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Conserved domains on  [gi|667705087|gb|KFA57936|]
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hypothetical protein HMPREF1632_00065 [Mageeibacillus indolicus 0009-5]

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. ...
 54-406 1.94e-47

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 pfam00148:

Pssm-ID: 445915 [Multi-domain]  Cd Length: 398  Bit Score: 168.19  E-value: 1.94e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087   54 CPLFGSLMLIRRIRNASCLVVGTDECTYYAKssaMAGGDFGTLAERCYSLVLQPTDISFGSGDKLNAAIEEITAQGKPEL 133
Cdd:pfam00148   1 CAPAGASVALLGIKDAVPLVHGPQGCATYVR---LLLTRHFREPIPLATTSLTEKDVVFGGEENLKEAIKEVDKRYKPKA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  134 LFVITTCVVELIGDDFDSLCARAAARLNIAVTVIHTEHYRSeNHLAGMEAALTACLPIMREQPPQLA---VNILGPRHDN 210
Cdd:pfam00148  78 IFVISTCLTETIGDDIEAVAREAREELGIPVIPVSTPGFVG-SHSTGYDVALEAIVRQLVGKKGEKEpgtVNILGGFNLG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  211 FAKS-ELAECLNTIGLPINLVLPSDCDITDIVKAPAARLNLV-TDRIGLPLAQAMLDRFGLPYIYFDRFV----TPRTIE 284
Cdd:pfam00148 157 PGDLrEIKRLLEKLGIEVNPVFTGGTTLEDLRAAGNAAANLVlCPFSGEYAAEMLEEKFGVPYIRLGAPIgleaTDRFLR 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  285 N--AYLDlfdkilKPETRQRMEEWlnsKKNAARRIAeRVTPKLQG-YSYIYGNTPLPqLELNAYLTELGLQPKLIQLSQW 361
Cdd:pfam00148 237 AlaKLFG------KEVAPEVIARE---RGRLLDAMV-DYHEYLAGkRVAIYGDPDLV-LGLARFLLELGMEPVAVGTGTG 305

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 667705087  362 TTADDTAVNRILAKYNPYVTRNANIAPLRDMYDILRPEFYFGHEY 406
Cdd:pfam00148 306 HPDDYERLKAELEEGDPEVIDGADLEELEELIKELKPDLLLGNSK 350
 
Name Accession Description Interval E-value
Oxidored_nitro pfam00148
Nitrogenase component 1 type Oxidoreductase;
54-406 1.94e-47

Nitrogenase component 1 type Oxidoreductase;


Pssm-ID: 395096 [Multi-domain]  Cd Length: 398  Bit Score: 168.19  E-value: 1.94e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087   54 CPLFGSLMLIRRIRNASCLVVGTDECTYYAKssaMAGGDFGTLAERCYSLVLQPTDISFGSGDKLNAAIEEITAQGKPEL 133
Cdd:pfam00148   1 CAPAGASVALLGIKDAVPLVHGPQGCATYVR---LLLTRHFREPIPLATTSLTEKDVVFGGEENLKEAIKEVDKRYKPKA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  134 LFVITTCVVELIGDDFDSLCARAAARLNIAVTVIHTEHYRSeNHLAGMEAALTACLPIMREQPPQLA---VNILGPRHDN 210
Cdd:pfam00148  78 IFVISTCLTETIGDDIEAVAREAREELGIPVIPVSTPGFVG-SHSTGYDVALEAIVRQLVGKKGEKEpgtVNILGGFNLG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  211 FAKS-ELAECLNTIGLPINLVLPSDCDITDIVKAPAARLNLV-TDRIGLPLAQAMLDRFGLPYIYFDRFV----TPRTIE 284
Cdd:pfam00148 157 PGDLrEIKRLLEKLGIEVNPVFTGGTTLEDLRAAGNAAANLVlCPFSGEYAAEMLEEKFGVPYIRLGAPIgleaTDRFLR 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  285 N--AYLDlfdkilKPETRQRMEEWlnsKKNAARRIAeRVTPKLQG-YSYIYGNTPLPqLELNAYLTELGLQPKLIQLSQW 361
Cdd:pfam00148 237 AlaKLFG------KEVAPEVIARE---RGRLLDAMV-DYHEYLAGkRVAIYGDPDLV-LGLARFLLELGMEPVAVGTGTG 305

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 667705087  362 TTADDTAVNRILAKYNPYVTRNANIAPLRDMYDILRPEFYFGHEY 406
Cdd:pfam00148 306 HPDDYERLKAELEEGDPEVIDGADLEELEELIKELKPDLLLGNSK 350
Oxidoreductase_nitrogenase cd00316
The nitrogenase enzyme system catalyzes the ATP-dependent reduction of dinitrogen to ammonia. ...
 54-413 2.25e-41

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: 151.66  E-value: 2.25e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  54 CPLFGSLMLIRRIRNASCLVVGTDECTYYAKSSAMAGGDFGTlaeRCYSLVLQPTDISFGSGDKLNAAIEEITAQGKPEL 133
Cdd:cd00316    7 CAPLGAARVALGIKDAIPLVHGPQGCAYFTRLTLRRHFKEPI---PLFTTSMTEKDVVFGGGEKLLEAIINELKRYKPKV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 134 LFVITTCVVELIGDDFDSLCARAAARLNIAVTVIHTEHYRSEnHLAGMEAALTA---CLPIMREQPPQLA--VNILGPRH 208
Cdd:cd00316   84 IFVYTTCTTELIGDDIEAVAKEASKEIGIPVVPASTPGFRGS-QSAGYDAAVKAiidHLVGTAEPEETEPgsVNLIGGYN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 209 DNFAK-SELAECLNTIGLPINLVLPSDCDITDIVKAPAARLNLVT-DRIGLPLAQAMLDRFGLPYIyfdrFVTPRTIEN- 285
Cdd:cd00316  163 LGGGDlRELKRLLEEMGIRVNALFDGGTTVEELRELGNAKLNLVLcRESGLYLARYLEEKYGIPYI----LINPIGLEAt 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 286 -AYLDLFDKILKPEtrQRMEEWLNSKKNAARRIAERVTPKLQGYS-YIYGNTPLPqLELNAYLTELGLQPKLIqLSQWTT 363
Cdd:cd00316  239 dAFLRKLAELFGIE--KEVPEVIARERARLLDALADYHEYLGGKKvAIFGDGDLL-LALARFLLELGMEVVAA-GTTFGH 314

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 667705087 364 ADDTAVNRILAKYNPYVTRNANIAPLRDMYDILRPEFYFGHEYFERLLKK 413
Cdd:cd00316  315 KADYERREELLGEGTEVVDDGDLEELEELIRELKPDLIIGGSKGRYIAKK 364
NifD/CfbD COG2710
Nitrogenase Mo-Fe protein NifD/coenzyme F430 biosynthesis subunit CfbD [Coenzyme transport and ...
 79-404 2.88e-31

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: 124.46  E-value: 2.88e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  79 CTYYAKSSAMAGGDFGTlaeRCYSLVLQPTDISFGSGDKLNAAIEEITAQGKPELLFVITTCVVELIGDDFDSLCARAAA 158
Cdd:COG2710   38 CAAYSRVTRGRHFKEPI---PLFSTDMTEDDVVFGGEKNLEEAIKNIIERYKPKLIFVYTTCLTETIGDDIEAVIKEARE 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 159 RLNIAVTVIHTEHYRSeNHLAGMEAALTACLPIM---REQPPQLAVNILGPrhdnFAKS-----ELAECLNTIGLPINlV 230
Cdd:COG2710  115 ELGIPVVPVSTPGFVG-SHSTGYHIAVEAIVEQLvgtGEPKTPGKINLIGG----YNLIpgdlwEIKRLLEEMGLRVI-A 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 231 LPSDCDIT--DIVKAPAARLNLV-TDRIGLPLAQAMLDRFGLPYIYFDRFVtprTIEN--AYLDLFDKILKPEtrqrMEE 305
Cdd:COG2710  189 LPDLGGTTveEIADAGRAKLNLVlCSRSGNYAARYLEEKYGIPYLEFVSPI---GLEAtdEFLRKLAELFGKP----VPE 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 306 WLNSKKNAARRIAERVTPKLQG-YSYIYGNTPLPqLELNAYLTELGLQPKLIqLSQWTTADDTA-VNRILAKYNPY-VTR 382
Cdd:COG2710  262 VIARERGRLVDALADYHFYLGGkKVAIYGDPDLL-WGLASFLLELGMEPVAA-VTTTGSPEDYErIKELLEELPEGtVID 339

                        330       340
                 ....*....|....*....|....*
gi 667705087 383 NANiapLRDMYDILR---PEFYFGH 404
Cdd:COG2710  340 DGD---LEELEELLKelkPDLLIGG 361
nifE TIGR01283
nitrogenase molybdenum-iron cofactor biosynthesis protein NifE; This protein is part of the ...
 105-327 1.18e-20

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: 93.96  E-value: 1.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  105 LQPTDISFGSGDKLNAAIEEITAQGKPELLFVITTCVVELIGDDFDSLCARAAARLNIAVTVIHTEHYRSENHLaGMEAA 184
Cdd:TIGR01283  93 LTEKDVIFGGEKKLFHAIREIVERYHPPAVFVYSTCVPALIGDDLEAVCKAAAEKTGIPVIPVDSEGFYGTKNL-GNKLA 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  185 LTACL--------PIMREQPPQL-AVNILGprHDNFAKS--ELAECLNTIGLPINLVLPSDCDITDIVKAPAARLNLVT- 252
Cdd:TIGR01283 172 CDALLkhvigtrePEPLPVGITVhDINLIG--EFNVAGEfwHVLPLLEKLGIRVLATITGDSRYAEVQTAHRAKLNMVQc 249

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 667705087  253 DRIGLPLAQAMLDRFGLPYIYFDrFVTPRTIENAYLDLFDKILKPETRQRMEEWLNSKKNAARRIAERVTPKLQG 327
Cdd:TIGR01283 250 SKAMINLARKMEEKYGIPYFEGS-FYGIEDTSKALRDIADLFGDPELLKRTEELIAREEAKIRPALEPYRERLKG 323
PRK02910 PRK02910
ferredoxin:protochlorophyllide reductase (ATP-dependent) subunit B;
101-273 3.62e-13

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


Pssm-ID: 235085 [Multi-domain]  Cd Length: 519  Bit Score: 71.45  E-value: 3.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 101 YSlVLQPTDISFGSGDKLNAAIEEITAQGKPELLFVITTCVVELIGDDFDSLcaraAARLNIAVTVIHTE--HYR-SENH 177
Cdd:PRK02910  57 YS-TVQARDLARGTAELLKDTLRRADERFQPDLIVVGPSCTAELLQEDLGGL----AKHAGLPIPVLPLElnAYRvKENW 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 178 laGMEAALT------ACLPIMREQP--PQLAVNILGP-------RHDnfaKSELAECLNTIGLPINLVLPSDCDITDIVK 242
Cdd:PRK02910 132 --AADETFYqlvralAKKAAELPQPktARPSVNLLGPtalgfhhRDD---LTELRRLLATLGIDVNVVAPLGASPADLKR 206

                        170       180       190
                 ....*....|....*....|....*....|..
gi 667705087 243 APAARLNLVTDR-IGLPLAQAMLDRFGLPYIY 273
Cdd:PRK02910 207 LPAAWFNVVLYReIGESAARYLEREFGQPYVK 238
 
Name Accession Description Interval E-value
Oxidored_nitro pfam00148
Nitrogenase component 1 type Oxidoreductase;
54-406 1.94e-47

Nitrogenase component 1 type Oxidoreductase;


Pssm-ID: 395096 [Multi-domain]  Cd Length: 398  Bit Score: 168.19  E-value: 1.94e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087   54 CPLFGSLMLIRRIRNASCLVVGTDECTYYAKssaMAGGDFGTLAERCYSLVLQPTDISFGSGDKLNAAIEEITAQGKPEL 133
Cdd:pfam00148   1 CAPAGASVALLGIKDAVPLVHGPQGCATYVR---LLLTRHFREPIPLATTSLTEKDVVFGGEENLKEAIKEVDKRYKPKA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  134 LFVITTCVVELIGDDFDSLCARAAARLNIAVTVIHTEHYRSeNHLAGMEAALTACLPIMREQPPQLA---VNILGPRHDN 210
Cdd:pfam00148  78 IFVISTCLTETIGDDIEAVAREAREELGIPVIPVSTPGFVG-SHSTGYDVALEAIVRQLVGKKGEKEpgtVNILGGFNLG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  211 FAKS-ELAECLNTIGLPINLVLPSDCDITDIVKAPAARLNLV-TDRIGLPLAQAMLDRFGLPYIYFDRFV----TPRTIE 284
Cdd:pfam00148 157 PGDLrEIKRLLEKLGIEVNPVFTGGTTLEDLRAAGNAAANLVlCPFSGEYAAEMLEEKFGVPYIRLGAPIgleaTDRFLR 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  285 N--AYLDlfdkilKPETRQRMEEWlnsKKNAARRIAeRVTPKLQG-YSYIYGNTPLPqLELNAYLTELGLQPKLIQLSQW 361
Cdd:pfam00148 237 AlaKLFG------KEVAPEVIARE---RGRLLDAMV-DYHEYLAGkRVAIYGDPDLV-LGLARFLLELGMEPVAVGTGTG 305

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 667705087  362 TTADDTAVNRILAKYNPYVTRNANIAPLRDMYDILRPEFYFGHEY 406
Cdd:pfam00148 306 HPDDYERLKAELEEGDPEVIDGADLEELEELIKELKPDLLLGNSK 350
Oxidoreductase_nitrogenase cd00316
The nitrogenase enzyme system catalyzes the ATP-dependent reduction of dinitrogen to ammonia. ...
 54-413 2.25e-41

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: 151.66  E-value: 2.25e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  54 CPLFGSLMLIRRIRNASCLVVGTDECTYYAKSSAMAGGDFGTlaeRCYSLVLQPTDISFGSGDKLNAAIEEITAQGKPEL 133
Cdd:cd00316    7 CAPLGAARVALGIKDAIPLVHGPQGCAYFTRLTLRRHFKEPI---PLFTTSMTEKDVVFGGGEKLLEAIINELKRYKPKV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 134 LFVITTCVVELIGDDFDSLCARAAARLNIAVTVIHTEHYRSEnHLAGMEAALTA---CLPIMREQPPQLA--VNILGPRH 208
Cdd:cd00316   84 IFVYTTCTTELIGDDIEAVAKEASKEIGIPVVPASTPGFRGS-QSAGYDAAVKAiidHLVGTAEPEETEPgsVNLIGGYN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 209 DNFAK-SELAECLNTIGLPINLVLPSDCDITDIVKAPAARLNLVT-DRIGLPLAQAMLDRFGLPYIyfdrFVTPRTIEN- 285
Cdd:cd00316  163 LGGGDlRELKRLLEEMGIRVNALFDGGTTVEELRELGNAKLNLVLcRESGLYLARYLEEKYGIPYI----LINPIGLEAt 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 286 -AYLDLFDKILKPEtrQRMEEWLNSKKNAARRIAERVTPKLQGYS-YIYGNTPLPqLELNAYLTELGLQPKLIqLSQWTT 363
Cdd:cd00316  239 dAFLRKLAELFGIE--KEVPEVIARERARLLDALADYHEYLGGKKvAIFGDGDLL-LALARFLLELGMEVVAA-GTTFGH 314

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 667705087 364 ADDTAVNRILAKYNPYVTRNANIAPLRDMYDILRPEFYFGHEYFERLLKK 413
Cdd:cd00316  315 KADYERREELLGEGTEVVDDGDLEELEELIRELKPDLIIGGSKGRYIAKK 364
NifD/CfbD COG2710
Nitrogenase Mo-Fe protein NifD/coenzyme F430 biosynthesis subunit CfbD [Coenzyme transport and ...
 79-404 2.88e-31

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: 124.46  E-value: 2.88e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  79 CTYYAKSSAMAGGDFGTlaeRCYSLVLQPTDISFGSGDKLNAAIEEITAQGKPELLFVITTCVVELIGDDFDSLCARAAA 158
Cdd:COG2710   38 CAAYSRVTRGRHFKEPI---PLFSTDMTEDDVVFGGEKNLEEAIKNIIERYKPKLIFVYTTCLTETIGDDIEAVIKEARE 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 159 RLNIAVTVIHTEHYRSeNHLAGMEAALTACLPIM---REQPPQLAVNILGPrhdnFAKS-----ELAECLNTIGLPINlV 230
Cdd:COG2710  115 ELGIPVVPVSTPGFVG-SHSTGYHIAVEAIVEQLvgtGEPKTPGKINLIGG----YNLIpgdlwEIKRLLEEMGLRVI-A 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 231 LPSDCDIT--DIVKAPAARLNLV-TDRIGLPLAQAMLDRFGLPYIYFDRFVtprTIEN--AYLDLFDKILKPEtrqrMEE 305
Cdd:COG2710  189 LPDLGGTTveEIADAGRAKLNLVlCSRSGNYAARYLEEKYGIPYLEFVSPI---GLEAtdEFLRKLAELFGKP----VPE 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 306 WLNSKKNAARRIAERVTPKLQG-YSYIYGNTPLPqLELNAYLTELGLQPKLIqLSQWTTADDTA-VNRILAKYNPY-VTR 382
Cdd:COG2710  262 VIARERGRLVDALADYHFYLGGkKVAIYGDPDLL-WGLASFLLELGMEPVAA-VTTTGSPEDYErIKELLEELPEGtVID 339

                        330       340
                 ....*....|....*....|....*
gi 667705087 383 NANiapLRDMYDILR---PEFYFGH 404
Cdd:COG2710  340 DGD---LEELEELLKelkPDLLIGG 361
Nitrogenase_MoFe_alpha_like cd01967
Nitrogenase_MoFe_alpha_like: Nitrogenase MoFe protein, alpha subunit_like. The nitrogenase ...
 47-430 1.48e-26

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: 110.77  E-value: 1.48e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  47 AVFPGSHCPLFGslmlirrIRNASCLVVGTDECTYYAKSSAMAG--GDFGTLaERCYSLVLQPTDISFGSGDKLNAAIEE 124
Cdd:cd01967   10 CAFGGAGVVLGP-------IKDAVHIVHGPIGCAYYTWDTRRNLssGENLFY-KYGFSTDMQEKDIVFGGEKKLKKAIKE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 125 ITAQGKPELLFVITTCVVELIGDDFDSLCARAAARLNIAVTVIHTEHYRSENHLAGMEAALTACLPIM---REQPPQLA- 200
Cdd:cd01967   82 AYERFPPKAIFVYSTCPTGLIGDDIEAVAKEASKELGIPVIPVNCEGFRGVSQSLGHHIANDAILDHLvgtKEPEEKTPy 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 201 -VNILGPRhdNFAKS--ELAECLNTIGLPINLVLPSDCDITDIVKAPAARLNLV-TDRIGLPLAQAMLDRFGLPYIYFDr 276
Cdd:cd01967  162 dVNIIGEY--NIGGDawVIKPLLEELGIRVNATFTGDGTVDELRRAHRAKLNLVhCSRSMNYLAREMEERYGIPYMEVN- 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 277 FVTPRTIENAYLDLFDKILKPEtrqRMEEWLNSKKNAARRIAERVTPKLQG-YSYIYGNTPLPQLELNAYLtELGLQPkL 355
Cdd:cd01967  239 FYGFEDTSESLRKIAKFFGDEE---KAEEVIAEEEARIKPELEKYRERLKGkKVIIYTGGARSWHVIAALR-ELGMEV-V 313

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 667705087 356 IQLSQWTTADDTAVNRILAKYNPYVTRNANIAPLRDMYDILRPEFYF-GHEYFERLLKKGIVQRAM--DRLGQAYGFQ 430
Cdd:cd01967  314 AAGYEFGHDDDYERIRKILDEGTLLVDDYNDLELEELVEKLKPDLILsGIKEKYVAQKLGIPFLDLhsERNGPYAGYE 391
Nitrogenase_NifE_I cd01968
Nitrogenase_NifE_I: a subgroup of the NifE subunit of the NifEN complex: NifE forms an ...
 105-327 2.03e-22

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: 98.93  E-value: 2.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 105 LQPTDISFGSGDKLNAAIEEITAQGKPELLFVITTCVVELIGDDFDSLCARAAARLNIAVTVIHTEHYRSE----NHLAG 180
Cdd:cd01968   61 LSEKDVIFGGEKKLYKAILEIIERYHPKAVFVYSTCVVALIGDDIDAVCKTASEKFGIPVIPVHSPGFVGNknlgNKLAC 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 181 mEAALTacLPIMREQPPQLA---VNILGPRhdNFAKS--ELAECLNTIGLPINLVLPSDCDITDIVKAPAARLNLVT-DR 254
Cdd:cd01968  141 -EALLD--HVIGTEEPEPLTpydINLIGEF--NVAGElwGVKPLLEKLGIRVLASITGDSRVDEIRRAHRAKLNVVQcSK 215

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 667705087 255 IGLPLAQAMLDRFGLPYIYFDrFVTPRTIENAYLDLFDKILKPETRQRMEEWLNSKKNAARRIAERVTPKLQG 327
Cdd:cd01968  216 SMIYLARKMEEKYGIPYIEVS-FYGIRDTSKSLRNIAELLGDEELIERTEELIAREEARLRPELAPYRARLEG 287
Nitrogenase_VnfE_like cd01972
Nitrogenase_VnfE_like: VnfE subunit of the VnfEN complex_like. This group in addition to VnfE ...
 50-327 4.82e-22

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: 97.88  E-value: 4.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  50 PGSH---CPLFGSLMLIRRIRNASCLVVGTDECTYYAKSSAMAGGDF---GTLAERCYSLVLQPTDISFGSGDKLNAAIE 123
Cdd:cd01972    3 QFSQasmCKFWTAFCILSGIRDAVVVQHGPIGCAAGQSFFNRLYRCGemrRGLNEPVLSTNLTEKDVVFGGEKKLEDTIK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 124 EITAQGKPELLFVITTCVVELIGDDFDSLCARAAARLNIAVTVIHTEHYRSENHLAGMEAALTACLPIMreQPPQL---- 199
Cdd:cd01972   83 EAYSRYKPKAIFVATSCATGIIGDDVESVVEELEDEIGIPVVALHCEGFKGKHWRSGFDAAFHGILRHL--VPPQDptkq 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 200 --AVNILG-----PRHDNFAKSELAECLNTIGLPINLVLPSDCDITDIVKAPAARLN--LVTDrIGLPLAQAMLDRFGLP 270
Cdd:cd01972  161 edSVNIIGlwggpERTEQEDVDEFKRLLNELGLRVNAIIAGGCSVEELERASEAAANvtLCLD-LGYYLGAALEQRFGVP 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 667705087 271 YIyfdRFVTPRTIE--NAYLDLFDKILKPEtrQRMEEWLNSKKNAARRIAERVTPKLQG 327
Cdd:cd01972  240 EI---KAPQPYGIEatDKWLREIAKVLGME--AEAEAVIEREHERVAPEIEELRKALKG 293
nifE TIGR01283
nitrogenase molybdenum-iron cofactor biosynthesis protein NifE; This protein is part of the ...
 105-327 1.18e-20

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: 93.96  E-value: 1.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  105 LQPTDISFGSGDKLNAAIEEITAQGKPELLFVITTCVVELIGDDFDSLCARAAARLNIAVTVIHTEHYRSENHLaGMEAA 184
Cdd:TIGR01283  93 LTEKDVIFGGEKKLFHAIREIVERYHPPAVFVYSTCVPALIGDDLEAVCKAAAEKTGIPVIPVDSEGFYGTKNL-GNKLA 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  185 LTACL--------PIMREQPPQL-AVNILGprHDNFAKS--ELAECLNTIGLPINLVLPSDCDITDIVKAPAARLNLVT- 252
Cdd:TIGR01283 172 CDALLkhvigtrePEPLPVGITVhDINLIG--EFNVAGEfwHVLPLLEKLGIRVLATITGDSRYAEVQTAHRAKLNMVQc 249

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 667705087  253 DRIGLPLAQAMLDRFGLPYIYFDrFVTPRTIENAYLDLFDKILKPETRQRMEEWLNSKKNAARRIAERVTPKLQG 327
Cdd:TIGR01283 250 SKAMINLARKMEEKYGIPYFEGS-FYGIEDTSKALRDIADLFGDPELLKRTEELIAREEAKIRPALEPYRERLKG 323
Nitrogenase_VnfN_like cd01971
Nitrogenase_vnfN_like: VnfN subunit of the VnfEN complex-like. This group in addition to VnfN ...
 54-275 6.56e-18

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: 85.54  E-value: 6.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  54 CPLFGSLMLIRRIRNASCLV-----VGTDECTYYAKSSAMAGGDFGTLAercySLVLQPTDISFGSGDKLNAAIEEITAQ 128
Cdd:cd01971    9 CALGGALYTVSAIPRAVPIIhsgpgCASKQSGAVAFGNGYQGGGYGVAP----CTNATETEIVFGGEDRLRELIKSTLSI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 129 GKPELLFVITTCVVELIGDDFDSLCaRAAARLNIAVTVIHTEHYRSENhLAGMEAALTACLP-IMREQPPQLA--VNILG 205
Cdd:cd01971   85 IDADLFVVLTGCIAEIIGDDVGAVV-SEFQEGGAPIVYLETGGFKGNN-YAGHEIVLKAIIDqYVGQSEEKEPglVNLWG 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 667705087 206 --PRHDNFAKSELAE---CLNTIGLPINLVLPSDCDITDIVKAPAARLNLV-TDRIGLPLAQAMLDRFGLPYIYFD 275
Cdd:cd01971  163 pvPYQDPFWRGDLEEikrVLEGIGLKVNILFGPESNGEELRSIPKAQFNLVlSPWVGLEFAQHLEEKYGQPYIHSP 238
Nitrogenase_MoFe_beta_like cd01965
Nitrogenase_MoFe_beta_like: Nitrogenase MoFe protein, beta subunit_like. The nitrogenase ...
 112-424 4.60e-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: 83.00  E-value: 4.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 112 FGSGDKLNAAIEEITAQGKPELLFVITTCVVELIGDDFDSLCARAAARL----NIAVTVIHTEHYRSeNHLAGMEAALTA 187
Cdd:cd01965   63 FGGEDNLIEALKNLLSRYKPDVIGVLTTCLTETIGDDVAGFIKEFRAEGpepaDFPVVYASTPSFKG-SHETGYDNAVKA 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 188 ---CLPIMREQPPQLAVNILGPRH---DNFakSELAECLNTIGLPINLVL-PSDCD-----------------ITDIVKA 243
Cdd:cd01965  142 iieQLAKPSEVKKNGKVNLLPGFPltpGDV--REIKRILEAFGLEPIILPdLSDSLdghltdgyspltkggttLEEIRDA 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 244 PAARLNLV-TDRIGLPLAQAMLDRFGLPYIYFDrfvTPRTIENAylDLFDKIL-------KPE--TRQR---------ME 304
Cdd:cd01965  220 GNAKATIAlGEYSGRKAAKALEEKFGVPYILFP---TPIGLKAT--DEFLRALsklsgkpIPEelERERgrlldamldSH 294

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 305 EWLNSKKNAarriaervtpklqgysyIYGNtPLPQLELNAYLTELGLQPKLIQLsqwTTADDTAVNRILAKYNPYVtRNA 384
Cdd:cd01965  295 FYLGGKRVA-----------------IAGD-PDLLLGLSRFLLEMGAEPVAAVT---GTDNPPFEKRMELLASLEG-IPA 352

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 667705087 385 NIAPLRDMYDI------LRPEFYFGH---EYFERLLKKGIVQRAM---DRLG 424
Cdd:cd01965  353 EVVFVGDLWDLeslakeEPVDLLIGNshgRYLARDLGIPLVRVGFpifDRLG 404
Pchlide_reductase_B cd01981
Pchlide_reductase_B: B protein of the NB protein complex of Protochlorophyllide (Pchlide) ...
 104-272 1.33e-15

Pchlide_reductase_B: B protein of the NB protein complex of Protochlorophyllide (Pchlide)_reductase. Pchlide reductase catalyzes the reductive formation of chlorophyllide (chlide) from protochlorophyllide (pchlide) during biosynthesis of chlorophylls and bacteriochlorophylls. This group contains both the light-independent Pchlide reductase (DPOR) and light-dependent Pchlide reductase (LPOR). Angiosperms contain only LPOR, cyanobacteria, algae and gymnosperms contain both DPOR and LPOR, primitive anoxygenic photosynthetic bacteria contain only DPOR. NB is structurally similar to the FeMo protein of nitrogenase, forming an N2B2 heterotetramer. N and B are homologous to the FeMo alpha and beta subunits respectively. Also in common with nitrogenase in vitro DPOR activity requires ATP hydrolysis and dithoionite or ferredoxin as electron donor. The NB protein complex may serve as a catalytic site for Pchlide reduction similar to MoFe for nitrogen reduction.


Pssm-ID: 238939 [Multi-domain]  Cd Length: 430  Bit Score: 78.58  E-value: 1.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 104 VLQPTDISFGSGDKLNAAIEEITAQGKPELLFVITTCVVELIGDDFDSLCARAAARLNIAVTVIHTEHYRsENHLAGMEA 183
Cdd:cd01981   59 TVDRHVLARGSQEKVVENITRKDKEEKPDLIVLTPTCTSSILQEDLQNFVRAAGLSSKSPVLPLDVNHYR-VNELQAADE 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 184 ALTAclpIMR----EQPPQLA---------VNILGP-------RHDnfaKSELAECLNTIGLPINLVLPSDCDITDIVKA 243
Cdd:cd01981  138 TFEQ---LVRfyaeKARPQGTprektekpsVNLIGPsslgfhnRHD---CRELKRLLHTLGIEVNVVIPEGASVDDLNEL 211

                        170       180       190
                 ....*....|....*....|....*....|
gi 667705087 244 PAARLNLVTDR-IGLPLAQAMLDRFGLPYI 272
Cdd:cd01981  212 PKAWFNIVPYReYGLSAALYLEEEFGMPSV 241
Nitrogenase_MoFe_alpha cd01976
Nitrogenase_MoFe_alpha_II: Nitrogenase MoFe protein, beta subunit. A group of proteins similar ...
 79-327 5.12e-15

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: 76.61  E-value: 5.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  79 CTYYA------KSSAMAGGD-FGTLaerCYSLVLQPTDISFGSGDKLNAAIEEItaqgkpELLF-------VITTCVVEL 144
Cdd:cd01976   43 CGQYSwatrrnYYRGETGVDnFGTM---QFTTDFQEKDIVFGGDKKLAKAIDEA------YELFplnkgisVQSECPVGL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 145 IGDDFDSLCARAAARLNIAVTVIHTEHYRSENHLAGMEAALTACLPIM------REQPPqLAVNILGPRH---DNFAKSE 215
Cdd:cd01976  114 IGDDIEAVARKASKELGIPVVPVRCEGFRGVSQSLGHHIANDAIRDHIlgkrneFEPTP-YDVNIIGDYNiggDAWASRI 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 216 LaecLNTIGLPINLVLPSDCDITDIVKAPAARLNLV-TDRIGLPLAQAMLDRFGLPYIYFDrFVTPRTIENAYLDL---F 291
Cdd:cd01976  193 L---LEEMGLRVVAQWSGDGTLNEMENAHKAKLNLIhCYRSMNYIARMMEEKYGIPWMEYN-FFGPTKIAESLRKIaayF 268

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 667705087 292 DkilkPETRQRMEEWLNSKKNAARRIAERVTPKLQG 327
Cdd:cd01976  269 D----DEITAKTEEVIAEYKPAMEAVIAKYRPRLEG 300
PRK02910 PRK02910
ferredoxin:protochlorophyllide reductase (ATP-dependent) subunit B;
101-273 3.62e-13

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


Pssm-ID: 235085 [Multi-domain]  Cd Length: 519  Bit Score: 71.45  E-value: 3.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 101 YSlVLQPTDISFGSGDKLNAAIEEITAQGKPELLFVITTCVVELIGDDFDSLcaraAARLNIAVTVIHTE--HYR-SENH 177
Cdd:PRK02910  57 YS-TVQARDLARGTAELLKDTLRRADERFQPDLIVVGPSCTAELLQEDLGGL----AKHAGLPIPVLPLElnAYRvKENW 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 178 laGMEAALT------ACLPIMREQP--PQLAVNILGP-------RHDnfaKSELAECLNTIGLPINLVLPSDCDITDIVK 242
Cdd:PRK02910 132 --AADETFYqlvralAKKAAELPQPktARPSVNLLGPtalgfhhRDD---LTELRRLLATLGIDVNVVAPLGASPADLKR 206

                        170       180       190
                 ....*....|....*....|....*....|..
gi 667705087 243 APAARLNLVTDR-IGLPLAQAMLDRFGLPYIY 273
Cdd:PRK02910 207 LPAAWFNVVLYReIGESAARYLEREFGQPYVK 238
PRK14477 PRK14477
bifunctional nitrogenase molybdenum-cofactor biosynthesis protein NifE/NifN; Provisional
 109-327 2.47e-12

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


Pssm-ID: 172952 [Multi-domain]  Cd Length: 917  Bit Score: 69.38  E-value: 2.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 109 DISFGSGDKLNAAIEEITAQGKPELLFVITTCVVELIGDDFDSLCARAAARLNIAVTVIHTEHYRSE----NHLAGmEAA 184
Cdd:PRK14477  91 DVIFGGEKKLYRAILELAERYQPKAVFVYATCVTALTGDDVEAVCKAAAEKVGIPVIPVNTPGFIGDknigNRLAG-EAL 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 185 LTACLPIMreQPPQLA---VNILGPRhdNFAkSELAECL---NTIGLPINLVLPSDCDITDIVKAPAARLNLVTDRIGLP 258
Cdd:PRK14477 170 LKHVIGTA--EPEVTTpydINLIGEY--NIA-GDLWGMLplfDRLGIRVLSCISGDAKFEELRYAHRAKLNVIICSKSLT 244

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 667705087 259 -LAQAMLDRFGLPYI---YFDRFVTPRTIENAYLDLFDKILKPETR---QRMEEWLNSKKNAARRIAERVTPKLQG 327
Cdd:PRK14477 245 nLARKMEKRYGIPYLeesFYGMTDTAKALRDIARELDDAGGGLEKRvlqDRVEKLIAEEEAKCRAALAPYRARLEG 320
chlB CHL00076
photochlorophyllide reductase subunit B
 113-272 9.33e-10

photochlorophyllide reductase subunit B


Pssm-ID: 214355 [Multi-domain]  Cd Length: 513  Bit Score: 60.42  E-value: 9.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 113 GSGDKLnaaIEEITAQGK---PELLFVITTCVVELIGDDFDSLCARAAARLNIAVTVIHTEHYRSeNHLAGMEAAL---- 185
Cdd:CHL00076  68 GSQEKV---VDNITRKDKeerPDLIVLTPTCTSSILQEDLQNFVDRASIESDSDVILADVNHYRV-NELQAADRTLeqiv 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 186 ---------TACLPIMREQPPqlAVNILG-------PRHDNfakSELAECLNTIGLPINLVLPSDCDITDIVKAPAARLN 249
Cdd:CHL00076 144 rfylekarkQGTLDQSKTDKP--SVNIIGiftlgfhNQHDC---RELKRLLQDLGIEINQIIPEGGSVEDLKNLPKAWFN 218

                        170       180
                 ....*....|....*....|....
gi 667705087 250 LVTDR-IGLPLAQAMLDRFGLPYI 272
Cdd:CHL00076 219 IVPYReVGLMTAKYLEKEFGMPYI 242
Pchlide_reductase_N cd01979
Pchlide_reductase_N: N protein of the NB protein complex of Protochlorophyllide (Pchlide) ...
 54-233 5.63e-09

Pchlide_reductase_N: N protein of the NB protein complex of Protochlorophyllide (Pchlide)_reductase. Pchlide reductase catalyzes the reductive formation of chlorophyllide (chlide) from protochlorophyllide (pchlide) during biosynthesis of chlorophylls and bacteriochlorophylls. This group contains both the light-independent Pchlide reductase (DPOR) and light-dependent Pchlide reductase (LPOR). Angiosperms contain only LPOR, cyanobacteria, algae and gymnosperms contain both DPOR and LPOR, primitive anoxygenic photosynthetic bacteria contain only DPOR. NB is structurally similar to the FeMo protein of nitrogenase, forming an N2B2 heterotetramer. N and B are homologous to the FeMo alpha and beta subunits respectively. Also in common with nitrogenase in vitro DPOR activity requires ATP hydrolysis and dithoionite or ferredoxin as electron donor. The NB protein complex may serve as a catalytic site for Pchlide reduction similar to MoFe for nitrogen reduction.


Pssm-ID: 238937 [Multi-domain]  Cd Length: 396  Bit Score: 57.76  E-value: 5.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  54 CPLFGSLMLIRRIRNASCLVVGTDECTYYAKSSAmaggDFGTLAERCYSL-VLQPTDISFGSGD--KLNAAIEEITAQGK 130
Cdd:cd01979   12 CGLACVAWLYQKIEDSFFLVVGTKTCAHFLQNAL----GVMIFAEPRFAMaELEEGDLSALLNDyaELDRVVTQIKRDRN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 131 PELLFVITTCVVELIGDDFDSLCARAAARLNIAVTVihtehYRSE----NHLAGMEAALTACLPIMREQP-PQLAVNILG 205
Cdd:cd01979   88 PSVIFLIGSCTTEVIKMDLEGAAPRLSAEIGVPILV-----ASASgldyTFTQGEDTVLAALVPRCPEKPsPERSLVLVG 162

                        170       180
                 ....*....|....*....|....*...
gi 667705087 206 PRHDNFAkSELAECLNTIGLPINLVLPS 233
Cdd:cd01979  163 SLPDIVE-DQLRRELEQLGIPVVGFLPP 189
Chlide_reductase_Z cd01982
Chlide_reductase_Z : Z subunit of chlorophyllide (chlide) reductase (BchZ). Chlide reductase ...
 190-273 1.50e-04

Chlide_reductase_Z : Z subunit of chlorophyllide (chlide) reductase (BchZ). Chlide reductase participates in photosynthetic pigment synthesis playing a role in the conversion of chlorophylls(Chl) into bacteriochlorophylls (BChl). Chlide reductase catalyzes the reduction of the B-ring of the tetrapyrolle. Chlide reductase is a three subunit enzyme (subunits are designated BchX, BchY and BchZ). The similarity between these three subunits and the subunits for nitrogenase suggests that BchX serves as an electron donor for the BchY-BchY catalytic subunits.


Pssm-ID: 238940 [Multi-domain]  Cd Length: 412  Bit Score: 44.06  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 190 PIMREQPPQLAVNILGPRHDNF-AKSELAEC---LNTIGLPINLVLPSDCDITDIVKAPAARLNLVTDR-IGLPLAQAMl 264
Cdd:cd01982  147 PKPFVQGRKGTVNIIGPSYGCFnSPSDLAEVkrlVTGIGAEVNHVYPFESHLAEIPKLKNAAVNVVMYReFGRGLAEDL- 225


                 ....*....
gi 667705087 265 drfGLPYIY 273
Cdd:cd01982  226 ---GRPYLY 231
PRK02842 PRK02842
ferredoxin:protochlorophyllide reductase (ATP-dependent) subunit N;
46-197 2.54e-04

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


Pssm-ID: 235076  Cd Length: 427  Bit Score: 43.36  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  46 HAVFpgshCPLFGSLMLIRRIRNASCLVVGTDECTYYAKSSA--M--AGGDFGTlaercysLVLQPTDISfGSGD---KL 118
Cdd:PRK02842  17 RHVF----CGLTSVVWLHRKIQDAFFLVVGSRTCAHLLQSAAgvMifAEPRFGT-------AILEEGDLA-GLADaneEL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 119 NAAIEE-ITAQGKPELLFVITTCVVELIGDDFdslcARAAARLNIAVTVIHTEHYRSE----NHLAGMEAALTACLPIMR 193
Cdd:PRK02842  85 DRVVEElIKRRPNISVLFLVGSCPSEVIKLDL----EGLAERLSTEFAGVPVLNYSGSgletTFTQGEDAVLAALVPFCP 160


                 ....
gi 667705087 194 EQPP 197
Cdd:PRK02842 161 EAPA 164
PRK14477 PRK14477
bifunctional nitrogenase molybdenum-cofactor biosynthesis protein NifE/NifN; Provisional
 37-278 4.80e-04

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


Pssm-ID: 172952 [Multi-domain]  Cd Length: 917  Bit Score: 42.81  E-value: 4.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  37 SLEDIQPLSHAVFPGSHCPLFGSLMLIRRIRNASCLVVGTDECTYYAKssamaggdfgTLAERCY--SLVLQPTDIS--- 111
Cdd:PRK14477 481 SRVKVPTKAATVNPQKNSPALGATLAYLGIDGMLPLLHGAQGCSTFIR----------LQLSRHFkeSIALNTTAMSevt 550

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 112 --FGSGDKLNAAIEEITAQGKPELLFVITTCVVELIGDDFDSLCA--RAAARLNIAVTVIH--TEHYR---SENHLAGME 182
Cdd:PRK14477 551 aiFGGWENLKQGILRVIEKFKPKVIGVMTTGLTETMGDDVRSAIVqfREEHPELDDVPVVWasTPDYCgslQEGYAAAVE 630

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087 183 AALTAcLPIMREQ-PPQlaVNILGPRHDNFAK-SELAECLNTIGLpINLVLPS-----DCDITDIVKA-----------P 244
Cdd:PRK14477 631 AIVAT-LPEPGERiPGQ--VNILPGAHLTPADvEEIKEIVEAFGL-DPVVVPDisnalDGHIDETVSPlstggttvediR 706

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 667705087 245 AARLNLVTDRIGLPLAQA---MLDRFGLPYIYF---------DRFV 278
Cdd:PRK14477 707 AAGRSAATLAVGDSLARAaekLQERFGIPAYGFtsltglkevDRFM 752
Nitrogenase_MoFe_beta cd01974
Nitrogenase_MoFe_beta: Nitrogenase MoFe protein, beta subunit. The nitrogenase enzyme ...
 112-151 1.06e-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: 41.11  E-value: 1.06e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 667705087 112 FGSGDKLNAAIEEITAQGKPELLFVITTCVVELIGDDFDS 151
Cdd:cd01974   67 FGGQNNLIDGLKNAYAVYKPDMIAVSTTCMAEVIGDDLNA 106
nifN TIGR01285
nitrogenase molybdenum-iron cofactor biosynthesis protein NifN; This protein forms a complex ...
 38-278 1.63e-03

nitrogenase molybdenum-iron cofactor biosynthesis protein NifN; This protein forms a complex with NifE, and appears as a NifEN in some species. NifEN is a required for producing the molybdenum-iron cofactor of molybdenum-requiring nitrogenases. NifN is closely related to the nitrogenase molybdenum-iron protein beta chain NifK. This model describes most examples of NifN but excludes some cases, such as the putative NifN of Chlorobium tepidum, for which a separate model may be created. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Central intermediary metabolism, Nitrogen fixation]


Pssm-ID: 273537 [Multi-domain]  Cd Length: 432  Bit Score: 40.52  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087   38 LEDIQPLSHavfpGSH-CPLFGSLMLIRRIRNASCLvvgtdectyyaKSSAMaggdfgtlaercyslvlQPTDISFGSGD 116
Cdd:TIGR01285  30 IEGAIPLFH----GAQgCTAFAKVFFVRHFREPIPL-----------QTTAM-----------------DEVSTILGGDE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  117 KLNAAIEEITAQGKPELLFVITTCVVELIGDDFDSLCARAAAR----LNIAVTVIHTEHYR---SENHLAGMEAALTACL 189
Cdd:TIGR01285  78 HIEEAIDTLCQRNKPKAIGLLSTGLTETRGEDIARVVRQFREKhpqhKGTAVVTVNTPDFKgslEDGYAAAVESIIEAWV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  190 PIMREQPPQLA-VNILGPRHDNFAK-SELAECLNTIGL-PInlVLP----------SDCD----------ITDIVKAPAA 246
Cdd:TIGR01285 158 PPAPARAQRNRrVNLLVGSLLTPGDiEELRRMVEAFGLkPI--ILPdlsrsldghlADDDfspitqggttLEQIRQIGQS 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 667705087  247 RLNLVTDRIGLPLAQAMLDRFGLPYIYF---------DRFV 278
Cdd:TIGR01285 236 CCTLAIGESMRRAASLLADRCGVPYIVFpslmgleavDAFL 276
Nitrogenase_NifN_2 cd03466
Nitrogenase_nifN_2: A subgroup of the NifN subunit of the NifEN complex: NifN forms an ...
 50-148 2.11e-03

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: 40.45  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  50 PGSHCPLFGSLMLIRRIRNASCLVVGTDECTYYAKSSaMAggdfgtlaeRCYSlvlQPTDIS----------FGSGDKLN 119
Cdd:cd03466    7 PCKICMPMGASMAFKGIEGCMPLLHGSQGCSTYIRRH-MA---------RHYN---EPVDIAssslneettvYGGEKNLK 73

                         90       100
                 ....*....|....*....|....*....
gi 667705087 120 AAIEEITAQGKPELLFVITTCVVELIGDD 148
Cdd:cd03466   74 KGLKNVIEQYNPEVIGIATTCLSETIGED 102
Chlide_reductase_Y cd01980
Chlide_reductase_Y : Y subunit of chlorophyllide (chlide) reductase (BchY). Chlide reductase ...
 50-146 4.23e-03

Chlide_reductase_Y : Y subunit of chlorophyllide (chlide) reductase (BchY). Chlide reductase participates in photosynthetic pigment synthesis playing a role in the conversion of chlorophylls(Chl) into bacteriochlorophylls (BChl). Chlide reductase catalyzes the reduction of the B-ring of the tetrapyrolle. Chlide reductase is a three subunit enzyme (subunits are designated BchX, BchY and BchZ). The similarity between these three subunits and the subunits for nitrogenase suggests that BchX serves as an electron donor for the BchY-BchY catalytic subunits.


Pssm-ID: 238938 [Multi-domain]  Cd Length: 416  Bit Score: 39.46  E-value: 4.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667705087  50 PGSHCPLFGSLMLIRRIRNASCLVVGTDECTY--------YAKSSAMAGGDFGTlaercyslvlqpTDISFGS-GDKLNA 120
Cdd:cd01980   14 PQTMCPAFGSLRVLTRIEGAATVLVGDAGCLYgltfvshfYAARRSIVAVPLSS------------ETLSTGKlFEDIRE 81

                         90       100
                 ....*....|....*....|....*.
gi 667705087 121 AIEEITAQGKPELLFVITTCVVELIG 146
Cdd:cd01980   82 AIRKLADPPAYTFIPVISLCVAETAG 107
Nitrogenase_VFe_alpha cd01977
Nitrogenase_VFe_alpha -like: Nitrogenase VFe protein, alpha subunit like. This group contains ...
 101-160 8.33e-03

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: 38.58  E-value: 8.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 667705087 101 YSLVLQPTDISFGSGDKLNAAIEEiTAQGKPEL--LFVITTCVVELIGDDFDSLCARAAARL 160
Cdd:cd01977   58 WSTDMKESHVVFGGEKKLKKNIIE-AFKEFPDIkrMTVYTTCTTALIGDDIKAVAKEVMEEL 118
 
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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