|
Name |
Accession |
Description |
Interval |
E-value |
| 8prop_hemeD1_NirS |
cd20779 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirS; ... |
60-506 |
0e+00 |
|
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirS; Cytochrome cd1 nitrite reductase NiR is a key denitrification enzyme that catalyzes the conversion of nitrite to nitric oxide in the nitrogen cycle. The crystal structure of the oxidized enzyme shows that the d1 heme iron of the active site is ligated by His/Tyr side chains, and the c heme iron is ligated by a His/His ligand pair. Nitrite reductase from Pseudomonas aeruginosa is a dimer of two identical subunits of 60 kDa, each containing one c and one d1 heme group. The c heme is the electron accepting pole of the molecule and is reduced in vitro by either azurin or cytochrome c551. The d1 heme is the site where nitrite, and oxygen reduction occur. The two types of heme are located in separate domains whose arrangement suggests a mechanism requiring domain movement during catalysis.
Pssm-ID: 467723 [Multi-domain] Cd Length: 438 Bit Score: 785.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 60 NWGTSNALTKAQITSMATFIQHTAPTPPEWGMAETLKTWKVLVKPADRPKKQLNMLNLENLFSVTLRDDGKIALVDGDTK 139
Cdd:cd20779 1 AWGKSGILTEEEIDLMARYLQLPPPAPPEFGMADMKASWKVIVPVAKRPTKPEHKRNWENFFGVILRDAGQVAIIDGDTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 140 QIVKLIDTGYAVHISRISASGRYLLVIGRDAKIDMIDLWPAEPTKVAEIKVGIEARSVETSKFKGYEDTYAIAGSYWPPQ 219
Cdd:cd20779 81 EIVSIVDTGFAVHILRSSASGRYFYTIGRDGKVTMIDLWMKKPTVVAEVKGCLDARSVDSSKYKGFEDKYAIVGCYWPPQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 220 FTIMDGETLEPKQIVSTRGMTVDKQEYHPEPRVAAIIASHEWPEFIVNIKETGKVMLVNYQDIKNLTITTIDAAPFLHDG 299
Cdd:cd20779 161 YVILDGLTLEPLKVVSTRGYTYDTGEYHPEPRVASIVASHFDPEWVVNVKETGQVWLVDYSDLKNLKVTMIEAERFLHDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 300 GWDSTHRYFMTAANNSNKVAVIDSRERKLTALVDVGKTPHPGRGANFIHPTYGPVWATSHLGDGGISVIGTDPVKHAQYA 379
Cdd:cd20779 241 GWDHTKRYFLVAANARNKVVVVDTKTKKLVALVETGIKPHPGRGANWVDPKYGPVWATGHLGEGKIALIGTDPKGHPQYA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 380 WKQVESLKGQGGGSLFIKTHPNSHHLYVDTTLNPDTKLSQSVAVFDINQLDKGYSVLPIAEYSgikqgalRVVQPEYNKA 459
Cdd:cd20779 321 WKVVRKIKLPGGGSLFIKTHPKSPWLWVDRTLNPDPKLARSVCVFDKKLLDKKYKCWPVADHG-------RAVHFEYNKA 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2096819685 460 GDEVWFSVWNGqtEESALVVIDDKTLKLKQVIRDKRLITPTGKFNVY 506
Cdd:cd20779 394 GDEVWVSVWDK--KPGAIVVYDDKTLKEKARITGDWLVTPTGKFNVY 438
|
|
| Cytochrom_D1 |
pfam02239 |
Cytochrome D1 heme domain; Cytochrome cd1 (nitrite reductase) catalyzes the conversion of ... |
115-508 |
0e+00 |
|
Cytochrome D1 heme domain; Cytochrome cd1 (nitrite reductase) catalyzes the conversion of nitrite to nitric oxide in the nitrogen cycle. This family represents the d1 heme binding domain of cytochrome cd1, in which His/Tyr side chains ligate the d1 heme iron of the active site in the oxidized state.
Pssm-ID: 366994 [Multi-domain] Cd Length: 368 Bit Score: 524.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 115 LNLENLFSVTLRDDGKIALVDGDTKQIVKLIDTGYAVHISRISAS-GRYLLVIGRDAKIDMIDLWpaEPTKVAEIKVGIE 193
Cdd:pfam02239 1 RDLGNLFVVTERDAGSVALLDGDRKEILARVDTGYALHISRMFSSdGRYVYVIGRDGGLTKIDLW--NQEIVAEVRQGGN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 194 ARSVETSkfkgYEDTYAIAGSYWPPQFTIMDGETLEPKQIVSTRGMTVDKqeyhPEPRVAAIIASHEWPEFIVNIKETGK 273
Cdd:pfam02239 79 ARSVATS----YDGRYVIVGNYWPGQYVIMDGRTLELVKVIPARGMTGDS----PESRVAAIVASPGRPEFVVNLKDTGE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 274 VMLVNYQDIKNLTITTIDAAPFLHDGGWDSTHRYFMTAANNSNKVAVIDSRERKLTALVDVGKTPHPGRGANFIHPTYGP 353
Cdd:pfam02239 151 IWLVDYSDGKNLKTTFIEAAKFLHDGGFDPDGRYFMAAANASDKIAVWDTKRGKLVALLDYGKTPHPGPGANMPHLEGGP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 354 VWATSHLGDGGISVIGTDPV-KHAQYAWKQVESLKGQGGGsLFIKTHPNSHHLYVDTTLNPDtklSQSVAVFDINQLDKg 432
Cdd:pfam02239 231 VWTTSHLGDFVTPLIGTDPVlVHDLQAWKQVKEIDVAGGG-LFVKTHPDSRYLWVDTFLNPD---NDSVAVIDSETLEK- 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2096819685 433 ysVLPIAEYSGIKqgalrVVQPEYNKAGDEVWFSVWNGqteESALVVIDDKTLKLKQVIrdkRLITPTGKFNVYNT 508
Cdd:pfam02239 306 --VLTLAPWPGLV-----VVHMEFNKRGDEVWLSVWDG---KGALVVYDDKTLKLKKVI---PLNTPSGKFNVYNT 368
|
|
| CccA |
COG2010 |
Cytochrome c, mono- and diheme variants [Energy production and conversion]; |
2-85 |
4.90e-15 |
|
Cytochrome c, mono- and diheme variants [Energy production and conversion];
Pssm-ID: 441613 [Multi-domain] Cd Length: 169 Bit Score: 73.06 E-value: 4.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 2 SQADFDTSKQIYFERCAGCHGVLRKGATGK--PLTPDITQARGQAYLEALITYGSPAG-MPNWGtsNALTKAQITSMATF 78
Cdd:COG2010 85 DAEALARGKALYEQNCAACHGADGKGGLGAapNLTDDALYGGDPEALVETILNGRPGGaMPAFG--GQLSDEEIAALAAY 162
|
....*..
gi 2096819685 79 IQHTAPT 85
Cdd:COG2010 163 LRSLSGN 169
|
|
| Cytochrome_CBB3 |
pfam13442 |
Cytochrome C oxidase, cbb3-type, subunit III; |
4-79 |
2.05e-08 |
|
Cytochrome C oxidase, cbb3-type, subunit III;
Pssm-ID: 463879 [Multi-domain] Cd Length: 67 Bit Score: 50.87 E-value: 2.05e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2096819685 4 ADFDTSKQIYFERCAGCHGvlrKGATGKPLTPDitqARGQAYLEALITYGsPAGMPNWGTSnaLTKAQITSMATFI 79
Cdd:pfam13442 1 AAAAAGEALYAANCASCHG---TGGAGPSLAGR---ALPPEALVDIIRNG-KGAMPAFGGD--LSDEELEALAAYL 67
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
287-426 |
3.07e-05 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 45.46 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 287 ITTIDAAPFLHDGGWDSTHRYFMTAANNSNKVAVIDSRERKLTALVDVGKTPHpgrgANFIHPTYGPVWATSHlGDGGIS 366
Cdd:COG3391 103 VATIPVGGGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIPVGAGPH----GIAVDPDGKRLYVANS-GSNTVS 177
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2096819685 367 VIGT--DPVkhaqyAWKQVESLKGqGGGSLFIKTHPNSHHLYVDTTLNPDT-KLSQSVAVFDI 426
Cdd:COG3391 178 VIVSviDTA-----TGKVVATIPV-GGGPVGVAVSPDGRRLYVANRGSNTSnGGSNTVSVIDL 234
|
|
| ccoP |
TIGR00782 |
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of ... |
7-80 |
1.52e-03 |
|
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of approximately 26 kDa of the cbb3 type copper and heme-containing cytochrome oxidase. [Energy metabolism, Electron transport]
Pssm-ID: 129864 [Multi-domain] Cd Length: 285 Bit Score: 40.65 E-value: 1.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2096819685 7 DTSKQIYFERCAGCHGVLRKG--ATGKP-LTPDITQARG-QAYLEALITYGSPAGMPNWGTSnaLTKAQITSMATFIQ 80
Cdd:TIGR00782 204 AKGQELFADNCTTCHGEDGKGlqELGAPnLTDDVWLYGGdLKTITTTITNGRGGVMPAWGPR--LSEAQIKALAAYVH 279
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| 8prop_hemeD1_NirS |
cd20779 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirS; ... |
60-506 |
0e+00 |
|
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirS; Cytochrome cd1 nitrite reductase NiR is a key denitrification enzyme that catalyzes the conversion of nitrite to nitric oxide in the nitrogen cycle. The crystal structure of the oxidized enzyme shows that the d1 heme iron of the active site is ligated by His/Tyr side chains, and the c heme iron is ligated by a His/His ligand pair. Nitrite reductase from Pseudomonas aeruginosa is a dimer of two identical subunits of 60 kDa, each containing one c and one d1 heme group. The c heme is the electron accepting pole of the molecule and is reduced in vitro by either azurin or cytochrome c551. The d1 heme is the site where nitrite, and oxygen reduction occur. The two types of heme are located in separate domains whose arrangement suggests a mechanism requiring domain movement during catalysis.
Pssm-ID: 467723 [Multi-domain] Cd Length: 438 Bit Score: 785.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 60 NWGTSNALTKAQITSMATFIQHTAPTPPEWGMAETLKTWKVLVKPADRPKKQLNMLNLENLFSVTLRDDGKIALVDGDTK 139
Cdd:cd20779 1 AWGKSGILTEEEIDLMARYLQLPPPAPPEFGMADMKASWKVIVPVAKRPTKPEHKRNWENFFGVILRDAGQVAIIDGDTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 140 QIVKLIDTGYAVHISRISASGRYLLVIGRDAKIDMIDLWPAEPTKVAEIKVGIEARSVETSKFKGYEDTYAIAGSYWPPQ 219
Cdd:cd20779 81 EIVSIVDTGFAVHILRSSASGRYFYTIGRDGKVTMIDLWMKKPTVVAEVKGCLDARSVDSSKYKGFEDKYAIVGCYWPPQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 220 FTIMDGETLEPKQIVSTRGMTVDKQEYHPEPRVAAIIASHEWPEFIVNIKETGKVMLVNYQDIKNLTITTIDAAPFLHDG 299
Cdd:cd20779 161 YVILDGLTLEPLKVVSTRGYTYDTGEYHPEPRVASIVASHFDPEWVVNVKETGQVWLVDYSDLKNLKVTMIEAERFLHDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 300 GWDSTHRYFMTAANNSNKVAVIDSRERKLTALVDVGKTPHPGRGANFIHPTYGPVWATSHLGDGGISVIGTDPVKHAQYA 379
Cdd:cd20779 241 GWDHTKRYFLVAANARNKVVVVDTKTKKLVALVETGIKPHPGRGANWVDPKYGPVWATGHLGEGKIALIGTDPKGHPQYA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 380 WKQVESLKGQGGGSLFIKTHPNSHHLYVDTTLNPDTKLSQSVAVFDINQLDKGYSVLPIAEYSgikqgalRVVQPEYNKA 459
Cdd:cd20779 321 WKVVRKIKLPGGGSLFIKTHPKSPWLWVDRTLNPDPKLARSVCVFDKKLLDKKYKCWPVADHG-------RAVHFEYNKA 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2096819685 460 GDEVWFSVWNGqtEESALVVIDDKTLKLKQVIRDKRLITPTGKFNVY 506
Cdd:cd20779 394 GDEVWVSVWDK--KPGAIVVYDDKTLKEKARITGDWLVTPTGKFNVY 438
|
|
| Cytochrom_D1 |
pfam02239 |
Cytochrome D1 heme domain; Cytochrome cd1 (nitrite reductase) catalyzes the conversion of ... |
115-508 |
0e+00 |
|
Cytochrome D1 heme domain; Cytochrome cd1 (nitrite reductase) catalyzes the conversion of nitrite to nitric oxide in the nitrogen cycle. This family represents the d1 heme binding domain of cytochrome cd1, in which His/Tyr side chains ligate the d1 heme iron of the active site in the oxidized state.
Pssm-ID: 366994 [Multi-domain] Cd Length: 368 Bit Score: 524.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 115 LNLENLFSVTLRDDGKIALVDGDTKQIVKLIDTGYAVHISRISAS-GRYLLVIGRDAKIDMIDLWpaEPTKVAEIKVGIE 193
Cdd:pfam02239 1 RDLGNLFVVTERDAGSVALLDGDRKEILARVDTGYALHISRMFSSdGRYVYVIGRDGGLTKIDLW--NQEIVAEVRQGGN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 194 ARSVETSkfkgYEDTYAIAGSYWPPQFTIMDGETLEPKQIVSTRGMTVDKqeyhPEPRVAAIIASHEWPEFIVNIKETGK 273
Cdd:pfam02239 79 ARSVATS----YDGRYVIVGNYWPGQYVIMDGRTLELVKVIPARGMTGDS----PESRVAAIVASPGRPEFVVNLKDTGE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 274 VMLVNYQDIKNLTITTIDAAPFLHDGGWDSTHRYFMTAANNSNKVAVIDSRERKLTALVDVGKTPHPGRGANFIHPTYGP 353
Cdd:pfam02239 151 IWLVDYSDGKNLKTTFIEAAKFLHDGGFDPDGRYFMAAANASDKIAVWDTKRGKLVALLDYGKTPHPGPGANMPHLEGGP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 354 VWATSHLGDGGISVIGTDPV-KHAQYAWKQVESLKGQGGGsLFIKTHPNSHHLYVDTTLNPDtklSQSVAVFDINQLDKg 432
Cdd:pfam02239 231 VWTTSHLGDFVTPLIGTDPVlVHDLQAWKQVKEIDVAGGG-LFVKTHPDSRYLWVDTFLNPD---NDSVAVIDSETLEK- 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2096819685 433 ysVLPIAEYSGIKqgalrVVQPEYNKAGDEVWFSVWNGqteESALVVIDDKTLKLKQVIrdkRLITPTGKFNVYNT 508
Cdd:pfam02239 306 --VLTLAPWPGLV-----VVHMEFNKRGDEVWLSVWDG---KGALVVYDDKTLKLKKVI---PLNTPSGKFNVYNT 368
|
|
| 8prop_hemeD1_NiR_alpha_gamma |
cd20781 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NiR ... |
80-512 |
5.41e-153 |
|
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NiR alpha and gamma proteobacteria subdivisions; Cytochrome cd1 (nitrite reductase) catalyzes in vitro the reduction of molecular oxygen to water and the reduction of nitrite to nitric oxide. Purification and characterization of NiR from several bacterial sources have shown that there are two distinct classes of dissimilatory NiRs that yield NO as the main reaction product, containing either copper or heme as cofactor, the heme-containing enzyme occurring more frequently. It forms a homodimer each containing one C and one D1 heme group. The C heme is the electron accepting pole of the molecule and is reduced in vitro by either azurin or cytochrome c551. The D1 heme is the site where nitrite, and oxygen reduction occur. NiR is a key denitrification enzyme, which controls the rate of the production of toxic nitric oxide (NO) and ultimately regulates the release of NO into the atmosphere. The two types of heme are located in separate domains whose arrangement suggests a mechanism requiring domain movement during catalysis. Heme binding nitrite reductase from alphaproteobacteria and gammaproteobacteria are present here.
Pssm-ID: 467725 [Multi-domain] Cd Length: 433 Bit Score: 443.76 E-value: 5.41e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 80 QHTAPTPPEWGMAETLKTWKVLVKPADRPKKQLNMLNLENLFSVTLRDDGKIALVDGDTKQIVKLIDTGYAVHISRISAS 159
Cdd:cd20781 1 QMEPPVPPEMSLALMKERHKVYVEPKDYPTKPLHGRNWENFFVVIERDAGKVAIIDGDKKEVVAHIDTGYAVHVLKASEH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 160 ---------GRYLLVIGRDAKIDMIDLWPA-EPTKVAEIKVGIEARSVETSkfkgYEDTYAIAGSYWPPQFTIMDGETLE 229
Cdd:cd20781 81 hkvekaknpGRFWYTMGRDGKLTKIDLWQTpDKMLVAEVQIAYDARDVAVS----GDGKYVIGGGYWPPHFVIVDAETME 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 230 PKQIVSTRGMTVDKqEYHPEPRVAAIIASHEWPEFIVNIKETGKVMLVNYQDIKNLTITTIDAAPFLHDGGWDSTHRYFM 309
Cdd:cd20781 157 PLKVVSTRGVNVDG-EYVNESRVAAIYTTPNAPTFLVAVKELGQMWQVDYSDLDNLRIDQIDTAKFLHDGFFDPTGRYFQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 310 TAANNSNKVAVIDSRERKLTALVDVGKTPHPGRGANFIHPTYGPVWATSHLGDGGISVIGTDPVKHAQYAWKQVESLKGQ 389
Cdd:cd20781 236 IAANASNKMVVVDTKTRKLEAMIDTGKLPHPGPGANWIDPKCGPVGGTTHLGEGKVTVWGNDPKGHPDQAWKICYEVETD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 390 GGGsLFIKTHPNSHHLYVDTTLNPDTKLSQSVAVFDinqlDKGYSVLPIAEYSgIKQGALrVVQPEYNKAGDEVWFSVWN 469
Cdd:cd20781 316 GPG-LFIRTHPNSDYVWADQTKHPEPEVQQSVQVID----KKTREIVKTIRVT-EEEGYV-AVHMEFNQDGTEVWVSVWN 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2096819685 470 ---GQTEESALVVIDDKTLKLKQVIrdKRLITPTGKFNVYNTQHDI 512
Cdd:cd20781 389 rkdSKEPNGEIVVYDAKTLEEKARI--KGLYTPTGKFNVYNRVNHV 432
|
|
| 8prop_heme_binding_protein |
cd20718 |
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ... |
96-506 |
2.35e-116 |
|
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; Members here contain an 8-bladed beta-propeller heme-binding domain in cytochrome cd1 (nitrite reductase) and similar proteins including NirN and NirF. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO(3-)-> NO(2-)-> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic nitrite reductase NirS via its maturation factor NirF. NirN and NirF form a stable complex with the nitrite reductase NirS during enzyme maturation. NirF is involved in heme d1 insertion.
Pssm-ID: 467720 [Multi-domain] Cd Length: 380 Bit Score: 348.17 E-value: 2.35e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 96 KTWKVLVKPADRPKKQLNMLNLENLFSVTLRDDGKIALVDGDTKQIVKLIDTGYA-VHISRISASGRYLLVIGRDAKIDM 174
Cdd:cd20718 5 KSLEVLVPERELPPVAYGIWDLENLMVVVERDAGSVLVIDGSTHEVLGRIDDGGAqVHVVVFSPDGRFAYVISRDGWLTK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 175 IDLWPAEPtkVAEIKVGIEARSVETSKfkgyEDTYAIAGSYWPPQFTIMDGETLEPKQIVSTRGMTVDKqeyHPEPRVAA 254
Cdd:cd20718 85 IDLYTLRP--VASIRIGVNSRGIALSD----DGKYVIAGNYEPGHVVILDADTLEPLKVIPTTGVNDDG---IIESRVGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 255 IIASHEWPEFIVNIKETGKVMLVNYQDIK-NLTITTIDAAPFLHDGGWDSTHRYFMTAANNSNKVAVIDSRERKLTALVD 333
Cdd:cd20718 156 ILETPPGPYFLVALKDAGSVWVIDYSDPDgNKVTDIGNIGRPLHDAFLDPDGRYFIVASQGSNTMWVLDLKTGKVVARIP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 334 VGKTPHPGRGANFIHptyGPVWATSHLGDGGISVIGTDpvkhaqyAWKQVESLKGQGGGsLFIKTHPNSHHLYVDTTLNP 413
Cdd:cd20718 236 TGKTPHPGPGATWGR---KGVTATPHLGEGIVTVWDLD-------TWKPVKYIPTPGPG-RFVRTHPSSPYVWADTVFGP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 414 DTKlsQSVAVFDINqldkgysVLPIAEYSGIKQGAlRVVQPEYNKAGDEVWFSVWNGqteeSALVVIDDKTLKLKQVIRD 493
Cdd:cd20718 305 ENA--DEIYVIDKE-------TLKVVKTLIPKPGK-RALHPEFTRDGKYVYVSVWDG----GEVVVYDAETLELVKRIPA 370
|
410
....*....|...
gi 2096819685 494 KrliTPTGKFNVY 506
Cdd:cd20718 371 E---TPTGIFNVG 380
|
|
| 8prop_hemeD1_cyt_cd1-like |
cd20783 |
eight-bladed heme d1-binding beta-propeller domain and similar proteins; Cytochrome cd1 (cyt ... |
93-506 |
6.13e-55 |
|
eight-bladed heme d1-binding beta-propeller domain and similar proteins; Cytochrome cd1 (cyt cd1) nitrite reductase catalyzes in vitro the reduction of molecular oxygen to water and the reduction of nitrite to nitric oxide). It is a dimer of two identical subunits of 60 kDa, each containing one c and one d1 heme group. The c heme is the electron accepting pole of the molecule and is reduced in vitro by either azurin or cytochrome c551. The d1 heme is the site where nitrite, and oxygen reduction occur. NiR is a key denitrification enzyme, which controls the rate of the production of toxic nitric oxide (NO) and ultimately regulates the release of NO into the atmosphere. The two types of heme are located in separate domains whose arrangement suggests a mechanism requiring domain movement during catalysis.
Pssm-ID: 467727 [Multi-domain] Cd Length: 388 Bit Score: 189.14 E-value: 6.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 93 ETLKTWKVLVKPADRPKKQLNMLNLENLFSVTLRDDGKIALVDGDTKQIVKLIDTGYAVHISRIS-ASGRYLLVIGRDAK 171
Cdd:cd20783 2 DIAASREVLVPESELPAEPTHDGNVDNLLLVTEREARSIAVIDGDTHTLLGHIEAGYRAHGYTFSpTDGRWAYNLGRDGW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 172 IDMIDLWPAEPtkVAEIKVGIEARSVETSKfkgyEDTYAIAGSYWPPQFTIMDGETLEPKQIVSTRGmtVDKQEYHPEPR 251
Cdd:cd20783 82 LYKIDLYSLQP--VAKVRVGLDARGIAISD----DGKYLIAGNYIPATAVILDAKTLEPLKVIDTSG--VDPDGKMVDSR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 252 VAAIIA---SHEWPEFIVNIKETGKVMLVNYQDiKNLTITTI-DAAPFLHDGGWDSTHRYFMTAANNSNKVAVIDSRERK 327
Cdd:cd20783 154 VASVNDvapDLVGPYFLLALKEAGQVWRIDYSK-PDFPITKVeNVGHILHDGFLSPDNKTFYLASQTDNWMAAIDVATMK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 328 LTALVDVGKTPHPGRGAnfihptygpVW--------ATSHLGDGGISVIGTDPVKHAqyawKQVESlkgqGGGSLFIKTH 399
Cdd:cd20783 233 IVAKIPTGDKPHPGSGA---------VWeadgkeyaATVHAGEGKVTIWDLDTNEIV----GEVPT----SGPGLFIRTT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 400 PNSHHLYVDTTLNPDtklSQSVAVFDINQldkgysvlPIAEYSGIKQGaLRVVQPEYNKAGDEVWFSVWNGQTeesaLVV 479
Cdd:cd20783 296 ENMPYVWADSMFAPE---PNEITVHEKAP--------PFKVVKRITDG-TRTLHPEPTADGKYVYVSDWDGNV----VRV 359
|
410 420
....*....|....*....|....*..
gi 2096819685 480 IDDKTLKLKQVIRDkrLITPTGKFNVY 506
Cdd:cd20783 360 YDAETLELVKEITG--ITTPTGIFNTS 384
|
|
| 8prop_hemeD1_cyt_cd1-like |
cd20782 |
cytochrome cd1 nitrate reductase eight-bladed heme d1-binding beta-propeller domain and ... |
86-503 |
5.14e-51 |
|
cytochrome cd1 nitrate reductase eight-bladed heme d1-binding beta-propeller domain and similar proteins; Cytochrome cd1 (cyt cd1) nitrite reductase catalyzes in vitro the reduction of molecular oxygen to water and the reduction of nitrite to nitric oxide). It is a dimer of two identical subunits of 60 kDa, each containing one c and one d1 heme group. The c heme is the electron accepting pole of the molecule and is reduced in vitro by either azurin or cytochrome c551. The d1 heme is the site where nitrite, and oxygen reduction occur. NiR is a key denitrification enzyme, which controls the rate of the production of toxic nitric oxide (NO) and ultimately regulates the release of NO into the atmosphere. The two types of heme are located in separate domains whose arrangement suggests a mechanism requiring domain movement during catalysis.
Pssm-ID: 467726 [Multi-domain] Cd Length: 415 Bit Score: 179.60 E-value: 5.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 86 PPEW---GMAETLKTWKVLVKPADRPKKQLNMLNLENLFSVTLRDDGKIALVDGDTKQIVKLI-DTGYAVH-------IS 154
Cdd:cd20782 11 PPSFdyrDLEDIADSHEIHKEEEELPQEPQHDDDLRDLLVVAERRNASVSLVDTVNHERLGRIeDVGRAIHviefhrdLP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 155 RISASGRYLLVIGRDAKIDMIDLWPAEptKVAEIKVGIEARSVETSKfkgyEDTYAIAGSYWPPQFTIMDGETLEPKQIV 234
Cdd:cd20782 91 ENEREGAYAYTQSRQGWVSKLDLFGGE--RVARVRAGTDARDIAVSR----DSNYLIAGYYNPNHLVVVDAETMEPLKRI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 235 STRGMTVDKQEYhpEPRVAAIIASHEWPEFIVNIKETGKVMLVNYQDIKNLTITTIDAAPFLHDGGWDSTHRYFMTAANN 314
Cdd:cd20782 165 PTHGVDPDGQSV--ESRVCTLYDVPGEGCFLAALKEAGQVWLIDYTQDDFPVVDEIDCGRTLHDGFFTPDGRYFMLASQT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 315 SNKVAVIDSRERKLTALVDVGKTPHPGRGAnfIHPTYGPVWaTSHLGDGGISVIGTDpvkhaqyAWKQVESLKGQGGGsL 394
Cdd:cd20782 243 DNCMSVLDVEEREVVDRIPTAGVPHPGPGA--LDPDRGLAF-TTHVGTDAVTAWDTE-------TWEPEADIEVPGGG-L 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 395 FIKTHPNSHHLYVDTTLNPDTKLSQSVAVFDINQLDkgysvlpIAEYSGIKQ-GALRVVQPEYNKAGDEVWFSVWNGQTe 473
Cdd:cd20782 312 FLRSHPDSDYVWGDVILDDTDRLDQLIYAIDPDTLE-------VATVIDTSEwGEGRAIHPEFSRDGEKVYVSHWDAGE- 383
|
410 420 430
....*....|....*....|....*....|
gi 2096819685 474 esaLVVIDDKTLKLKQVIRDkrLITPTGKF 503
Cdd:cd20782 384 ---ILVFDSHTGELIEEIDG--LETPTGKF 408
|
|
| 8prop_heme-binding_NirN |
cd20777 |
eight-bladed heme d1-binding beta-propeller domain in dihydro-heme d1 dehydrogenase NirN; The ... |
87-507 |
4.90e-39 |
|
eight-bladed heme d1-binding beta-propeller domain in dihydro-heme d1 dehydrogenase NirN; The monomeric dihydro-heme d1 dehydrogenase NirN is part of the denitrification process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. NirN, similar to the homodimeric cytochrome cd1 (nitrite reductase; NirS), consists of an eight-bladed heme d1-binding beta-propeller and a cytochrome c domain, but their relative orientation differs with respect to NirS. His147, His323 and Tyr461, but not His417 are essential for activity. All 8 blades of the propeller are included in this alignment.
Pssm-ID: 467721 [Multi-domain] Cd Length: 405 Bit Score: 146.74 E-value: 4.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 87 PEWGMAETLKT---WKVLVKPADRPKKQLNMLNLenlFSVTLRDDGKIALVDGDTKQIVKLIDTGYAVHIS-RISASGRY 162
Cdd:cd20777 1 PQWTAADIRASrevPPPAATLPDRPVFGADPLNL---FVVVESGDHHVTVLDGDRFEPLARFPTRFALHGGpKFSPDGRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 163 LLVIGRDAKIDMIDLWPAEPtkVAEIKVGIEARSVETSKfkgyEDTYAIAGSYWPPQFTIMDGETLEPKQIVSTRGMtvD 242
Cdd:cd20777 78 VYFASRDGWVTKYDLWNLKV--VAEVRAGLNTRNLAVSS----DGRYVAVANYLPHTLVLLDARDLSLLKVIPAADA--Q 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 243 KQeyhpEPRVAAIIASHEWPEFIVNIKETGKVMLVNYQD---------------------IKNLTITTIDAAPFLHDGGW 301
Cdd:cd20777 150 GR----SSRVSAVYDAPPRRSFVVALKDVPELWELSYDEgadpvpiglvhdflyeegaasPGFFAPRRIALPAPLDDFFF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 302 DSTHRYFMTAANNSNKVAVIDSRERKLTALVDVGKTPHPGRGANFIHPTYgPVWATSHLGDGGISVIGTDpvkhaqyAWK 381
Cdd:cd20777 226 DPDYRNLLGASRQGGGGQVIDLDVGRVIASLPLSGMPHLGSGIYWKRDGR-RVMATPNLSRGVISVIDLQ-------TWA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 382 QVESLKGQGGGsLFIKTHPNSHHLYVDTTLNPDtklSQSVAVFDINQLDKGYSVLPIAEYSgikqgalrVVQPEYNKAGD 461
Cdd:cd20777 298 IVKEIPTPGPG-FFMRSHENSPYAWADVFMGPK---RDKLHLIDKQTLEIVKTLRPEPGKT--------AAHVEFTRDGR 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2096819685 462 EVWFSVWNgqtEESALVVIDDKTLK-LKQVIRDKrlitPTGKFNVYN 507
Cdd:cd20777 366 YALASVWE---DDGALIVYDAHTLKeVKRLPMNK----PSGKYNVWN 405
|
|
| 8prop_hemeD1_NiR_delta_epsilon |
cd20780 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NiR ... |
91-510 |
1.64e-29 |
|
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NiR delta/epsilon subdivisions; Cytochrome cd1 (nitrite reductase) catalyzes in vitro the reduction of molecular oxygen to water and the reduction of nitrite to nitric oxide. Purification and characterization of NiR from several bacterial sources have shown that there are two distinct classes of dissimilatory NiRs that yield NO as the main reaction product, containing either copper or heme as cofactor- the heme-containing enzyme occurring more frequently. It forms a homodimer with each subunit containing one C and one D1 heme group. The C heme is the electron accepting pole of the molecule and is reduced in vitro by either azurin or cytochrome c551. The D1 heme is the site where nitrite, and oxygen reduction occur. NiR is a key denitrification enzyme, which controls the rate of the production of toxic nitric oxide (NO) and ultimately regulates the release of NO into the atmosphere. The two types of heme are located in separate domains whose arrangement suggests a mechanism requiring domain movement during catalysis. The heme-binding nitrite reductase in delta and epsilon subdivisions are present here.
Pssm-ID: 467724 [Multi-domain] Cd Length: 436 Bit Score: 120.33 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 91 MAETLKTWKVLVKPADRPKKQLNMLNLENLFSVTL---RDDGKIALVDGDTKQIVKLIDTGYAVHISRISASG-RYLLVI 166
Cdd:cd20780 19 LDEVKKTWKKLADREELAKKYPHAVDVKSVTDITFateRDASLVDFIDGTTGKVLSRHKAGFAVHVTVTNKRNpRYAYSI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 167 GRDAKIDMIDL-WPAEPtKVAEIKVGIEARSVETSKfkgyEDTYAIAGSYWPPQFTIMDGETLEPKQIVSTRGMTVDKQE 245
Cdd:cd20780 99 SRSGRLTMFDLaAPGQP-ALASVQVGQESRGLAVSP----DGKYVMAGNYNPGGAVLCDAMTLEPLKVYDTSSVIDPDGQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 246 YHPEpRVAAIIASHEWPEFIVNIKETGKVMLVNYQ--------DIKNLTITTIDAapFLHDGgwDSTHRYFMTAANNSNK 317
Cdd:cd20780 174 IGPS-RVASIADTPYGPYFAFALKDAGHVYIVDYSkpdfpivgDIPNIGKILHDA--FLNEG--EGFGRYLMIASQGSDV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 318 VAVIDSRERKLTALVDVGKT--PHPGRGANFIHPT-YGPVWATSHLGDGGIsVIGTDPvkhaqyaWKQVESLKGQGGGsL 394
Cdd:cd20780 249 MGIVDFKTKNLAAKVYTGPKskPHPGQGSSWYNKGlGKQLHATVSMNVGDV-VIWDSN-------WDVVKHVPTAGGG-L 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 395 FIKTHPNSHHLYVDTTLNPDTKLSQsvaVFDIN----QLDKGYSVlpiaeysGIKQGAL-------------RVVQPEYN 457
Cdd:cd20780 320 FVGTSEHTPYLWADCVLGGPDNYNK---VHLINkqtlETDRIIKV-------GKTKGTLidaktkkvlqtwdRLLHAEPA 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2096819685 458 KAGDEVWFSVWNgqteESALVVIDDKTLKLKQVIrdKRLITPTGKFNVYNTQH 510
Cdd:cd20780 390 NHGKWTMISEWT----TGRIGIYESKTGKFVKYI--ENLTTPTFTYSVEHRQH 436
|
|
| 8prop_hemeD1_cyt_cd1-like |
cd20785 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase and ... |
87-503 |
4.41e-25 |
|
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase and similar proteins; Cytochrome cd1 (cyt cd1) nitrite reductase catalyzes in vitro the reduction of molecular oxygen to water and the reduction of nitrite to nitric oxide). It is a dimer of two identical subunits of 60 kDa, each containing one c and one d1 heme group. The c heme is the electron accepting pole of the molecule and is reduced in vitro by either azurin or cytochrome c551. The d1 heme is the site where nitrite, and oxygen reduction occur. NiR is a key denitrification enzyme, which controls the rate of the production of toxic nitric oxide (NO) and ultimately regulates the release of NO into the atmosphere. The two types of heme are located in separate domains whose arrangement suggests a mechanism requiring domain movement during catalysis.
Pssm-ID: 467729 [Multi-domain] Cd Length: 412 Bit Score: 107.38 E-value: 4.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 87 PEWGMAETLKTWKVLVKPADR--PKKQLNMLNLENLFSVTLR------DDGKIALVDGDTKQIVKLIDTGYAVHISRISA 158
Cdd:cd20785 6 PSWGLEDIRKSLEVLVADESTlpSKPTYAIDDIDDLMAVMARgrygrgKGSKVVFFDGKTNRKVGEIPTGFAPHIMDFHP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 159 SG-RYLLVIGRDAKIDMIDLWPAEptKVAEIKVGIEARSVETSkfkgYEDTYAIAGSYWPPQFTIMDGETLEPKQIVSTR 237
Cdd:cd20785 86 VNpRWAYVKTDTGEVYKIDLYSMQ--AVRSVKAGLNGPSLAVS----RDGKYLAAGSFVPHTAVILDADTLEPLKYFELE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 238 GMTVDKQeyHPEPRVAAIIASHEWPEFIVNIKETGKVMLVNYqDIKNLTITTI-DAAPFLHDGGWDSTHRYFMTAANNSN 316
Cdd:cd20785 160 GVDPDGK--MVESDSGMITGTPYANYFAIALEQAGQVWIVDL-DKPGMPVTKIkNVGRHLHDAFLSPDGRYLMVASYDDN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 317 KVAVIDSRERKLTALVDVGKTPHPGRGAnfIHPTYGPVwatshLGDGgiSVIGTDPVKHAQYAW--------KQVESLkg 388
Cdd:cd20785 237 KNAVIDLKEKKVVKKIPAGCQPHLGSGA--VVKVGGRL-----LGFG--TNIGSCDDKTVVTVWdmdtfevvKQIPVS-- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 389 qgGGSLFIKTHPNSHHlyvdttlnpdtklsqsVAVfDINQLDKGYSVLPIaeysgIKQGALRVVQ----------PEYNK 458
Cdd:cd20785 306 --GPTESPAAHPNAPY----------------VAV-DIVGKDPRARKIQL-----IDKNTLEVVKtldvgghshfPEYTA 361
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2096819685 459 AGDEVWFSV-WNGqteeSALVVIDDKTLKLkqvIRDKRLITPTGKF 503
Cdd:cd20785 362 DGDYLYVSAgYNG----DRLVIYDSKTLKK---VKEIPMESPAGIF 400
|
|
| 8prop_hemeD1_cyt_cd1-like |
cd20784 |
cytochrome cd1 nitrate reductase eight-bladed heme d1-binding beta-propeller domain and ... |
87-507 |
8.75e-24 |
|
cytochrome cd1 nitrate reductase eight-bladed heme d1-binding beta-propeller domain and similar proteins; Cytochrome cd1 (cyt cd1) nitrite reductase catalyzes in vitro the reduction of molecular oxygen to water and the reduction of nitrite to nitric oxide). It is a dimer of two identical subunits of 60 kDa, each containing one c and one d1 heme group. The c heme is the electron accepting pole of the molecule and is reduced in vitro by either azurin or cytochrome c551. The d1 heme is the site where nitrite, and oxygen reduction occur. NiR is a key denitrification enzyme, which controls the rate of the production of toxic nitric oxide (NO) and ultimately regulates the release of NO into the atmosphere. The two types of heme are located in separate domains whose arrangement suggests a mechanism requiring domain movement during catalysis.
Pssm-ID: 467728 [Multi-domain] Cd Length: 367 Bit Score: 102.70 E-value: 8.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 87 PEWGMAETLKTWKVLvkpaDRPKKQLNMLNLENLFSVTLRDDGKIALVDGDtkQIVKLIDTGyAVHIS-RISASGRYLLV 165
Cdd:cd20784 2 IRWSKEDIKKSITIF----NDKPKPLEIKDIENITLVVERGGGKVWVMEGF--RVLDKFDFG-NVHGGiKFSPSGKKIYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 166 IGRDAKIDMIDLwpAEPTKVAEIKVGIEARSVETSKfkgyEDTYAIAGSYWPPQFTIMDGETLEPKQIVSTRGmtvdkqe 245
Cdd:cd20784 75 PSRDGWIGKYDL--KEGRETGKVRACINLRNIALSR----DGKYLAAACLLPENLVILDTKTLKPVKVIKLDG------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 246 yhpepRVAAIIASHEWPEFIVNIKETGKVMLVNYqdiKNLTITTIDAAPFLHDGGWDSTHRYFMTAANNSNKVAVIDSRE 325
Cdd:cd20784 142 -----KISAVYELYSKDKAIFTFRDKPKLGFLDT---KTLKIEYIKIKEPFEDFFIDPFEEYIIGTSRKGKKLYVYSLKD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 326 RKLTALVDVGKTPHPG------RGANFihptYgpvWATSHLGDGGISVIgtdpvkhAQYAWKQVE--SLKGQGggsLFIK 397
Cdd:cd20784 214 LKKVFEHKMEGMPHLFsatfwyKKGKF----Y---FATPHIKKPYVSIW-------KMYDWKFVKeiDLGGDG---FFVR 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 398 THPNSHHLYVDTtlNPDTklsqsvaVFDINQldKGYSVLPIaeysGIKQGAlRVVQPEYNKAGDEVWFSVWNgqtEESAL 477
Cdd:cd20784 277 THPKTPYLWVDN--GTDK-------LVLIDK--KDLSVKKI----TPPKGK-KAIHTEFSGDGKYAYVSIYE---KDGAL 337
|
410 420 430
....*....|....*....|....*....|
gi 2096819685 478 VVIDDKTLKLKQVIRDKRlitPTGKFNVYN 507
Cdd:cd20784 338 VVYDTFTLKELKRYPANI---PVGKYNFVN 364
|
|
| CccA |
COG2010 |
Cytochrome c, mono- and diheme variants [Energy production and conversion]; |
2-85 |
4.90e-15 |
|
Cytochrome c, mono- and diheme variants [Energy production and conversion];
Pssm-ID: 441613 [Multi-domain] Cd Length: 169 Bit Score: 73.06 E-value: 4.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 2 SQADFDTSKQIYFERCAGCHGVLRKGATGK--PLTPDITQARGQAYLEALITYGSPAG-MPNWGtsNALTKAQITSMATF 78
Cdd:COG2010 85 DAEALARGKALYEQNCAACHGADGKGGLGAapNLTDDALYGGDPEALVETILNGRPGGaMPAFG--GQLSDEEIAALAAY 162
|
....*..
gi 2096819685 79 IQHTAPT 85
Cdd:COG2010 163 LRSLSGN 169
|
|
| Cytochrome_CBB3 |
pfam13442 |
Cytochrome C oxidase, cbb3-type, subunit III; |
4-79 |
2.05e-08 |
|
Cytochrome C oxidase, cbb3-type, subunit III;
Pssm-ID: 463879 [Multi-domain] Cd Length: 67 Bit Score: 50.87 E-value: 2.05e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2096819685 4 ADFDTSKQIYFERCAGCHGvlrKGATGKPLTPDitqARGQAYLEALITYGsPAGMPNWGTSnaLTKAQITSMATFI 79
Cdd:pfam13442 1 AAAAAGEALYAANCASCHG---TGGAGPSLAGR---ALPPEALVDIIRNG-KGAMPAFGGD--LSDEELEALAAYL 67
|
|
| 8prop_hemeD1_NirF |
cd20778 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ... |
123-503 |
2.16e-08 |
|
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; Denitrification is a process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO3- -> NO2- -> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic cytochrome cd1 (nitrite reductase) NirS via its maturation factor NirF. The nirFDLGHJE genes encode proteins required for heme d1 biosynthesis. NirS, NirF, and NirN, the monomeric dihydro-heme d1 dehydrogenase form a stable complex during nitrite reductase maturation. The nitrite reductase NirS is bound to the denitrification supercomplex via NorB, while the electron donor system NirM and the enzyme maturation machinery NirN-NirF-NirQ, interacting with NirS, are bound via NorC.
Pssm-ID: 467722 [Multi-domain] Cd Length: 381 Bit Score: 56.14 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 123 VTLRDDGKIALVDGDTKQIVKLI----DTGYAVHIsrISASGRYLLVIGRDA---KIDMIDLwpaepTKVAEIKVGIEAR 195
Cdd:cd20778 23 VVEREAGSVFVVDRSKHESLGRIeglgNLSHATMV--FSRDGRYAYVIGRDGglsKVDLLTL-----KVVARVKQSGNSI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 196 SVETSKfkgyeDTYAIA-GSYWPPQFTIMDGETLEPKQIVStrgmTVDKQEYHPEPRVAAIIASheWPEFIVNIKETGKV 274
Cdd:cd20778 96 GGAISQ-----DGRYVAvANYDPGGVKILDADTLKVLADIP----AGSKGGGQRSRVVGLVDAP--GNRFIFSLMDADEI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 275 MLVNYQDIKNLTITT---IDAAPFlhDGGWDSTHRYFMTAANNSNKVAVIDSRERKLTALVdvgKTPHPGRGANFIhpty 351
Cdd:cd20778 165 WVLDASDPDFPVVKKfkdIGRMPY--DALITPDGRYYIAGLFNSDGVGLLDLWKPERGVRR---ILLDYGKGEEKL---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 352 gPVWATSHLGDGGIS-------VIGTDPVK-HAQYAWKQVES--LKGQgggSLFIKTHPNSHHLYVD--TTLNP-----D 414
Cdd:cd20778 236 -PVYKMPHLEGWAVAgdkafvpAVGEHRVLvYDTNDWKFIKSipLAGQ---PVFAVARPDGRYVWVNfsGPDNDtvqviD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 415 TKLSQSVAVFDINQldkgysvlpiaeysgikqgalRVVQPEYNKAGDEVWFSVwngqTEESALVVIDDKTLKLkqvIRDK 494
Cdd:cd20778 312 TKTLKVVKTLEPGK---------------------RVLHMEFTPRGEAVYISV----NDDNKVVVYDTRTFRE---IKEV 363
|
....*....
gi 2096819685 495 RLITPTGKF 503
Cdd:cd20778 364 PAKKPSGIF 372
|
|
| TsdA |
COG3258 |
Thiosulfate dehydrogenase TsdA, contains C-terminal cytochrome c domain [Inorganic ion ... |
3-88 |
1.02e-07 |
|
Thiosulfate dehydrogenase TsdA, contains C-terminal cytochrome c domain [Inorganic ion transport and metabolism];
Pssm-ID: 442489 [Multi-domain] Cd Length: 216 Bit Score: 52.55 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 3 QADFDTSKQIYFERCAGCHGVL---RKGATGKPLTPDI------TQARGQAYLEALITYGSPAGMPnWGTSNALTKAQIT 73
Cdd:COG3258 114 SADVERGKALYAERCASCHGADgegQGRADGQYGFPPLwggdsyNDGAGMARLGTLADFIKGRNMP-LGKPGSLSDDEAW 192
|
90
....*....|....*
gi 2096819685 74 SMATFIQHTAPTPPE 88
Cdd:COG3258 193 DVAAYVRSLPRPVPR 207
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
287-426 |
3.07e-05 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 45.46 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 287 ITTIDAAPFLHDGGWDSTHRYFMTAANNSNKVAVIDSRERKLTALVDVGKTPHpgrgANFIHPTYGPVWATSHlGDGGIS 366
Cdd:COG3391 103 VATIPVGGGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIPVGAGPH----GIAVDPDGKRLYVANS-GSNTVS 177
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2096819685 367 VIGT--DPVkhaqyAWKQVESLKGqGGGSLFIKTHPNSHHLYVDTTLNPDT-KLSQSVAVFDI 426
Cdd:COG3391 178 VIVSviDTA-----TGKVVATIPV-GGGPVGVAVSPDGRRLYVANRGSNTSnGGSNTVSVIDL 234
|
|
| Cytochrom_C |
pfam00034 |
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ... |
10-82 |
1.60e-04 |
|
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and cytochrome c' families are not included. All these are now in a new clan together. The C-terminus of DUF989, pfam06181, has now been merged into this family.
Pssm-ID: 459641 [Multi-domain] Cd Length: 89 Bit Score: 40.60 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096819685 10 KQIYFERCAGCHGVlrKGATGKPLTPDITQA-----------------RGQAYLEALITYGSPAGMPNWgtsNALTKAQI 72
Cdd:pfam00034 4 KKLFAANCAACHGV--NGEGAGAGGPDLAGLaarypgdalgairenkhAIGGGGVDRAGGPPGTGMPAF---DGLTDEEI 78
|
90
....*....|
gi 2096819685 73 TSMATFIQHT 82
Cdd:pfam00034 79 ADLVAYLLSL 88
|
|
| ccoP |
TIGR00782 |
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of ... |
7-80 |
1.52e-03 |
|
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of approximately 26 kDa of the cbb3 type copper and heme-containing cytochrome oxidase. [Energy metabolism, Electron transport]
Pssm-ID: 129864 [Multi-domain] Cd Length: 285 Bit Score: 40.65 E-value: 1.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2096819685 7 DTSKQIYFERCAGCHGVLRKG--ATGKP-LTPDITQARG-QAYLEALITYGSPAGMPNWGTSnaLTKAQITSMATFIQ 80
Cdd:TIGR00782 204 AKGQELFADNCTTCHGEDGKGlqELGAPnLTDDVWLYGGdLKTITTTITNGRGGVMPAWGPR--LSEAQIKALAAYVH 279
|
|
| |
