQPL 72
Cdd:cd01971   204 SIPKAQFNLVLSPWVGLEFAQHLEEKYGQPYIHSPTLpiGAKATAEFLRQVAKFAgiekakvEAFIKAEEKRYYHYLERF 283

                          90
                  ....*....|.
gi 1039027902  73 VDAVVAKYRPR 83
Cdd:cd01971   284 SDFMARWGLPR 294
 
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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