|
Name |
Accession |
Description |
Interval |
E-value |
| nifD |
TIGR01282 |
nitrogenase molybdenum-iron protein alpha chain; Nitrogenase consists of alpha (NifD) and beta ... |
12-478 |
0e+00 |
|
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: 968.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 12 LIQEVLEVFPETARKERRKHMMVSDPEMESvGKCIISNRKSQPGVMTVRGCAYAGSKGVVFGPIKDMAHISHGPVGCGQY 91
Cdd:TIGR01282 1 LIDEVLEVYPEKAAKKRSKHLVVNEPEGKS-DCGVKSNIKSVPGVMTIRGCAYAGSKGVVWGPIKDMVHISHGPVGCGQY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 92 SRAGRRNYYTGVSGVDSFGTLNFTSDFQERDIVFGGDKKLSKLIEEMELLFPLTKGITIQSECPVGLIGDDISAVANASS 171
Cdd:TIGR01282 80 SWGGRRNYYKGETGVDNFGTMQFTSDFQEKDIVFGGDKKLKKAIDEIEELFPLNKGISIQSECPVGLIGDDIEAVAKKAS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 172 KALDKPVIPVRCEGFRGVSQSLGHHIANDVVRDWILNNREGQPFETTPYDVAIIGDYNIGGDAWASRILLEEMGLRVVAQ 251
Cdd:TIGR01282 160 KELGKPVVPVRCEGFRGVSQSLGHHIANDAVRDWVLGKGDKEKFEPTPYDVAIIGDYNIGGDAWESRILLEEIGLRVVAQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 252 WSGDGTLVEMENTPFVKLNLVHCYRSMNYIARHMEEKHQIPWMEYNFFGPTKIAESLRKIADQFDDTIRANAEAVIARYE 331
Cdd:TIGR01282 240 WSGDGTLNEMENAPKAKLNLIHCYRSMNYISRHMEEKYGIPWMEYNFFGPTKIAESLRKIAEFFDDEIKEKAEEVIAKYQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 332 GQMAAIIAKYRPRLEGRKVLLYMGGLRPRHVIGAYEDLGMEIIAAGYEFAHNDDYDRTLPDLKEGTLLFDDASSYELEAF 411
Cdd:TIGR01282 320 PAVDAVIAKYRPRLEGKTVMLYVGGLRPRHVIGAFEDLGMEVIGTGYEFAHNDDYERTTKYMKDGTLIYDDVTHYEFEEF 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575523319 412 VKALKPDLIGSGIKEKYIFQKMGVPFRQMHSWDYSGPYHGYDGFAIFARDMDMTLNNPAWNELTAPW 478
Cdd:TIGR01282 400 VEKLKPDLVGSGIKEKYVFQKMGVPFRQMHSWDYSGPYHGYDGFAIFARDMDMALNSPTWKLIKAPW 466
|
|
| Nitrogenase_MoFe_alpha |
cd01976 |
Nitrogenase_MoFe_alpha_II: Nitrogenase MoFe protein, beta subunit. A group of proteins similar ... |
46-468 |
0e+00 |
|
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: 876.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 46 IISNRKSQPGVMTVRGCAYAGSKGVVFGPIKDMAHISHGPVGCGQYSRAGRRNYYTGVSGVDSFGTLNFTSDFQERDIVF 125
Cdd:cd01976 1 IKSNIKSVPGVMTIRGCAYAGSKGVVWGPIKDMVHISHGPVGCGQYSWATRRNYYRGETGVDNFGTMQFTTDFQEKDIVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 126 GGDKKLSKLIEEMELLFPLTKGITIQSECPVGLIGDDISAVANASSKALDKPVIPVRCEGFRGVSQSLGHHIANDVVRDW 205
Cdd:cd01976 81 GGDKKLAKAIDEAYELFPLNKGISVQSECPVGLIGDDIEAVARKASKELGIPVVPVRCEGFRGVSQSLGHHIANDAIRDH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 206 ILNNREgqPFETTPYDVAIIGDYNIGGDAWASRILLEEMGLRVVAQWSGDGTLVEMENTPFVKLNLVHCYRSMNYIARHM 285
Cdd:cd01976 161 ILGKRN--EFEPTPYDVNIIGDYNIGGDAWASRILLEEMGLRVVAQWSGDGTLNEMENAHKAKLNLIHCYRSMNYIARMM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 286 EEKHQIPWMEYNFFGPTKIAESLRKIADQFDDTIRANAEAVIARYEGQMAAIIAKYRPRLEGRKVLLYMGGLRPRHVIGA 365
Cdd:cd01976 239 EEKYGIPWMEYNFFGPTKIAESLRKIAAYFDDEITAKTEEVIAEYKPAMEAVIAKYRPRLEGKTVMLYVGGLRPRHYIGA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 366 YEDLGMEIIAAGYEFAHNDDYDRTLPDLKEGTLLFDDASSYELEAFVKALKPDLIGSGIKEKYIFQKMGVPFRQMHSWDY 445
Cdd:cd01976 319 YEDLGMEVVGTGYEFAHRDDYERTEVIPKEGTLLYDDVTHYELEEFVKRLKPDLIGSGIKEKYVFQKMGIPFRQMHSWDY 398
|
410 420
....*....|....*....|...
gi 575523319 446 SGPYHGYDGFAIFARDMDMTLNN 468
Cdd:cd01976 399 SGPYHGFDGFAIFARDMDMAINS 421
|
|
| N2-ase-Ialpha |
TIGR01862 |
nitrogenase component I, alpha chain; This model represents the alpha chain of all three ... |
27-471 |
0e+00 |
|
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: 636.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 27 ERRKHMMVSDPEMESVGKCIISNRKSQPGVMTVRGCAYAGSKGVVFGPIKDMAHISHGPVGCGQYSRAGRRNYYTGVSGV 106
Cdd:TIGR01862 1 DRKKHIVVKDPGETQSEKLPIANTKTIPGLMTERGCAYAGAKGVIGGPIKDMIHISHGPVGCTYYTWGTKRYPSDNENGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 107 DSFGTLNFTSDFQERDIVFGGDKKLSKLIEEMELLFPLTKGITIQSECPVGLIGDDISAVANASSKALDKPVIPVRCEGF 186
Cdd:TIGR01862 81 GAFLKYVFSTDMQESDIVFGGEKKLKKLIHEAFTEFPLIKAISVYATCPTGLIGDDIEAVAKEVSKEIGKDVVAVNCPGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 187 RGVSQSLGHHIANDVVRDWILNNREgqPFETTPYDVAIIGDYNIGGDAWASRILLEEMGLRVVAQWSGDGTLVEMENTPF 266
Cdd:TIGR01862 161 AGVSQSKGHHIANIAVINDKVGTRE--KEITTEYDVNIIGEYNIGGDAWVMRIYLEEMGIQVVATFTGDGTYDEIRLMHK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 267 VKLNLVHCYRSMNYIARHMEEKHQIPWMEYNFFGPTKIAESLRKIADQFDdtIRANAEAVIARYEGQMAAIIAKYRPRLE 346
Cdd:TIGR01862 239 AKLNLVHCARSANYIANELEERYGIPWMKIDFFGFTYTAESLRAIAAFFG--IEKRAEEVIAEEKAKWKPELDYYKERLQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 347 GRKVLLYMGGLRPRHVIG-AYEDLGMEIIAAGYEFAHNDDYDRTLPDLKEGTLLFDDASSYELEAFVKALKPDLIGSGIK 425
Cdd:TIGR01862 317 GKRVCLYIGGSRLWHWIGsAEEDLGMEVVAVGYEFAHEDDYEKTMKRMGEGTLLIDDPNELEFEEILEKLKPDIIFSGIK 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 575523319 426 EKYIFQKMGVPFRQMHSWDYsGPYHGYDGFAIFARDMDMTLNNPAW 471
Cdd:TIGR01862 397 EKFVAQKLGVPYRQMHSYDN-GPYHGFEGFVNFARDMYNAIYNPCW 441
|
|
| Nitrogenase_MoFe_alpha_like |
cd01967 |
Nitrogenase_MoFe_alpha_like: Nitrogenase MoFe protein, alpha subunit_like. The nitrogenase ... |
54-468 |
0e+00 |
|
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: 635.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 54 PGVMTVRGCAYAGSKGVVFGPIKDMAHISHGPVGCGQYSRAGRRNYYtgvSGVDSFGTLNFTSDFQERDIVFGGDKKLSK 133
Cdd:cd01967 1 PGPMTERGCCAFGGAGVVLGPIKDAVHIVHGPIGCAYYTWDTRRNLS---SGENLFYKYGFSTDMQEKDIVFGGEKKLKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 134 LIEEMELLFPLtKGITIQSECPVGLIGDDISAVANASSKALDKPVIPVRCEGFRGVSQSLGHHIANDVVRDWILNNREgq 213
Cdd:cd01967 78 AIKEAYERFPP-KAIFVYSTCPTGLIGDDIEAVAKEASKELGIPVIPVNCEGFRGVSQSLGHHIANDAILDHLVGTKE-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 214 PFETTPYDVAIIGDYNIGGDAWASRILLEEMGLRVVAQWSGDGTLVEMENTPFVKLNLVHCYRSMNYIARHMEEKHQIPW 293
Cdd:cd01967 155 PEEKTPYDVNIIGEYNIGGDAWVIKPLLEELGIRVNATFTGDGTVDELRRAHRAKLNLVHCSRSMNYLAREMEERYGIPY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 294 MEYNFFGPTKIAESLRKIADQFDDTirANAEAVIARYEGQMAAIIAKYRPRLEGRKVLLYMGGLRPRHVIGAYEDLGMEI 373
Cdd:cd01967 235 MEVNFYGFEDTSESLRKIAKFFGDE--EKAEEVIAEEEARIKPELEKYRERLKGKKVIIYTGGARSWHVIAALRELGMEV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 374 IAAGYEFAHNDDYDRTLPDLKEGTLLFDDASSYELEAFVKALKPDLIGSGIKEKYIFQKMGVPFRQMHSWDySGPYHGYD 453
Cdd:cd01967 313 VAAGYEFGHDDDYERIRKILDEGTLLVDDYNDLELEELVEKLKPDLILSGIKEKYVAQKLGIPFLDLHSER-NGPYAGYE 391
|
410
....*....|....*
gi 575523319 454 GFAIFARDMDMTLNN 468
Cdd:cd01967 392 GFLNFARDIDTALNS 406
|
|
| NifD/CfbD |
COG2710 |
Nitrogenase Mo-Fe protein NifD/coenzyme F430 biosynthesis subunit CfbD [Coenzyme transport and ... |
49-472 |
6.75e-162 |
|
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: 464.20 E-value: 6.75e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 49 NRKSQpGVMTVRGCAYAGSKgVVFGPIKDMAHISHGPVGCGQYSRAGRRNYYtgvsgvdSFGTLNFTSDFQERDIVFGGD 128
Cdd:COG2710 1 NRKAL-GVNPAKGCQPLGAK-LALLGIKDAIPLVHGSQGCAAYSRVTRGRHF-------KEPIPLFSTDMTEDDVVFGGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 129 KKLSKLIEEMELLF-PltKGITIQSECPVGLIGDDISAVANASSKALDKPVIPVRCEGFRGvSQSLGHHIANDVVRDWIL 207
Cdd:COG2710 72 KNLEEAIKNIIERYkP--KLIFVYTTCLTETIGDDIEAVIKEAREELGIPVVPVSTPGFVG-SHSTGYHIAVEAIVEQLV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 208 NNREgqpfETTPYDVAIIGDYN-IGGDAWASRILLEEMGLRVVAQWS-GDGTLVEMENTPFVKLNLVHCYRSMNYIARHM 285
Cdd:COG2710 149 GTGE----PKTPGKINLIGGYNlIPGDLWEIKRLLEEMGLRVIALPDlGGTTVEEIADAGRAKLNLVLCSRSGNYAARYL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 286 EEKHQIPWME-YNFFGPTKIAESLRKIADQFDDTIranaEAVIARYEGQMAAIIAKYRPRLEGRKVLLYMGGLRPRHVIG 364
Cdd:COG2710 225 EEKYGIPYLEfVSPIGLEATDEFLRKLAELFGKPV----PEVIARERGRLVDALADYHFYLGGKKVAIYGDPDLLWGLAS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 365 AYEDLGMEIIAAGYEFAHNDDYDRT---LPDLKEGTLLfDDASSYELEAFVKALKPDLIGSGIKEKYIFQKMGVPFRQMH 441
Cdd:COG2710 301 FLLELGMEPVAAVTTTGSPEDYERIkelLEELPEGTVI-DDGDLEELEELLKELKPDLLIGGSKGKYLARKLGIPLLRVG 379
|
410 420 430
....*....|....*....|....*....|....*..
gi 575523319 442 SWDY------SGPYHGYDGFAIFARDMDMTLNNPAWN 472
Cdd:COG2710 380 FPIYdrvglqRRPYAGYRGALNLLEDIANALLSPVWE 416
|
|
| Oxidoreductase_nitrogenase |
cd00316 |
The nitrogenase enzyme system catalyzes the ATP-dependent reduction of dinitrogen to ammonia. ... |
56-467 |
2.86e-149 |
|
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: 431.70 E-value: 2.86e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 56 VMTVRGCAYAGSKGVVFGpIKDMAHISHGPVGCGQYSRAGRRNYYtgvsgvdSFGTLNFTSDFQERDIVFGG-DKKLSKL 134
Cdd:cd00316 1 INPAKGCAPLGAARVALG-IKDAIPLVHGPQGCAYFTRLTLRRHF-------KEPIPLFTTSMTEKDVVFGGgEKLLEAI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 135 IEEMELLFPltKGITIQSECPVGLIGDDISAVANASSKALDKPVIPVRCEGFRGvSQSLGHHIANDVVRDWILNNREgqP 214
Cdd:cd00316 73 INELKRYKP--KVIFVYTTCTTELIGDDIEAVAKEASKEIGIPVVPASTPGFRG-SQSAGYDAAVKAIIDHLVGTAE--P 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 215 FETTPYDVAIIGDYNI-GGDAWASRILLEEMGLRVVAQWSGDGTLVEMENTPFVKLNLVHCYRSMNYIARHMEEKHQIPW 293
Cdd:cd00316 148 EETEPGSVNLIGGYNLgGGDLRELKRLLEEMGIRVNALFDGGTTVEELRELGNAKLNLVLCRESGLYLARYLEEKYGIPY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 294 MEYNFFGPTKIAESLRKIADQFDdtIRANAEAVIARYEGQMAAIIAKYRPRLEGRKVLLYMGGLRPRHVIGAYEDLGMEI 373
Cdd:cd00316 228 ILINPIGLEATDAFLRKLAELFG--IEKEVPEVIARERARLLDALADYHEYLGGKKVAIFGDGDLLLALARFLLELGMEV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 374 IAAGYEFAHNDDYDRTLPDLKEGTLLFDDASSYELEAFVKALKPDLIGSGIKEKYIFQKMGVPFRQMHSWDYSGPYHGYD 453
Cdd:cd00316 306 VAAGTTFGHKADYERREELLGEGTEVVDDGDLEELEELIRELKPDLIIGGSKGRYIAKKLGIPLVRIGFPIHRRPYVGYE 385
|
410
....*....|....
gi 575523319 454 GFAIFARDMDMTLN 467
Cdd:cd00316 386 GALNLAEEIANALL 399
|
|
| nifE |
TIGR01283 |
nitrogenase molybdenum-iron cofactor biosynthesis protein NifE; This protein is part of the ... |
43-471 |
1.13e-132 |
|
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: 391.34 E-value: 1.13e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 43 GKCIISNRKSQPGVMTVRGCAYAGSKgVVFGPIKDMAHISHGPVGCGQYSRAGRRNYYTGvsgvDSFGTLNFTSDFQERD 122
Cdd:TIGR01283 23 KGCKSGCANSLPGGATQRGCVFDGAR-IVLLPITDAAHLVHGPIGCAGSSWDIRGSRSSG----PELYRLGFTTDLTEKD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 123 IVFGGDKKLSKLIEEM-ELLFPltKGITIQSECPVGLIGDDISAVANASSKALDKPVIPVRCEGFRGvSQSLGHHIANDV 201
Cdd:TIGR01283 98 VIFGGEKKLFHAIREIvERYHP--PAVFVYSTCVPALIGDDLEAVCKAAAEKTGIPVIPVDSEGFYG-TKNLGNKLACDA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 202 VRDWILNNREGQ--PFETTPYDVAIIGDYNIGGDAWASRILLEEMGLRVVAQWSGDGTLVEMENTPFVKLNLVHCYRSMN 279
Cdd:TIGR01283 175 LLKHVIGTREPEplPVGITVHDINLIGEFNVAGEFWHVLPLLEKLGIRVLATITGDSRYAEVQTAHRAKLNMVQCSKAMI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 280 YIARHMEEKHQIPWMEYNFFGPTKIAESLRKIADQF-DDTIRANAEAVIARYEGQMAAIIAKYRPRLEGRKVLLYMGGLR 358
Cdd:TIGR01283 255 NLARKMEEKYGIPYFEGSFYGIEDTSKALRDIADLFgDPELLKRTEELIAREEAKIRPALEPYRERLKGKKAAIYTGGVK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 359 PRHVIGAYEDLGMEIIAAGYEFAHNDDYDRTLPDLKEGTLLFDDASSYELEAFVKALKPDLIGSGIKEKYIFQKMGVPFR 438
Cdd:TIGR01283 335 SWSVVSALQDLGMEVVATGTQKSTEEDYARIRELMGEGTVMLDDANPRELLKLLLEYKADILIAGGRERYTALKLGIPFL 414
|
410 420 430
....*....|....*....|....*....|...
gi 575523319 439 QmHSWDYSGPYHGYDGFAIFARDMDMTLNNPAW 471
Cdd:TIGR01283 415 D-INHEREHPYAGYDGMVEFAREVDLTVESPIW 446
|
|
| Nitrogenase_NifE_I |
cd01968 |
Nitrogenase_NifE_I: a subgroup of the NifE subunit of the NifEN complex: NifE forms an ... |
54-471 |
5.29e-130 |
|
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: 382.82 E-value: 5.29e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 54 PGVMTVRGCAYAGSKgVVFGPIKDMAHISHGPVGCGQYS---RAGRRnyytgvSGVDSFGTlNFTSDFQERDIVFGGDKK 130
Cdd:cd01968 2 PGGVTQRGCVFDGAR-VVLMPITDAAHLVHGPIGCAGYSwdiRGSRS------SGSELYRM-GFSTDLSEKDVIFGGEKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 131 LSKLIEEM-ELLFPltKGITIQSECPVGLIGDDISAVANASSKALDKPVIPVRCEGFRGvSQSLGHHIANDVVRDWILNN 209
Cdd:cd01968 74 LYKAILEIiERYHP--KAVFVYSTCVVALIGDDIDAVCKTASEKFGIPVIPVHSPGFVG-NKNLGNKLACEALLDHVIGT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 210 REgqPFETTPYDVAIIGDYNIGGDAWASRILLEEMGLRVVAQWSGDGTLVEMENTPFVKLNLVHCYRSMNYIARHMEEKH 289
Cdd:cd01968 151 EE--PEPLTPYDINLIGEFNVAGELWGVKPLLEKLGIRVLASITGDSRVDEIRRAHRAKLNVVQCSKSMIYLARKMEEKY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 290 QIPWMEYNFFGPTKIAESLRKIADQFDDT-IRANAEAVIARYEGQMAAIIAKYRPRLEGRKVLLYMGGLRPRHVIGAYED 368
Cdd:cd01968 229 GIPYIEVSFYGIRDTSKSLRNIAELLGDEeLIERTEELIAREEARLRPELAPYRARLEGKKAALYTGGVKSWSLVSALQD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 369 LGMEIIAAGYEFAHNDDYDRTLPDLKEGTLLFDDASSYELEAFVKALKPDLIGSGIKEKYIFQKMGVPFRQmHSWDYSGP 448
Cdd:cd01968 309 LGMEVVATGTQKGTKEDYERIKELLGEGTVIVDDANPRELKKLLKEKKADLLVAGGKERYLALKLGIPFCD-INHERKHP 387
|
410 420
....*....|....*....|...
gi 575523319 449 YHGYDGFAIFARDMDMTLNNPAW 471
Cdd:cd01968 388 YAGYEGMLNFAKEVDLAVNSPVW 410
|
|
| Oxidored_nitro |
pfam00148 |
Nitrogenase component 1 type Oxidoreductase; |
62-467 |
5.01e-115 |
|
Nitrogenase component 1 type Oxidoreductase;
Pssm-ID: 395096 [Multi-domain] Cd Length: 398 Bit Score: 344.23 E-value: 5.01e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 62 CAYAGSKgVVFGPIKDMAHISHGPVGCGQYSRAGRRNYYTGVSGVdsfgtlnFTSDFQERDIVFGGDKKLSKLIEEMELL 141
Cdd:pfam00148 1 CAPAGAS-VALLGIKDAVPLVHGPQGCATYVRLLLTRHFREPIPL-------ATTSLTEKDVVFGGEENLKEAIKEVDKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 142 FPlTKGITIQSECPVGLIGDDISAVANASSKALDKPVIPVRCEGFRGvSQSLGHHIANDVVRDWILnnreGQPFETTPYD 221
Cdd:pfam00148 73 YK-PKAIFVISTCLTETIGDDIEAVAREAREELGIPVIPVSTPGFVG-SHSTGYDVALEAIVRQLV----GKKGEKEPGT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 222 VAIIGDYNIG-GDAWASRILLEEMGLRVVAQWSGDGTLVEMENTPFVKLNLVHCYRSMNYIARHMEEKHQIPWMEY-NFF 299
Cdd:pfam00148 147 VNILGGFNLGpGDLREIKRLLEKLGIEVNPVFTGGTTLEDLRAAGNAAANLVLCPFSGEYAAEMLEEKFGVPYIRLgAPI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 300 GPTKIAESLRKIADQFDdtiRANAEAVIARYEGQMAAIIAKYRPRLEGRKVLLYMGGLRPRHVIGAYEDLGMEIIAAGYE 379
Cdd:pfam00148 227 GLEATDRFLRALAKLFG---KEVAPEVIARERGRLLDAMVDYHEYLAGKRVAIYGDPDLVLGLARFLLELGMEPVAVGTG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 380 FAHNDDYDRTLPDLKEGT-LLFDDASSYELEAFVKALKPDLIGSGIKEKYIFQKMGV-------PFRQMHSWDYsGPYHG 451
Cdd:pfam00148 304 TGHPDDYERLKAELEEGDpEVIDGADLEELEELIKELKPDLLLGNSKGRYIARKLGIplvrvgfPIVDRHGLHR-RPYVG 382
|
410
....*....|....*.
gi 575523319 452 YDGFAIFARDMDMTLN 467
Cdd:pfam00148 383 YRGALNLADRIANALL 398
|
|
| Nitrogenase_VFe_alpha |
cd01977 |
Nitrogenase_VFe_alpha -like: Nitrogenase VFe protein, alpha subunit like. This group contains ... |
54-471 |
8.68e-113 |
|
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: 339.03 E-value: 8.68e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 54 PGVMTVRGCAYAGSKGVVFGPIKDMAHISHGPVGCGQYSRAGRRnyYtgVSGVDSFgTLNFT--SDFQERDIVFGGDKKL 131
Cdd:cd01977 1 PGSLSERGCAYCGAKLVIGGVIKDVIHVIHGPVGCTYDTWHTKR--Y--PSDNDNF-QLKYIwsTDMKESHVVFGGEKKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 132 SKLIEEMELLFPLTKGITIQSECPVGLIGDDISAVANASSKAL-DKPVIPVRCEGFRGVSQSLGHHIANDVvrdWIlNNR 210
Cdd:cd01977 76 KKNIIEAFKEFPDIKRMTVYTTCTTALIGDDIKAVAKEVMEELpDVDIFVCNAPGFAGPSQSKGHHVLNIA---WI-NQK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 211 EG--QPFETTPYDVAIIGDYNIGGDAWASRILLEEMGLRVVAQWSGDGTLVEMENTPFVKLNLVHCYRSMNYIARHMEEK 288
Cdd:cd01977 152 VGtvEPEITSDYTINYIGDYNIQGDTEVLQKYFERMGIQVLSTFTGNGTYDDLRWMHRAKLNVVNCARSAGYIANELKKR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 289 HQIPWMEYNFFGPTKIAESLRKIADQFDdtIRANAEAVI----ARYEGQMAAiiakYRPRLEGRKVLLYMGGLRPRHVIG 364
Cdd:cd01977 232 YGIPRLDVDGFGFEYCAESLRKIGAFFG--IEDRAEAVIaeemAKWKPELDW----YKERLKGKKVCIWTGGPKLWHWTK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 365 AYED-LGMEIIAAGYEFAHNDDYDRTLPDLKEGTLLFDDASSYELEAFVKALKPDLIGSGIKEKYIFQKMGVPFRQMHSW 443
Cdd:cd01977 306 VIEDeLGMQVVAMSSKFGHQEDFEKVIARGGEGTIYIDDPNELEFFEILEMLKPDIILTGPRVGELVKKLHVPYVNIHAY 385
|
410 420
....*....|....*....|....*...
gi 575523319 444 dYSGPYHGYDGFAIFARDMDMTLNNPAW 471
Cdd:cd01977 386 -HNGPYMGFEGFVNLARDMYNAIYSPIW 412
|
|
| alt_nitrog_alph |
TIGR01284 |
nitrogenase alpha chain; This model represents the alpha chains of various forms of the ... |
27-472 |
4.05e-108 |
|
nitrogenase alpha chain; This model represents the alpha chains of various forms of the nitrogen-fixing enzyme nitrogenase: vanadium-iron, iron-iron, and molybdenum-iron. Most examples of NifD, the molybdenum-iron type nitrogenase alpha chain, are excluded from this model and described instead by equivalog model TIGR01282. It appears by phylogenetic and UPGMA trees that this model represents a distinct clade of NifD homologs, in which arose several molybdenum-independent forms. [Central intermediary metabolism, Nitrogen fixation]
Pssm-ID: 188127 Cd Length: 457 Bit Score: 328.72 E-value: 4.05e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 27 ERRKHMMV---SDPEMESVGKCiisNRKSQPGVMTVRGCAYAGSKGVVFGPIKDMAHISHGPVGCgQYSRAGRRNYytgV 103
Cdd:TIGR01284 11 ERKKHIYVkkqGEPEGDFLPAC---NTTTIPGCMSERGCAFCGAKGVIGGAIKDAIHVIHGPVGC-TYDTWHTKRY---P 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 104 SGVDSFgTLNFT--SDFQERDIVFGGDKKLSKLIEEMELLFPLTKGITIQSECPVGLIGDDISAVANASSKAL-DKPVIP 180
Cdd:TIGR01284 84 TDNEKF-NLKYItgTDLKESHVVFGGEKKLKRCILEAFREFPEIKRMYTYATCTTALIGDDIDAIAREVMEEIpDVDVFA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 181 VRCEGFRGVSQSLGHHIANdvvRDWIlNNREG--QPFETTPYDVAIIGDYNIGGDAWASRILLEEMGLRVVAQWSGDGTL 258
Cdd:TIGR01284 163 INAPGFAGPSQSKGHHVAN---ITWI-NDKVGtaEPEITTEYDVNLIGEYNIQGDLWVLKKYFERMGIQVLSTFTGNGCY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 259 VEMENTPFVKLNLVHCYRSMNYIARHMEEKHQIPWMEYNFFGPTKIAESLRKIADQFDdtIRANAEAVIARYEGQMAAII 338
Cdd:TIGR01284 239 DELRWMHRAKLNVVRCARSANYIANELEERYGIPRLDIDFFGFEYCAKNLRKIGEFFG--IEERAERVIEEEMAKWKPEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 339 AKYRPRLEGRKVLLYMGGLRPRHVIGAYED-LGMEIIAAGYEFAHNDDYDRTLPDLKEGTLLFDDASSYELEAFVKALKP 417
Cdd:TIGR01284 317 DWYKERLRGKKVWVWSGGPKLWHWPRPLEDeLGMEVVAVSTKFGHEDDYEKIIARVREGTVIIDDPNELELEEIIEKYKP 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 575523319 418 DLIGSGIKEKYIFQKMGVPFRQMHSWdYSGPYHGYDGFAIFARDMDMTLNNPAWN 472
Cdd:TIGR01284 397 DIILTGIREGELAKKLGVPYINIHSY-HNGPYIGFEGFVNLARDMYNAIYNPVWD 450
|
|
| PRK14477 |
PRK14477 |
bifunctional nitrogenase molybdenum-cofactor biosynthesis protein NifE/NifN; Provisional |
50-482 |
9.90e-100 |
|
bifunctional nitrogenase molybdenum-cofactor biosynthesis protein NifE/NifN; Provisional
Pssm-ID: 172952 [Multi-domain] Cd Length: 917 Bit Score: 319.76 E-value: 9.90e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 50 RKSQPGVMTVRGCAYAGSKgVVFGPIKDMAHISHGPVGCGQYSRAGRrnyytgvsGVDSFGT----LNFTSDFQERDIVF 125
Cdd:PRK14477 24 KKSEPGEGAERSCAYDGAR-VVLMPITDVIHLVHGPIACAGNSWDNR--------GARSSGSqlyrRGFTTEMLENDVIF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 126 GGDKKLSKLIEEMELLFPlTKGITIQSECPVGLIGDDISAVANASSKALDKPVIPVRCEGFRGvSQSLGHHIANDVVRDW 205
Cdd:PRK14477 95 GGEKKLYRAILELAERYQ-PKAVFVYATCVTALTGDDVEAVCKAAAEKVGIPVIPVNTPGFIG-DKNIGNRLAGEALLKH 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 206 ILNNREgqPFETTPYDVAIIGDYNIGGDAWASRILLEEMGLRVVAQWSGDGTLVEMENTPFVKLNLVHCYRSMNYIARHM 285
Cdd:PRK14477 173 VIGTAE--PEVTTPYDINLIGEYNIAGDLWGMLPLFDRLGIRVLSCISGDAKFEELRYAHRAKLNVIICSKSLTNLARKM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 286 EEKHQIPWMEYNFFGPTKIAESLRKIADQFDD--------TIRANAEAVIARYEGQMAAIIAKYRPRLEGRKVLLYMGGL 357
Cdd:PRK14477 251 EKRYGIPYLEESFYGMTDTAKALRDIARELDDaggglekrVLQDRVEKLIAEEEAKCRAALAPYRARLEGKRVVLFTGGV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 358 RPRHVIGAYEDLGMEIIAAGYEFAHNDDYDRTLPDLKEGTLLFDDASSYELEAFVKALKPDLIGSGIKEKYIFQKMGVPF 437
Cdd:PRK14477 331 KTWSMVNALRELGVEVLAAGTQNSTLEDFARMKALMHKDAHIIEDTSTAGLLRVMREKMPDLIVAGGKTKFLALKTRTPF 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 575523319 438 RQMHSwDYSGPYHGYDGFAIFARDMDMTLNNPAWNELT--APWLKSA 482
Cdd:PRK14477 411 LDINH-GRSHPYAGYEGMVTFARQLDLTVNNPIWPALRapAPWEKGA 456
|
|
| Nitrogenase_VnfE_like |
cd01972 |
Nitrogenase_VnfE_like: VnfE subunit of the VnfEN complex_like. This group in addition to VnfE ... |
60-420 |
1.62e-31 |
|
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: 125.61 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 60 RGCAYAGSKGVVFGpIKDMAHISHGPVGCGQYSRAGRRNYYTGVSGVDSFGTLnFTSDFQERDIVFGGDKKLSKLIEEM- 138
Cdd:cd01972 8 SMCKFWTAFCILSG-IRDAVVVQHGPIGCAAGQSFFNRLYRCGEMRRGLNEPV-LSTNLTEKDVVFGGEKKLEDTIKEAy 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 139 ELLFPltKGITIQSECPVGLIGDDISAVANASSKALDKPVIPVRCEGFRGVSQSLGHHIANDVVRDWILNNREGQPFETT 218
Cdd:cd01972 86 SRYKP--KAIFVATSCATGIIGDDVESVVEELEDEIGIPVVALHCEGFKGKHWRSGFDAAFHGILRHLVPPQDPTKQEDS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 219 pydVAIIG-----DYNIGGDAWASRILLEEMGLRVVAQWSGDGTLVEMENTPFVKLNLVHCYRSMNYIARHMEEKHQIPW 293
Cdd:cd01972 164 ---VNIIGlwggpERTEQEDVDEFKRLLNELGLRVNAIIAGGCSVEELERASEAAANVTLCLDLGYYLGAALEQRFGVPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 294 ME----YNFFGpTKiaESLRKIADQFDdtIRANAEAVIARYEGQMAAIIAKYRPRLEGRKVLLYMGGLrPRHVIGA---Y 366
Cdd:cd01972 241 IKapqpYGIEA-TD--KWLREIAKVLG--MEAEAEAVIEREHERVAPEIEELRKALKGKKAIVETGAA-YGHLLIAvlrE 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575523319 367 EDLGMEIIAagYEFAHNDDYDRTLP-------------DLKEGTLLFDDAssYELEAFVKALKPDLI 420
Cdd:cd01972 315 LGFGEVPVV--LVFHHDPTYDRGDSekdllehgvdpeiDITKYTVSNGQY--YQFYNLLKRVKPDFI 377
|
|
| Nitrogenase_VnfN_like |
cd01971 |
Nitrogenase_vnfN_like: VnfN subunit of the VnfEN complex-like. This group in addition to VnfN ... |
61-331 |
3.82e-25 |
|
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: 107.12 E-value: 3.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 61 GCAYAGSKGVVFGpIKDMAHISHGPVGCG--QYSRAGRRNYYTGvSGVDSFGTLNFTsdfqERDIVFGGDKKLSKLIEEM 138
Cdd:cd01971 8 GCALGGALYTVSA-IPRAVPIIHSGPGCAskQSGAVAFGNGYQG-GGYGVAPCTNAT----ETEIVFGGEDRLRELIKST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 139 ELLFPlTKGITIQSECPVGLIGDDISAVANaSSKALDKPVIPVRCEGFRGvSQSLGHHIANDVVRDWILNNREG-QP--- 214
Cdd:cd01971 82 LSIID-ADLFVVLTGCIAEIIGDDVGAVVS-EFQEGGAPIVYLETGGFKG-NNYAGHEIVLKAIIDQYVGQSEEkEPglv 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 215 --FETTPY-DVAIIGDYniggdAWASRiLLEEMGLRVVAQWSGDGTLVEMENTPFVKLNLVHCYRSMNYIARHMEEKHQI 291
Cdd:cd01971 159 nlWGPVPYqDPFWRGDL-----EEIKR-VLEGIGLKVNILFGPESNGEELRSIPKAQFNLVLSPWVGLEFAQHLEEKYGQ 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 575523319 292 PWMEYNFF--GPTKIAESLRKIADqFDDTIRANAEAVIARYE 331
Cdd:cd01971 233 PYIHSPTLpiGAKATAEFLRQVAK-FAGIEKAKVEAFIKAEE 273
|
|
| Nitrogenase_MoFe_beta_like |
cd01965 |
Nitrogenase_MoFe_beta_like: Nitrogenase MoFe protein, beta subunit_like. The nitrogenase ... |
75-454 |
1.04e-17 |
|
Nitrogenase_MoFe_beta_like: Nitrogenase MoFe protein, beta subunit_like. The nitrogenase enzyme catalyzes the ATP-dependent reduction of dinitrogen (N2) to ammonia. This group contains the 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). These 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 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. 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, 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 N2-reduction and, ethane as a minor product during acetylene reduction
Pssm-ID: 238927 [Multi-domain] Cd Length: 428 Bit Score: 84.92 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 75 IKDMAHISHGPVGCGQYSRAG-RRNYYTGVSGVdsfgtlnfTSDFQERDIVFGGDKKLSKLIEEMELLFPlTKGITIQSE 153
Cdd:cd01965 20 IEGCMPLVHGSQGCSSFARVLfTRHFKEPIPIA--------STSMTEDAAVFGGEDNLIEALKNLLSRYK-PDVIGVLTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 154 CPVGLIGDDISAVANASSKAL----DKPVIPVRCEGFRGvSQSLGHHIAndvVRDwILNNREGQPFETTPYDVAII--GD 227
Cdd:cd01965 91 CLTETIGDDVAGFIKEFRAEGpepaDFPVVYASTPSFKG-SHETGYDNA---VKA-IIEQLAKPSEVKKNGKVNLLpgFP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 228 YNIGGDAWASRIlLEEMGLRVVA--------------QWS----GDGTLVEMENTPFVKLNLVHCYRSMNYIARHMEEKH 289
Cdd:cd01965 166 LTPGDVREIKRI-LEAFGLEPIIlpdlsdsldghltdGYSpltkGGTTLEEIRDAGNAKATIALGEYSGRKAAKALEEKF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 290 QIPWmeYNFFGPTKIAESlrkiaDQFddtIRANAE----AVIARYE---GQMAAIIAKYRPRLEGRKVLLYmggLRPRHV 362
Cdd:cd01965 245 GVPY--ILFPTPIGLKAT-----DEF---LRALSKlsgkPIPEELErerGRLLDAMLDSHFYLGGKRVAIA---GDPDLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 363 IGAYE---DLGMEIIAAgyeFAHNDDyDRTLPDLKEGTLLFD-------DASSYELEAFVKALKPDL-IGSGiKEKYIFQ 431
Cdd:cd01965 312 LGLSRfllEMGAEPVAA---VTGTDN-PPFEKRMELLASLEGipaevvfVGDLWDLESLAKEEPVDLlIGNS-HGRYLAR 386
|
410 420 430
....*....|....*....|....*....|.
gi 575523319 432 KMGVP--------FRQMHSWDYsgPYHGYDG 454
Cdd:cd01965 387 DLGIPlvrvgfpiFDRLGLHRR--PYVGYRG 415
|
|
| Nitrogenase_VFe_beta_like |
cd01973 |
Nitrogenase_VFe_beta -like: Nitrogenase VFe protein, beta subunit like. This group contains ... |
62-214 |
2.56e-05 |
|
Nitrogenase_VFe_beta -like: Nitrogenase VFe protein, beta subunit like. This group contains proteins similar to the beta subunits of the VFe protein of the vanadium-dependent (V-) nitrogenase. Nitrogenase catalyzes the ATP-dependent reduction of dinitrogen (N2) to ammonia. In addition to V-nitrogenase there is a molybdenum (Mo)-dependent nitrogenase and an iron only (Fe-) nitrogenase. The Mo-nitrogenase 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: 238933 [Multi-domain] Cd Length: 454 Bit Score: 46.71 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 62 CAYAGSKGVVFGpIKDMAHISHGPVGCGQYSRAGRRNYYTgvsgvDSFGTLnfTSDFQERDIVFGGDKKLSKLIEEMELL 141
Cdd:cd01973 13 CQPAGAQYAGIG-IKDCIPLVHGGQGCTMFVRLLFAQHFK-----ENFDIA--SSSLHEDSAVFGGAKRVEEGVLVLARR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 142 FPLTKGITIQSECPVGLIGDDISAVANASSKALDKP-------VIPVRCEGFRGvSQSLGHHIAndvVRDWILN-NREGQ 213
Cdd:cd01973 85 YPDLRVIPIITTCSTEIIGDDIEGVIRKLNEALKEEfpdrevhLIPVHTPSFKG-SMVTGYDEA---VRSVVKTiAKKGA 160
|
.
gi 575523319 214 P 214
Cdd:cd01973 161 P 161
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
287-377 |
7.65e-05 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 44.22 E-value: 7.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 287 EKHQIPWMEYNFFGPTKIAESLRKIADQFDDTirANAEAVIARYEGQMAAIIAKYRPRLEGRKVLLYMGGLRPRHVIGA- 365
Cdd:COG0614 80 EKIGIPVVVLDPRSLEDLYESIRLLGELLGRE--ERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPLYTAGGg 157
|
90
....*....|....*...
gi 575523319 366 ------YEDLGMEIIAAG 377
Cdd:COG0614 158 sfigelLELAGGRNVAAD 175
|
|
| Nitrogenase_NifN_2 |
cd03466 |
Nitrogenase_nifN_2: A subgroup of the NifN subunit of the NifEN complex: NifN forms an ... |
72-436 |
8.31e-05 |
|
Nitrogenase_nifN_2: A subgroup of the NifN subunit of the NifEN complex: NifN forms an alpha2beta2 tetramer with NifE. NifN and nifE are structurally homologous to nitrogenase MoFe protein beta and alpha 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). This group also contains the Clostidium fused NifN-NifB protein.
Pssm-ID: 239549 [Multi-domain] Cd Length: 429 Bit Score: 44.69 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 72 FGPIKDMAHISHGPVGCGQYSRAGRRNYYTGVSGVDSfgtlnftSDFQERDIVFGGDKKLSKLIEEMELLF-PLTKGITi 150
Cdd:cd03466 20 FKGIEGCMPLLHGSQGCSTYIRRHMARHYNEPVDIAS-------SSLNEETTVYGGEKNLKKGLKNVIEQYnPEVIGIA- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 151 qSECPVGLIGDDISAVAN--ASSKALDKP-VIPVRCEGFRGvSQSLGHHIAndvVRDwILNNREGQPFETTPYDVaIIGD 227
Cdd:cd03466 92 -TTCLSETIGEDVPRIIRefREEVDDSEPkIIPASTPGYGG-THVEGYDTA---VRS-IVKNIAVDPDKIEKINV-IAGM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 228 YNIGGDAWASRIlLEEMGLRVV----------AQWSGDGTLVEMENTP----------FVKLNLVHCYRSMNYIARHMEE 287
Cdd:cd03466 165 MSPADIREIKEI-LREFGIEYIllpdtsetldGPFWGEYHRLPSGGTPiseikgmggaKATIELGMFVDHGLSAGSYLEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 288 KHQIPWMEYNffgptkIAESLRKiADQFDDTIRANAEAVIA----RYEGQM--AAIIA-KYrprLEGRKVLLYMgglRPR 360
Cdd:cd03466 244 EFGIPNYRLP------LPIGLRA-TDEFMSLLSKLTGKPIPekytRERGRLldAMIDAhKY---NFGRKAAIYG---EPD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 361 HVIGAYE---DLGM--EIIAAGYEFAH-NDDYDRTLPDLKEGTLLFDDASSYELEAFVKALKPD-LIGSGiKEKYIFQKM 433
Cdd:cd03466 311 FVVAITRfvlENGMvpVLIATGSESKKlKEKLEEDLKEYVEKCVILDGADFFDIESYAKELKIDvLIGNS-YGRRIAEKL 389
|
...
gi 575523319 434 GVP 436
Cdd:cd03466 390 GIP 392
|
|
| Nitrogenase_MoFe_beta |
cd01974 |
Nitrogenase_MoFe_beta: Nitrogenase MoFe protein, beta subunit. The nitrogenase enzyme ... |
82-372 |
1.09e-03 |
|
Nitrogenase_MoFe_beta: Nitrogenase MoFe protein, beta subunit. The nitrogenase enzyme catalyzes the ATP-dependent reduction of dinitrogen to ammonia. The Molybdenum (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. This group contains the beta subunit of the MoFe protein. 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: 238934 [Multi-domain] Cd Length: 435 Bit Score: 41.49 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 82 SHGPVGCGQYSRAG-RRNYYTGVSGVdsfgtlnfTSDFQERDIVFGGdkkLSKLIEEMELLFPLTKG--ITIQSECPVGL 158
Cdd:cd01974 31 VHGSQGCVAYFRSHlSRHFKEPVSAV--------SSSMTEDAAVFGG---QNNLIDGLKNAYAVYKPdmIAVSTTCMAEV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 159 IGDDISAVANASSKA----LDKPVIPVRCEGFrgvsqsLGHHIAN-DVVRDWILNNregqpFETTPYDVAIIGDYNI--G 231
Cdd:cd01974 100 IGDDLNAFIKNAKNKgsipADFPVPFANTPSF------VGSHITGyDNMVKGILTH-----LTEGSGGAGKNGKLNIipG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 232 GDAWASRI-----LLEEMGLRVVA-----------------QWSGDGTLVEMENTPFVKLNLVHCYRSMNYIARHMEEKH 289
Cdd:cd01974 169 FDTYAGNMreikrLLELMGVDYTIlpdtsdvldtpadgeyrMYPGGTTLEELKDAGNAKATLALQEYATEKTAKFLEKKC 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523319 290 QIPWMEYNF-FGPTKIAESLRKIADQFDDTIRANAEaviarYE-GQMAAIIAKYRPRLEGRKVLLYmGGlrPRHVIGAYE 367
Cdd:cd01974 249 KVPVETLNMpIGVAATDEFLMALSELTGKPIPEELE-----EErGRLVDAMTDSHQYLHGKKFALY-GD--PDFLIGLTS 320
|
....*...
gi 575523319 368 ---DLGME 372
Cdd:cd01974 321 fllELGME 328
|
|
| |
