|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02252 |
PLN02252 |
nitrate reductase [NADPH] |
6-307 |
1.37e-137 |
|
nitrate reductase [NADPH]
Pssm-ID: 215141 [Multi-domain] Cd Length: 888 Bit Score: 410.61 E-value: 1.37e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 6 LWTASLPVLSRVVLSPVWFVYSLFMKLFQRSSP-AITLENPDIKYPLRLIDKEIISHDTRRFRFALPSPQHILGLPIGQH 84
Cdd:PLN02252 591 LVTTGAAASSSASSHPLSAISTASALAAASPAPgRPVALNPREKIPCRLVEKISLSHDVRLFRFALPSEDHVLGLPVGKH 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 85 IYLSTRIDGNLVIRPYTPVSSDDDKGFVDLVVKVYFKDTHPKFPAGGKMSQYLENMNIGDTIEFRGPNGLLVYQGKGKFA 164
Cdd:PLN02252 671 VFLCATINGKLCMRAYTPTSSDDEVGHFELVIKVYFKNVHPKFPNGGLMSQYLDSLPIGDTIDVKGPLGHIEYAGRGSFL 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 165 IRADKKsnpvvrTVKSVGMIAGGTGITPMLQVIRAVLKDPNDHTVCYLLFANQSEKDILLRPELEELRNEHSSRFKLWYT 244
Cdd:PLN02252 751 VNGKPK------FAKKLAMLAGGTGITPMYQVIQAILRDPEDKTEMSLVYANRTEDDILLREELDRWAAEHPDRLKVWYV 824
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564361154 245 VDK-APDAWDYSQGFVNEEMIRDHLPPPGEETLILMCGPPPMIQFACLPNLERVGHPKERCFTF 307
Cdd:PLN02252 825 VSQvKREGWKYSVGRVTEAMLREHLPEGGDETLALMCGPPPMIEFACQPNLEKMGYDKDSILVF 888
|
|
| cyt_b5_reduct_like |
cd06183 |
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ... |
51-307 |
8.64e-127 |
|
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as an electron donor. Like ferredoxin reductases, these proteins have an N-terminal FAD binding subdomain and a C-terminal NADH binding subdomain, separated by a cleft, which accepts FAD. The NADH-binding moiety interacts with part of the FAD and resembles a Rossmann fold. However, NAD is bound differently than in canonical Rossmann fold proteins. Nitrate reductases, flavoproteins similar to pyridine nucleotide cytochrome reductases, catalyze the reduction of nitrate to nitrite. The enzyme can be divided into three functional fragments that bind the cofactors molybdopterin, heme-iron, and FAD/NADH.
Pssm-ID: 99780 [Multi-domain] Cd Length: 234 Bit Score: 361.11 E-value: 8.64e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 51 LRLIDKEIISHDTRRFRFALPSPQHILGLPIGQHIYLSTRIDGNLVIRPYTPVSSDDDKGFVDLVVKVYFkdthpkfpaG 130
Cdd:cd06183 1 FKLVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPDDGEQVVRPYTPISPDDDKGYFDLLIKIYP---------G 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 131 GKMSQYLENMNIGDTIEFRGPNGLLVYQGKGKfairadkksnpvvrtVKSVGMIAGGTGITPMLQVIRAVLKDPNDHTVC 210
Cdd:cd06183 72 GKMSQYLHSLKPGDTVEIRGPFGKFEYKPNGK---------------VKHIGMIAGGTGITPMLQLIRAILKDPEDKTKI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 211 YLLFANQSEKDILLRPELEELRNEHSSRFKLWYTVDKAPDAWDYSQGFVNEEMIRDHLPP-PGEETLILMCGPPPMIQFA 289
Cdd:cd06183 137 SLLYANRTEEDILLREELDELAKKHPDRFKVHYVLSRPPEGWKGGVGFITKEMIKEHLPPpPSEDTLVLVCGPPPMIEGA 216
|
250
....*....|....*...
gi 564361154 290 CLPNLERVGHPKERCFTF 307
Cdd:cd06183 217 VKGLLKELGYKKDNVFKF 234
|
|
| PTZ00319 |
PTZ00319 |
NADH-cytochrome B5 reductase; Provisional |
22-307 |
2.05e-123 |
|
NADH-cytochrome B5 reductase; Provisional
Pssm-ID: 173521 [Multi-domain] Cd Length: 300 Bit Score: 355.29 E-value: 2.05e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 22 VWFVYSLFMKLFQRSSPAITLeNPDIKYPLRLIDKEIISHDTRRFRFALPSPQHILGLPIGQHIYLSTRIDGN----LVI 97
Cdd:PTZ00319 8 IALGVAAFFAFMFSRSPPVAL-DPDMFQHFKLIKKTEVTHDTFIFRFALHSPTQRLGLPIGQHIVFRCDCTTPgkpeTVQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 98 RPYTPVSSDDDKGFVDLVVKVYFKDTHPKFPAGGKMSQYLENMNIGDTIEFRGPNGLLVYQGKGKFAIRADKKSnPVVRT 177
Cdd:PTZ00319 87 HSYTPISSDDEKGYVDFLIKVYFKGVHPSFPNGGRLSQHLYHMKLGDKIEMRGPVGKFEYLGNGTYTVHKGKGG-LKTMH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 178 VKSVGMIAGGTGITPMLQVIRAVLKDPNDHTVCYLLFANQSEKDILLRPELEELRNEhsSRFKLWYTVDK-APDAWDYSQ 256
Cdd:PTZ00319 166 VDAFAMIAGGTGITPMLQIIHAIKKNKEDRTKVFLVYANQTEDDILLRKELDEAAKD--PRFHVWYTLDReATPEWKYGT 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 564361154 257 GFVNEEMIRDHLPPPG------EETLILMCGPPPMIQFACLPNLERVGHPKERCFTF 307
Cdd:PTZ00319 244 GYVDEEMLRAHLPVPDpqnsgiKKVMALMCGPPPMLQMAVKPNLEKIGYTADNMFTF 300
|
|
| FNR_like |
cd00322 |
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
56-306 |
3.32e-51 |
|
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).
Pssm-ID: 99778 [Multi-domain] Cd Length: 223 Bit Score: 168.39 E-value: 3.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 56 KEIISHDTRRFRFALPSPQHILGlpiGQHIYLSTRIDGNLVIRPYTPVSSDDDKGFVDLVVKVYFkdthpkfpaGGKMSQ 135
Cdd:cd00322 3 TEDVTDDVRLFRLQLPNGFSFKP---GQYVDLHLPGDGRGLRRAYSIASSPDEEGELELTVKIVP---------GGPFSA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 136 YLENMNIGDTIEFRGPNGllvyqgkgkFAIRADKKSNPVVrtvksvgMIAGGTGITPMLQVIRAVLKDPNDHTVcYLLFA 215
Cdd:cd00322 71 WLHDLKPGDEVEVSGPGG---------DFFLPLEESGPVV-------LIAGGIGITPFRSMLRHLAADKPGGEI-TLLYG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 216 NQSEKDILLRPELEELRNEHsSRFKLWYTVDKAPDAWDYSQGFVNEEMIRDHLPPPGEETLILMCGPPPMIQfACLPNLE 295
Cdd:cd00322 134 ARTPADLLFLDELEELAKEG-PNFRLVLALSRESEAKLGPGGRIDREAEILALLPDDSGALVYICGPPAMAK-AVREALV 211
|
250
....*....|.
gi 564361154 296 RVGHPKERCFT 306
Cdd:cd00322 212 SLGVPEERIHT 222
|
|
| NAD_binding_1 |
pfam00175 |
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ... |
183-290 |
3.81e-51 |
|
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity.
Pssm-ID: 425503 [Multi-domain] Cd Length: 109 Bit Score: 164.36 E-value: 3.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 183 MIAGGTGITPMLQVIRAVLKDPNDHTVCYLLFANQSEKDILLRPELEELRNEHSSRFKLWYTVDKAPDAWDYSQGFVNEE 262
Cdd:pfam00175 1 MIAGGTGIAPVRSMLRAILEDPKDPTQVVLVFGNRNEDDILYREELDELAEKHPGRLTVVYVVSRPEAGWTGGKGRVQDA 80
|
90 100
....*....|....*....|....*...
gi 564361154 263 MIRDHLPPPGEETLILMCGPPPMIQFAC 290
Cdd:pfam00175 81 LLEDHLSLPDEETHVYVCGPPGMIKAVR 108
|
|
| FAD_binding_6 |
pfam00970 |
Oxidoreductase FAD-binding domain; |
50-157 |
8.16e-51 |
|
Oxidoreductase FAD-binding domain;
Pssm-ID: 425968 [Multi-domain] Cd Length: 99 Bit Score: 163.14 E-value: 8.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 50 PLRLIDKEIISHDTRRFRFALPSPQHILGLPIGQHIYLSTRIDGNLVIRPYTPVSSDDDKGFVDLVVKVYfkdthpkfpA 129
Cdd:pfam00970 1 PLTLVEKELVSHDTRIFRFALPHPDQVLGLPVGQHLFLRLPIDGELVIRSYTPISSDDDKGYLELLVKVY---------P 71
|
90 100
....*....|....*....|....*...
gi 564361154 130 GGKMSQYLENMNIGDTIEFRGPNGLLVY 157
Cdd:pfam00970 72 GGKMSQYLDELKIGDTIDFKGPLGRFEY 99
|
|
| Fpr |
COG1018 |
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
49-306 |
1.20e-43 |
|
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 149.17 E-value: 1.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 49 YPLRLIDKEIISHDTRRFRFALPSPQHILG-LPiGQHIYLSTRIDGNLVIRPYTPVSSDDDKGFVDLVVKVyfkdthpkf 127
Cdd:COG1018 4 RPLRVVEVRRETPDVVSFTLEPPDGAPLPRfRP-GQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVKRV--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 128 pAGGKMSQYL-ENMNIGDTIEFRGPNGLLVYQGKGkfairadkkSNPVVrtvksvgMIAGGTGITPMLQVIRAVLKDPND 206
Cdd:COG1018 74 -PGGGGSNWLhDHLKVGDTLEVSGPRGDFVLDPEP---------ARPLL-------LIAGGIGITPFLSMLRTLLARGPF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 207 HTVcYLLFANQSEKDILLRPELEELRNEHsSRFKLWYTVDKAPDAWdysQGFVNEEMIRDHLPPPgEETLILMCGPPPMI 286
Cdd:COG1018 137 RPV-TLVYGARSPADLAFRDELEALAARH-PRLRLHPVLSREPAGL---QGRLDAELLAALLPDP-ADAHVYLCGPPPMM 210
|
250 260
....*....|....*....|
gi 564361154 287 QfACLPNLERVGHPKERCFT 306
Cdd:COG1018 211 E-AVRAALAELGVPEERIHF 229
|
|
| PTZ00274 |
PTZ00274 |
cytochrome b5 reductase; Provisional |
50-286 |
1.21e-38 |
|
cytochrome b5 reductase; Provisional
Pssm-ID: 140300 Cd Length: 325 Bit Score: 138.90 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 50 PLRLIDKEIISHDTRRFRFALPSPQHILGLPIG--QHIYLSTRIDGNLVIRPYTPVSSDDDKGFVDLVVKVyfkdthpkf 127
Cdd:PTZ00274 54 PYQLGEVIPITHDTALFRFLLHSEEEFNLKPCStlQACYKYGVQPMDQCQRFYTPVTANHTKGYFDIIVKR--------- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 128 PAGGKMSQYLENMNIGDTIEFRGPNGLLVYqgkgkfaiRADKksnpvvrtVKSVGMIAGGTGITPMLQVIRAVLKDP--- 204
Cdd:PTZ00274 125 KKDGLMTNHLFGMHVGDKLLFRSVTFKIQY--------RPNR--------WKHVGMIAGGTGFTPMLQIIRHSLTEPwds 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 205 --NDHTVCYLLFANQSEKDILLRPELEELRNEHSSRFKLWYTVDKA--PDAWDYSQGFVNEEMIRDHLPPPGEET-LILM 279
Cdd:PTZ00274 189 geVDRTKLSFLFCNRTERHILLKGLFDDLARRYSNRFKVYYTIDQAvePDKWNHFLGYVTKEMVRRTMPAPEEKKkIIML 268
|
....*..
gi 564361154 280 CGPPPMI 286
Cdd:PTZ00274 269 CGPDQLL 275
|
|
| Mcr1 |
COG0543 |
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
52-305 |
3.15e-36 |
|
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];
Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 130.37 E-value: 3.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 52 RLIDKEIISHDTRRFRFALPsPQHILGLPiGQHIYLstRIDGNLVIRPYTPVSSDDDKGFVDLVVKVYfkdthpkfpagG 131
Cdd:COG0543 1 KVVSVERLAPDVYLLRLEAP-LIALKFKP-GQFVML--RVPGDGLRRPFSIASAPREDGTIELHIRVV-----------G 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 132 KMSQYLENMNIGDTIEFRGPngllvyQGKGkFAIRADKKsnPVVrtvksvgMIAGGTGITPMLQVIRAVLKDPNDhtvCY 211
Cdd:COG0543 66 KGTRALAELKPGDELDVRGP------LGNG-FPLEDSGR--PVL-------LVAGGTGLAPLRSLAEALLARGRR---VT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 212 LLFANQSEKDILLRPELEELRNehssrFKLWYTVDkapDAWDYSQGFVNEEMIRDHlpPPGEETLILMCGPPPMIQFACl 291
Cdd:COG0543 127 LYLGARTPEDLYLLDELEALAD-----FRVVVTTD---DGWYGRKGFVTDALKELL--AEDSGDDVYACGPPPMMKAVA- 195
|
250
....*....|....
gi 564361154 292 PNLERVGHPKERCF 305
Cdd:COG0543 196 ELLLERGVPPERIY 209
|
|
| FNR_iron_sulfur_binding_3 |
cd06217 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
57-303 |
1.04e-35 |
|
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap between the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99813 [Multi-domain] Cd Length: 235 Bit Score: 128.54 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 57 EII--SHDTRRFRFALPSPQHILGLPiGQHIYLS-TRIDGNLVIRPYTPVSSDDDKGFVDLVVKVYfkdthpkfpAGGKM 133
Cdd:cd06217 8 EIIqeTPTVKTFRLAVPDGVPPPFLA-GQHVDLRlTAIDGYTAQRSYSIASSPTQRGRVELTVKRV---------PGGEV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 134 SQYL-ENMNIGDTIEFRGPNgllvyqgkGKFAIRaDKKSNPVVrtvksvgMIAGGTGITPMLQVIRAvLKDPNDHTVCYL 212
Cdd:cd06217 78 SPYLhDEVKVGDLLEVRGPI--------GTFTWN-PLHGDPVV-------LLAGGSGIVPLMSMIRY-RRDLGWPVPFRL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 213 LFANQSEKDILLRPELEELRNEHSsrfklWYTVD-----KAPDAWDYSQGFVNEEMIrDHLPPPGEETLILMCGPPPMIQ 287
Cdd:cd06217 141 LYSARTAEDVIFRDELEQLARRHP-----NLHVTealtrAAPADWLGPAGRITADLI-AELVPPLAGRRVYVCGPPAFVE 214
|
250
....*....|....*.
gi 564361154 288 fACLPNLERVGHPKER 303
Cdd:cd06217 215 -AATRLLLELGVPRDR 229
|
|
| PA_degradation_oxidoreductase_like |
cd06214 |
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ... |
49-303 |
4.09e-35 |
|
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation oxidoreductase. PA oxidoreductases of E. coli hydroxylate PA-CoA in the second step of PA degradation. Members of this group typically fuse a ferredoxin reductase-like domain with an iron-sulfur binding cluster domain. Ferredoxins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal portion may contain a flavin prosthetic group, as in flavoenzymes, or use flavin as a substrate. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria and participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99810 [Multi-domain] Cd Length: 241 Bit Score: 127.27 E-value: 4.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 49 YPLRLIDKEIISHDTRRFRFALPSP-QHILGLPIGQHIYLSTRIDGNLVIRPYTpVSSDDDKGFVDLVVK-Vyfkdthpk 126
Cdd:cd06214 2 HPLTVAEVVRETADAVSITFDVPEElRDAFRYRPGQFLTLRVPIDGEEVRRSYS-ICSSPGDDELRITVKrV-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 127 fpAGGKMSQYL-ENMNIGDTIEFRGPNGllvyqgkgKFAIRADKKSNPVVrtvksvgMIAGGTGITPMLQVIRAVLKDPN 205
Cdd:cd06214 73 --PGGRFSNWAnDELKAGDTLEVMPPAG--------RFTLPPLPGARHYV-------LFAAGSGITPVLSILKTALAREP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 206 DHTVCyLLFANQSEKDILLRPELEELRNEHSSRFKLWYTVDKAPDAWDYSQGFVNEEMIR---DHLPPPGEETLILMCGP 282
Cdd:cd06214 136 ASRVT-LVYGNRTEASVIFREELADLKARYPDRLTVIHVLSREQGDPDLLRGRLDAAKLNallKNLLDATEFDEAFLCGP 214
|
250 260
....*....|....*....|.
gi 564361154 283 PPMIQfACLPNLERVGHPKER 303
Cdd:cd06214 215 EPMMD-AVEAALLELGVPAER 234
|
|
| FNR_iron_sulfur_binding_1 |
cd06215 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
51-306 |
7.96e-35 |
|
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal portion of the FAD/NAD binding domain contains most of the NADP(H) binding residues and the N-terminal sub-domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. In this ferredoxin like sub-group, the FAD/NAD sub-domains is typically fused to a C-terminal iron-sulfur binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins which act as electron carriers in photosynthesis and ferredoxins which participate in redox chains from bacteria to mammals. Ferredoxin reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99811 [Multi-domain] Cd Length: 231 Bit Score: 126.17 E-value: 7.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 51 LRLIDKEIISHDTRRFRFALPSPQHILGLPiGQHIYLSTRIDGNLVIRPYTPVSSDDDKGFVDLVVKVYfkdthpkfpAG 130
Cdd:cd06215 1 LRCVKIIQETPDVKTFRFAAPDGSLFAYKP-GQFLTLELEIDGETVYRAYTLSSSPSRPDSLSITVKRV---------PG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 131 GKMSQYL-ENMNIGDTIEFRGPngllvyqgKGKFAIRADKKSNPVvrtvksvgMIAGGTGITPMLQVIRAVLKDPNDHTV 209
Cdd:cd06215 71 GLVSNWLhDNLKVGDELWASGP--------AGEFTLIDHPADKLL--------LLSAGSGITPMMSMARWLLDTRPDADI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 210 CYLLFAnQSEKDILLRPELEELRNEHSSrFKLWYTV-DKAPDAWDYSQGFVNEEMIRDHLPPPGEETlILMCGPPPMIQF 288
Cdd:cd06215 135 VFIHSA-RSPADIIFADELEELARRHPN-FRLHLILeQPAPGAWGGYRGRLNAELLALLVPDLKERT-VFVCGPAGFMKA 211
|
250
....*....|....*...
gi 564361154 289 ACLpNLERVGHPKERCFT 306
Cdd:cd06215 212 VKS-LLAELGFPMSRFHQ 228
|
|
| PTZ00306 |
PTZ00306 |
NADH-dependent fumarate reductase; Provisional |
63-302 |
1.33e-31 |
|
NADH-dependent fumarate reductase; Provisional
Pssm-ID: 140327 [Multi-domain] Cd Length: 1167 Bit Score: 124.51 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 63 TRRFRFALPSPQHILGLPIGQHIYLSTRIDGNLVIRPYTPVSSDDDKGFVDLVVKvyfKDThpkfpagGKMSQYLENMNI 142
Cdd:PTZ00306 932 SRVLRFNLPGALQRSGLTLGQFIAIRGDWDGQQLIGYYSPITLPDDLGVISILAR---GDK-------GTLKEWISALRP 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 143 GDTIEFRGPNGLLVYQgkgKFAIRADKKSNPVVRtvkSVGMIAGGTGITPMLQVIRAVLKDPNDHTV--CYLLFANQSEK 220
Cdd:PTZ00306 1002 GDSVEMKACGGLRIER---RPADKQFVFRGHVIR---KLALIAGGTGVAPMLQIIRAALKKPYVDSIesIRLIYAAEDVS 1075
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 221 DILLRPELEELRNEHSSRFKLWYTVDKAPDAWDYSQGFVNEEMIRDHLPPPGEETLILMCGPPPMiQFACLPNLERVGHP 300
Cdd:PTZ00306 1076 ELTYRELLESYRKENPGKFKCHFVLNNPPEGWTDGVGFVDRALLQSALQPPSKDLLVAICGPPVM-QRAVKADLLALGYN 1154
|
..
gi 564361154 301 KE 302
Cdd:PTZ00306 1155 ME 1156
|
|
| FNR_like_1 |
cd06196 |
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ... |
49-286 |
4.65e-26 |
|
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which varies in orientation with respect to the NAD(P) binding domain. The N-terminal region may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.
Pssm-ID: 99793 [Multi-domain] Cd Length: 218 Bit Score: 102.70 E-value: 4.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 49 YPLRLIDKEIISHDTRRFRFALPspqHILGLPIGQHIYLSTRIDG-NLVIRPYTPVSSDDDKgFVDLVVKVYfkdthpkf 127
Cdd:cd06196 1 HTVTLLSIEPVTHDVKRLRFDKP---EGYDFTPGQATEVAIDKPGwRDEKRPFTFTSLPEDD-VLEFVIKSY-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 128 PAGGKMSQYLENMNIGDTIEFRGPNGLLVYQGKGKFairadkksnpvvrtvksvgmIAGGTGITPMLQVIRAVLKDP--N 205
Cdd:cd06196 69 PDHDGVTEQLGRLQPGDTLLIEDPWGAIEYKGPGVF--------------------IAGGAGITPFIAILRDLAAKGklE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 206 DHTvcyLLFANQSEKDILLRPELEELRNEhssrfKLWYTVDKAPDAwDYSQGFVNEEMIRDHLPPPGEETLIlmCGPPPM 285
Cdd:cd06196 129 GNT---LIFANKTEKDIILKDELEKMLGL-----KFINVVTDEKDP-GYAHGRIDKAFLKQHVTDFNQHFYV--CGPPPM 197
|
.
gi 564361154 286 I 286
Cdd:cd06196 198 E 198
|
|
| sulfite_reductase_like |
cd06221 |
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ... |
99-306 |
1.99e-25 |
|
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural similarity to ferredoxin reductase and sequence similarity to dihydroorotate dehydrogenases. Clostridium pasteurianum inducible dissimilatory type sulfite reductase is linked to ferredoxin and reduces NH2OH and SeO3 at a lesser rate than it's normal substate SO3(2-). Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+.
Pssm-ID: 99817 [Multi-domain] Cd Length: 253 Bit Score: 101.92 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 99 PYTPVSSDDDKGFVDLVVKvyfkdthpkfpAGGKMSQYLENMNIGDTIEFRGP--NGLLVYQGKGKfairadkksnPVVr 176
Cdd:cd06221 45 PISISSDPTRRGPLELTIR-----------RVGRVTEALHELKPGDTVGLRGPfgNGFPVEEMKGK----------DLL- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 177 tvksvgMIAGGTGITPMLQVIRAVLKDPNDHTVCYLLFANQSEKDILLRPELEELRNehSSRFKLWYTVDKAPDAWDYSQ 256
Cdd:cd06221 103 ------LVAGGLGLAPLRSLINYILDNREDYGKVTLLYGARTPEDLLFKEELKEWAK--RSDVEVILTVDRAEEGWTGNV 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 564361154 257 GFVNEEMirDHLPPPGEETLILMCGPPPMIQFAcLPNLERVGHPKERCFT 306
Cdd:cd06221 175 GLVTDLL--PELTLDPDNTVAIVCGPPIMMRFV-AKELLKLGVPEEQIWV 221
|
|
| NqrF |
COG2871 |
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ... |
48-306 |
4.82e-24 |
|
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and conversion]; Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase
Pssm-ID: 442118 [Multi-domain] Cd Length: 396 Bit Score: 100.71 E-value: 4.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 48 KYPLRLIDKEIISHDTRRFRFALPSPQHI---------LGLPIGQHIYLSTRID-----------GNLVIRPYTPVSSDD 107
Cdd:COG2871 131 KWEATVVSNENVTTFIKELVLELPEGEEIdfkagqyiqIEVPPYEVDFKDFDIPeeekfglfdknDEEVTRAYSMANYPA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 108 DKGFVDLVVKVyfkDTHPKFPAGGKMSQYLENMNIGDTIEFRGPngllvYqgkGKFAIRADKKsnPVVrtvksvgMIAGG 187
Cdd:COG2871 211 EKGIIELNIRI---ATPPMDVPPGIGSSYIFSLKPGDKVTISGP-----Y---GEFFLRDSDR--EMV-------FIGGG 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 188 TGITPMLQVIRAVLKDPNDHTVCYLLFANQSEKDILLRPELEELRNEHSsRFKlWYTV--DKAP-DAWDYSQGFVNEEMI 264
Cdd:COG2871 271 AGMAPLRSHIFDLLERGKTDRKITFWYGARSLRELFYLEEFRELEKEHP-NFK-FHPAlsEPLPeDNWDGETGFIHEVLY 348
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 564361154 265 RDHL--PPPGEETLILMCGPPPMIQfACLPNLERVGHPKERCFT 306
Cdd:COG2871 349 ENYLkdHPAPEDCEAYLCGPPPMID-AVIKMLDDLGVEEENIYF 391
|
|
| O2ase_reductase_like |
cd06187 |
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
54-306 |
5.38e-24 |
|
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons using oxygen as the oxidant. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate, while mono-oxygenases (aka mixed oxygenases) add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate.
Pssm-ID: 99784 [Multi-domain] Cd Length: 224 Bit Score: 97.28 E-value: 5.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 54 IDKEIISHDTRRFRFALPSPQHILGlpiGQhiYLSTRIDG-NLVIRPYTPVSSDDDKGFVDLVVKVYfkdthpkfpAGGK 132
Cdd:cd06187 2 VSVERLTHDIAVVRLQLDQPLPFWA---GQ--YVNVTVPGrPRTWRAYSPANPPNEDGEIEFHVRAV---------PGGR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 133 MSQYLEN-MNIGDTIEFRGPNGllvyqgkgkFAIRADKKSNPVVrtvksvgMIAGGTGITPMLQVIRAVLKDPNDHTVcY 211
Cdd:cd06187 68 VSNALHDeLKVGDRVRLSGPYG---------TFYLRRDHDRPVL-------CIAGGTGLAPLRAIVEDALRRGEPRPV-H 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 212 LLFANQSEKDILLRPELEELRNEHsSRFKLWYTVDKAPDAWDYSQGFVNEEMIRDHlpPPGEETLILMCGPPPMIQfACL 291
Cdd:cd06187 131 LFFGARTERDLYDLEGLLALAARH-PWLRVVPVVSHEEGAWTGRRGLVTDVVGRDG--PDWADHDIYICGPPAMVD-ATV 206
|
250
....*....|....*
gi 564361154 292 PNLERVGHPKERCFT 306
Cdd:cd06187 207 DALLARGAPPERIHF 221
|
|
| flavohem_like_fad_nad_binding |
cd06184 |
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ... |
50-303 |
8.59e-24 |
|
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain containing a B-type heme fused with a ferredoxin reductase-like FAD/NAD-binding domain. Flavohemoglobins detoxify nitric oxide (NO) via an NO dioxygenase reaction. The hemoglobin domain adopts a globin fold with an embedded heme molecule. Flavohemoglobins also have a C-terminal reductase domain with bindiing sites for FAD and NAD(P)H. This domain catalyzes the conversion of NO + O2 + NAD(P)H to NO3- + NAD(P)+. Instead of the oxygen transport function of hemoglobins, flavohemoglobins seem to act in NO dioxygenation and NO signalling.
Pssm-ID: 99781 Cd Length: 247 Bit Score: 97.24 E-value: 8.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 50 PLRLIDKEIISHDTRRFRF------ALPSPQhilglPiGQHIYLSTRIDGN--LVIRPYTpVSSDDDKGFVDLVVKvyfK 121
Cdd:cd06184 8 PFVVARKVAESEDITSFYLepadggPLPPFL-----P-GQYLSVRVKLPGLgyRQIRQYS-LSDAPNGDYYRISVK---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 122 DthpkfpAGGKMSQYL-ENMNIGDTIEFRGPNGLLVYQgkgkfairaDKKSNPVVrtvksvgMIAGGTGITPMLQVIRAV 200
Cdd:cd06184 78 E------PGGLVSNYLhDNVKVGDVLEVSAPAGDFVLD---------EASDRPLV-------LISAGVGITPMLSMLEAL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 201 LKDPNDHTVcYLLFANQSEKDILLRPELEELRNEHSS-RFKLWYTvdkAPDAWDY-----SQGFVNEEMIRDHLPPPGEE 274
Cdd:cd06184 136 AAEGPGRPV-TFIHAARNSAVHAFRDELEELAARLPNlKLHVFYS---EPEAGDReedydHAGRIDLALLRELLLPADAD 211
|
250 260
....*....|....*....|....*....
gi 564361154 275 tlILMCGPPPMIQfACLPNLERVGHPKER 303
Cdd:cd06184 212 --FYLCGPVPFMQ-AVREGLKALGVPAER 237
|
|
| BenDO_FAD_NAD |
cd06209 |
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ... |
57-286 |
1.21e-22 |
|
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. As a Class I bacterial dioxygenases, benzoate dioxygenase like proteins combine an [2Fe-2S] cluster containing N-terminal ferredoxin at the end fused to an FAD/NADP(P) domain. In dioxygenase FAD/NAD(P) binding domain, the reductase transfers 2 electrons from NAD(P)H to the oxygenase which insert into an aromatic substrate, an initial step in microbial aerobic degradation of aromatic rings. Flavin oxidoreductases use flavins as substrates, unlike flavoenzymes which have a flavin prosthetic group.
Pssm-ID: 99805 [Multi-domain] Cd Length: 228 Bit Score: 93.81 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 57 EIISHDTRRFRFALPSPQHILGLPiGQhiYLSTRIDGNLVIRPYTPvSSDDDKGFVDLVVKvyfkdthpKFPaGGKMSQY 136
Cdd:cd06209 10 ERLSDSTIGLTLELDEAGALAFLP-GQ--YVNLQVPGTDETRSYSF-SSAPGDPRLEFLIR--------LLP-GGAMSSY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 137 LENM-NIGDTIEFRGPngllvyqgKGKFAIRadkksnPVVRTVKsvgMIAGGTGITPMLQVIRAVLKDPNDHTVcYLLFA 215
Cdd:cd06209 77 LRDRaQPGDRLTLTGP--------LGSFYLR------EVKRPLL---MLAGGTGLAPFLSMLDVLAEDGSAHPV-HLVYG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564361154 216 NQSEKDILLRPELEELRnEHSSRFKLWYTVDkAPDAWDYSQGFVNEEMIRDHLppPGEETLILMCGPPPMI 286
Cdd:cd06209 139 VTRDADLVELDRLEALA-ERLPGFSFRTVVA-DPDSWHPRKGYVTDHLEAEDL--NDGDVDVYLCGPPPMV 205
|
|
| FNR_iron_sulfur_binding_2 |
cd06216 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
52-287 |
1.24e-22 |
|
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99812 [Multi-domain] Cd Length: 243 Bit Score: 94.21 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 52 RLIDKEIISHDTRRFRFAlPSPQHILGLPiGQHIYLSTRIDGNLVIRPYTPVSSDDDK-GFVDLVVKvyfkdTHPkfpaG 130
Cdd:cd06216 21 RVVAVRPETADMVTLTLR-PNRGWPGHRA-GQHVRLGVEIDGVRHWRSYSLSSSPTQEdGTITLTVK-----AQP----D 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 131 GKMSQYL-ENMNIGDTIEFRGPngllvyqgKGKFAIrADKKSNPVVrtvksvgMIAGGTGITPMLQVIRAVLKDPNDHTV 209
Cdd:cd06216 90 GLVSNWLvNHLAPGDVVELSQP--------QGDFVL-PDPLPPRLL-------LIAAGSGITPVMSMLRTLLARGPTADV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564361154 210 cYLLFANQSEKDILLRPELEELRNEHSS-RFKLWYTVDKApdawdysQGFVNEEMIrDHLPPPGEETLILMCGPPPMIQ 287
Cdd:cd06216 154 -VLLYYARTREDVIFADELRALAAQHPNlRLHLLYTREEL-------DGRLSAAHL-DAVVPDLADRQVYACGPPGFLD 223
|
|
| T4MO_e_transfer_like |
cd06190 |
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ... |
53-287 |
1.83e-22 |
|
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates toluene and forms p-cresol as part of a three component toluene-4-monoxygenase system. Electron transfer is from NADH to an NADH:ferredoxin oxidoreductase (TmoF in P. mendocina) to ferredoxin to an iron-containing oxygenase. TmoF is homologous to other mono- and dioxygenase systems within the ferredoxin reductase family.
Pssm-ID: 99787 Cd Length: 232 Bit Score: 93.47 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 53 LIDKEIISHDTRRFRFALPSPQHILglPiGQHIYLStrIDGNLVIRPYTPVSSDDDKGFVDLVVKvyfkdthpKFPaGGK 132
Cdd:cd06190 1 LVDVRELTHDVAEFRFALDGPADFL--P-GQYALLA--LPGVEGARAYSMANLANASGEWEFIIK--------RKP-GGA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 133 MSQYL-ENMNIGDTIEFRGPNGLLVyqgkgkfaIRADKKSNPVvrtvksvgMIAGGTGITPMLQVIRAVLKDPN--DHTV 209
Cdd:cd06190 67 ASNALfDNLEPGDELELDGPYGLAY--------LRPDEDRDIV--------CIAGGSGLAPMLSILRGAARSPYlsDRPV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 210 cYLLFANQSEKDILLRPELEELRnEHSSRFKLWYTVDKAPDA----WDYSQGFVNEEmIRDHLPPPGEETLILMCGPPPM 285
Cdd:cd06190 131 -DLFYGGRTPSDLCALDELSALV-ALGARLRVTPAVSDAGSGsaagWDGPTGFVHEV-VEATLGDRLAEFEFYFAGPPPM 207
|
..
gi 564361154 286 IQ 287
Cdd:cd06190 208 VD 209
|
|
| monooxygenase_like |
cd06212 |
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
57-305 |
1.56e-20 |
|
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. These flavoprotein monooxygenases use molecular oxygen as a substrate and require reduced FAD. One atom of oxygen is incorportated into the aromatic compond, while the other is used to form a molecule of water. In contrast dioxygenases add both atoms of oxygen to the substrate.
Pssm-ID: 99808 [Multi-domain] Cd Length: 232 Bit Score: 88.16 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 57 EIISHDTRRFRFALPSPQHILGLPiGQhiYLSTRIDGNLVIRPYTPVSSDDDKGFVDLVVKVYfkdthpkfpAGGKMSQY 136
Cdd:cd06212 9 EALTHDIRRLRLRLEEPEPIKFFA-GQ--YVDITVPGTEETRSFSMANTPADPGRLEFIIKKY---------PGGLFSSF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 137 LEN-MNIGDTIEFRGPngllvYqgkGKFAIRaDKKSNPVVrtvksvgMIAGGTGITPMLQVIRAVLKDPNDHTVCYLlFA 215
Cdd:cd06212 77 LDDgLAVGDPVTVTGP-----Y---GTCTLR-ESRDRPIV-------LIGGGSGMAPLLSLLRDMAASGSDRPVRFF-YG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 216 NQSEKDILLRPELEELRNEHSSrFKLWYTVDKAPD--AWDYSQGFVNEeMIRDHLPPPgEETLILMCGPPPMIQfACLPN 293
Cdd:cd06212 140 ARTARDLFYLEEIAALGEKIPD-FTFIPALSESPDdeGWSGETGLVTE-VVQRNEATL-AGCDVYLCGPPPMID-AALPV 215
|
250
....*....|..
gi 564361154 294 LERVGHPKERCF 305
Cdd:cd06212 216 LEMSGVPPDQIF 227
|
|
| FNR_iron_sulfur_binding |
cd06191 |
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
51-303 |
1.34e-19 |
|
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with a C-terminal iron-sulfur binding cluster domain. FNR was intially identified as a chloroplast reductase activity catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methnae assimilation in a variety of organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).
Pssm-ID: 99788 [Multi-domain] Cd Length: 231 Bit Score: 85.66 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 51 LRLIDKEIISHDTRRFRFALPSPQHILGLPiGQHIYLSTRIDGNLVIRPYTpVSSDDDKGFVDLVVKvyfkdthpKFPaG 130
Cdd:cd06191 1 LRVAEVRSETPDAVTIVFAVPGPLQYGFRP-GQHVTLKLDFDGEELRRCYS-LCSSPAPDEISITVK--------RVP-G 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 131 GKMSQYL-ENMNIGDTIEFRGPNGLLVYQgkgkfAIRADKksnpvvrtvksVGMIAGGTGITPMLQVIRAVLKDPNDHTV 209
Cdd:cd06191 70 GRVSNYLrEHIQPGMTVEVMGPQGHFVYQ-----PQPPGR-----------YLLVAAGSGITPLMAMIRATLQTAPESDF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 210 CyLLFANQSEKDILLRPELEELRNEHsSRFKLWYTVDK-APDAWDYSQGFVNEEMIRDHLPPPGEETLILMCGPPPMIQf 288
Cdd:cd06191 134 T-LIHSARTPADMIFAQELRELADKP-QRLRLLCIFTReTLDSDLLHGRIDGEQSLGAALIPDRLEREAFICGPAGMMD- 210
|
250
....*....|....*
gi 564361154 289 ACLPNLERVGHPKER 303
Cdd:cd06191 211 AVETALKELGMPPER 225
|
|
| NADH_quinone_reductase |
cd06188 |
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ... |
96-305 |
2.27e-19 |
|
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) provides a means of storing redox reaction energy via the transmembrane translocation of Na2+ ions. The C-terminal domain resembles ferredoxin:NADP+ oxidoreductase, and has NADH and FAD binding sites. (Na+-NQR) is distinct from H+-translocating NADH:quinone oxidoreductases and noncoupled NADH:quinone oxidoreductases. The NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain of this group typically contains an iron-sulfur cluster binding domain.
Pssm-ID: 99785 [Multi-domain] Cd Length: 283 Bit Score: 85.82 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 96 VIRPYTPVSSDDDKGFVDLVVKVyfkDTHPKFPAG---GKMSQYLENMNIGDTIEFRGPngllvYqgkGKFAIRADKKsn 172
Cdd:cd06188 85 VSRAYSLANYPAEEGELKLNVRI---ATPPPGNSDippGIGSSYIFNLKPGDKVTASGP-----F---GEFFIKDTDR-- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 173 PVVrtvksvgMIAGGTGITPMLQVIRAVLKDPNDHTVCYLLFANQSEKDILLRPELEELRNEHsSRFKlWYTVDKAP--- 249
Cdd:cd06188 152 EMV-------FIGGGAGMAPLRSHIFHLLKTLKSKRKISFWYGARSLKELFYQEEFEALEKEF-PNFK-YHPVLSEPqpe 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 250 DAWDYSQGFV----NEEMIRDHLPPpgEETLILMCGPPPMIQfACLPNLERVGHPKERCF 305
Cdd:cd06188 223 DNWDGYTGFIhqvlLENYLKKHPAP--EDIEFYLCGPPPMNS-AVIKMLDDLGVPRENIA 279
|
|
| COG4097 |
COG4097 |
Predicted ferric reductase [Inorganic ion transport and metabolism]; |
24-303 |
7.79e-19 |
|
Predicted ferric reductase [Inorganic ion transport and metabolism];
Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 86.10 E-value: 7.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 24 FVYSLFMKLFQRSspaitlenpdiKYPLRLIDKEIISHDTRRFRFALPSPQHILGLPiGQHIYLstRIDGNLVIR---PY 100
Cdd:COG4097 201 AVYSRLGRPLRSR-----------RHPYRVESVEPEAGDVVELTLRPEGGRWLGHRA-GQFAFL--RFDGSPFWEeahPF 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 101 TPVSSDDDKGFVDLVVKvyfkdthpkfpAGGKMSQYLENMNIGDTIEFRGPngllvYqgkGKFAIRADKKSNPVVrtvks 180
Cdd:COG4097 267 SISSAPGGDGRLRFTIK-----------ALGDFTRRLGRLKPGTRVYVEGP-----Y---GRFTFDRRDTAPRQV----- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 181 vgMIAGGTGITPMLQVIRAVLKDPNDHTVCYLLFANQSEKDILLRPELEELRNEHSSrFKLWYTVDKApdawdysQGFVN 260
Cdd:COG4097 323 --WIAGGIGITPFLALLRALAARPGDQRPVDLFYCVRDEEDAPFLEELRALAARLAG-LRLHLVVSDE-------DGRLT 392
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 564361154 261 EEMIRDHLPPPgEETLILMCGPPPMIQfACLPNLERVGHPKER 303
Cdd:COG4097 393 AERLRRLVPDL-AEADVFFCGPPGMMD-ALRRDLRALGVPARR 433
|
|
| phenol_2-monooxygenase_like |
cd06211 |
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ... |
53-306 |
8.73e-18 |
|
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use molecular oxygen as a substrate in the microbial degredation of phenol. This protein is encoded by a single gene and uses a tightly bound FAD cofactor in the NAD(P)H dependent conversion of phenol and O2 to catechol and H2O. This group is related to the NAD binding ferredoxin reductases.
Pssm-ID: 99807 Cd Length: 238 Bit Score: 80.83 E-value: 8.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 53 LIDKEIISHDTRRFRFALPSPQHILGLPiGQhiYLSTRIDGNLVIRPYTPVSSDDDKGFVDLvvkvyfkdtHPKFPAGGK 132
Cdd:cd06211 11 VVEIEDLTPTIKGVRLKLDEPEEIEFQA-GQ--YVNLQAPGYEGTRAFSIASSPSDAGEIEL---------HIRLVPGGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 133 MSQYL-ENMNIGDTIEFRGPngllvYqgkGKFAIRaDKKSNPVVrtvksvgMIAGGTGITPmlqvIRAVLKDPNDHTV-- 209
Cdd:cd06211 79 ATTYVhKQLKEGDELEISGP-----Y---GDFFVR-DSDQRPII-------FIAGGSGLSS----PRSMILDLLERGDtr 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 210 -CYLLFANQSEKDILLRPELEELRNEHSsRFKLWYTVDKAP--DAWDYSQGFVNEeMIRDHLPPPGEETLILMCGPPPMI 286
Cdd:cd06211 139 kITLFFGARTRAELYYLDEFEALEKDHP-NFKYVPALSREPpeSNWKGFTGFVHD-AAKKHFKNDFRGHKAYLCGPPPMI 216
|
250 260
....*....|....*....|
gi 564361154 287 QfACLPNLERVGHPKERCFT 306
Cdd:cd06211 217 D-ACIKTLMQGRLFERDIYY 235
|
|
| flavin_oxioreductase |
cd06189 |
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ... |
59-305 |
2.30e-17 |
|
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron transfer from iron complexes or iron proteins. Structurally similar to ferredoxin reductases, but with only 15% sequence identity, flavin reductases reduce FAD, FMN, or riboflavin via NAD(P)H. Flavin is used as a substrate, rather than a tightly bound prosthetic group as in flavoenzymes; weaker binding is due to the absence of a binding site for the AMP moeity of FAD.
Pssm-ID: 99786 [Multi-domain] Cd Length: 224 Bit Score: 79.13 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 59 ISHDTRRFRfaLPSPQHILGLPiGQhiYLSTRIDGNlVIRPYTPVSSDDDKGFVDLVVKVYfkdthpkfpAGGKMSQY-L 137
Cdd:cd06189 9 LNDDVYRVR--LKPPAPLDFLA-GQ--YLDLLLDDG-DKRPFSIASAPHEDGEIELHIRAV---------PGGSFSDYvF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 138 ENMNIGDTIEFRGPngllvyqgKGKFAIRADKkSNPVVrtvksvgMIAGGTGITPMLQVIRAVLKDPNDHTVcYLLFANQ 217
Cdd:cd06189 74 EELKENGLVRIEGP--------LGDFFLREDS-DRPLI-------LIAGGTGFAPIKSILEHLLAQGSKRPI-HLYWGAR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 218 SEKDILLRPELEELRNEHSsrfKLWYT--VDKAPDAWDYSQGFVNEEMIRDHLPPpgEETLILMCGPPPMIQfACLPNLE 295
Cdd:cd06189 137 TEEDLYLDELLEAWAEAHP---NFTYVpvLSEPEEGWQGRTGLVHEAVLEDFPDL--SDFDVYACGSPEMVY-AARDDFV 210
|
250
....*....|
gi 564361154 296 RVGHPKERCF 305
Cdd:cd06189 211 EKGLPEENFF 220
|
|
| MMO_FAD_NAD_binding |
cd06210 |
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ... |
57-306 |
5.74e-17 |
|
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent hydroxylation of methane to methanol. This multicomponent enzyme mediates electron transfer via a hydroxylase (MMOH), a coupling protein, and a reductase which is comprised of an N-terminal [2Fe-2S] ferredoxin domain, an FAD binding subdomain, and an NADH binding subdomain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. Dioxygenases add both atom of oxygen to the substrate, while mono-oxygenases add one atom to the substrate and one atom to water.
Pssm-ID: 99806 Cd Length: 236 Bit Score: 78.54 E-value: 5.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 57 EIISHDTRRFRFAlPSPQHILGLPI----GQhiYLSTRIDGNLVIRPYTPVSSDDDKGFVDLVVKVyfkdtHPkfpaGGK 132
Cdd:cd06210 10 DRVSSNVVRLRLQ-PDDAEGAGIAAefvpGQ--FVEIEIPGTDTRRSYSLANTPNWDGRLEFLIRL-----LP----GGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 133 MSQYLEN-MNIGDTIEFRGPngllvyqgKGKFAIRADkksnpvvrTVKSVGMIAGGTGITPMLQVIR--AVLKDPNDhtv 209
Cdd:cd06210 78 FSTYLETrAKVGQRLNLRGP--------LGAFGLREN--------GLRPRWFVAGGTGLAPLLSMLRrmAEWGEPQE--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 210 CYLLFANQSEKDILLRPELEELRNEHSSrFKLWYTVDKAPDAWDYSQGFVnEEMIRDHLPPPGEETLILMCGPPPMIQFA 289
Cdd:cd06210 139 ARLFFGVNTEAELFYLDELKRLADSLPN-LTVRICVWRPGGEWEGYRGTV-VDALREDLASSDAKPDIYLCGPPGMVDAA 216
|
250
....*....|....*..
gi 564361154 290 CLPNLERvGHPKERCFT 306
Cdd:cd06210 217 FAAAREA-GVPDEQVYL 232
|
|
| BenC |
NF040810 |
benzoate 1,2-dioxygenase electron transfer component BenC; |
130-286 |
3.00e-13 |
|
benzoate 1,2-dioxygenase electron transfer component BenC;
Pssm-ID: 468751 [Multi-domain] Cd Length: 333 Bit Score: 69.08 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 130 GGKMSQYL-ENMNIGDTIEFRGPNGllvyqgkgKFAIRADKKsnPVVrtvksvgMIAGGTGITP---MLQVIRAvlkDPN 205
Cdd:NF040810 173 GGLMSSYLtERAKPGDRLSLTGPLG--------SFYLREVTR--PLL-------MLAGGTGLAPflsMLEVLAE---QGS 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 206 DHTVcYLLFANQSEKDILLRPELEELRNEHSSrFKlWYTVDKAPDAWDYSQGFVNEEMIRDHLPppGEETLILMCGPPPM 285
Cdd:NF040810 233 EQPV-HLIYGVTRDADLVEVERLEAFAARLPN-FT-FRTCVADAASAHPRKGYVTQHIEAEWLN--DGDVDVYLCGPPPM 307
|
.
gi 564361154 286 I 286
Cdd:NF040810 308 V 308
|
|
| FNR_N-term_Iron_sulfur_binding |
cd06194 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
53-286 |
3.79e-13 |
|
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an N-terminal Iron-Sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99791 [Multi-domain] Cd Length: 222 Bit Score: 67.29 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 53 LIDKEIISHDTRRFRFALPSPqhilgLPI--GQHIYLsTRIDGnlVIRPYTPVSSDDDKGFVDLVVKVYfkdthpkfpAG 130
Cdd:cd06194 1 VVSLQRLSPDVLRVRLEPDRP-----LPYlpGQYVNL-RRAGG--LARSYSPTSLPDGDNELEFHIRRK---------PN 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 131 GKMSQYL-ENMNIGDTIEFRGPNGLLVYqgkgkfaiRADKKSNPVVrtvksvgMIAGGTGITPMLQVIRAVLKDPNDHTV 209
Cdd:cd06194 64 GAFSGWLgEEARPGHALRLQGPFGQAFY--------RPEYGEGPLL-------LVGAGTGLAPLWGIARAALRQGHQGEI 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564361154 210 cYLLFANQSEKDILLRPELEELRNEHSSrFKLWYTVDKAPDawdySQGFVNEEMIRDHLPPPGEETLILMCGPPPMI 286
Cdd:cd06194 129 -RLVHGARDPDDLYLHPALLWLAREHPN-FRYIPCVSEGSQ----GDPRVRAGRIAAHLPPLTRDDVVYLCGAPSMV 199
|
|
| oxygenase_e_transfer_subunit |
cd06213 |
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
52-305 |
4.82e-13 |
|
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate while mono-oxygenases add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate.
Pssm-ID: 99809 Cd Length: 227 Bit Score: 67.34 E-value: 4.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 52 RLIDKEIISHDTRRFRFALPSPQHILGlpiGQhiYLSTRIDGNLVIRPYTPVSSDDDKGFVDLVVKvyfkdthpKFPaGG 131
Cdd:cd06213 4 TIVAQERLTHDIVRLTVQLDRPIAYKA---GQ--YAELTLPGLPAARSYSFANAPQGDGQLSFHIR--------KVP-GG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 132 KMSQYLENMN-IGDTIEFRGPNGllvyqgkgKFAIRADKksNPVVrtvksvgMIAGGTGITPmlqvIRAVLKDPNDHTV- 209
Cdd:cd06213 70 AFSGWLFGADrTGERLTVRGPFG--------DFWLRPGD--APIL-------CIAGGSGLAP----ILAILEQARAAGTk 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 210 --CYLLFANQSEKDILLRPELEELRNEHSSRFKLWYTVDKAP--DAWDYSQGFVNEEmIRDHLPPPGEETLilmCGPPPM 285
Cdd:cd06213 129 rdVTLLFGARTQRDLYALDEIAAIAARWRGRFRFIPVLSEEPadSSWKGARGLVTEH-IAEVLLAATEAYL---CGPPAM 204
|
250 260
....*....|....*....|
gi 564361154 286 IQFAcLPNLERVGHPKERCF 305
Cdd:cd06213 205 IDAA-IAVLRALGIAREHIH 223
|
|
| FNR_like_3 |
cd06198 |
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ... |
82-287 |
2.00e-12 |
|
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) domain, which varies in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.
Pssm-ID: 99795 [Multi-domain] Cd Length: 216 Bit Score: 65.36 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 82 GQHIYLstRIDGNLVIR--PYTPVSSDDDKGFVDLVVKvyfkdthpkfpAGGKMSQYL-ENMNIGDTIEFRGPngllvYq 158
Cdd:cd06198 26 GQFAFL--RFDASGWEEphPFTISSAPDPDGRLRFTIK-----------ALGDYTRRLaERLKPGTRVTVEGP-----Y- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 159 gkGKFAIRADKKsnPVVrtvksvgMIAGGTGITPMLQVIRAVLKDPNDHTVcYLLFANQSEKDILLRPELEELRNEHSSR 238
Cdd:cd06198 87 --GRFTFDDRRA--RQI-------WIAGGIGITPFLALLEALAARGDARPV-TLFYCVRDPEDAVFLDELRALAAAAGVV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564361154 239 FKLwytVDKAPDAWDYsqgfvnEEMIRDHLPPPGEETLILMCGPPPMIQ 287
Cdd:cd06198 155 LHV---IDSPSDGRLT------LEQLVRALVPDLADADVWFCGPPGMAD 194
|
|
| FNR1 |
cd06195 |
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ... |
82-290 |
4.21e-12 |
|
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99792 [Multi-domain] Cd Length: 241 Bit Score: 64.51 E-value: 4.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 82 GQHIYLSTRID-GNLVIRPYTPVSSDDDKGFVDLVVKVyfkdthpkfpAGGKMSQYLENMNIGDTIE-FRGPNGLLVyqg 159
Cdd:cd06195 28 GQFTKLGLPNDdGKLVRRAYSIASAPYEENLEFYIILV----------PDGPLTPRLFKLKPGDTIYvGKKPTGFLT--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 160 kgkfairADKKSNPvvrtvKSVGMIAGGTGITPmlqvIRAVLKDP-----NDHTVcyLLFANQSEKDILLRPELEELRNE 234
Cdd:cd06195 95 -------LDEVPPG-----KRLWLLATGTGIAP----FLSMLRDLeiwerFDKIV--LVHGVRYAEELAYQDEIEALAKQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564361154 235 HSSRFKLWYTVDKAPDAWDYSQ----GFVNEEMIRD-HLPPPGEETLILMCGPPPMIQFAC 290
Cdd:cd06195 157 YNGKFRYVPIVSREKENGALTGripdLIESGELEEHaGLPLDPETSHVMLCGNPQMIDDTQ 217
|
|
| PRK13289 |
PRK13289 |
NO-inducible flavohemoprotein; |
129-304 |
1.28e-11 |
|
NO-inducible flavohemoprotein;
Pssm-ID: 237337 [Multi-domain] Cd Length: 399 Bit Score: 64.43 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 129 AGGKMSQYL-ENMNIGDTIEFRGPNGLLVYqgkgkfairADKKSNPVVrtvksvgMIAGGTGITPMLQVIRAVLKDPNDH 207
Cdd:PRK13289 227 AGGKVSNYLhDHVNVGDVLELAAPAGDFFL---------DVASDTPVV-------LISGGVGITPMLSMLETLAAQQPKR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 208 TVCYLLFANQSEKDIlLRPELEELRNEHsSRFKL--WYT----VDKAPDAWDYsQGFVNEEMIRDHLPPPGEETLIlmCG 281
Cdd:PRK13289 291 PVHFIHAARNGGVHA-FRDEVEALAARH-PNLKAhtWYRepteQDRAGEDFDS-EGLMDLEWLEAWLPDPDADFYF--CG 365
|
170 180
....*....|....*....|...
gi 564361154 282 PPPMIQFAcLPNLERVGHPKERC 304
Cdd:PRK13289 366 PVPFMQFV-AKQLLELGVPEERI 387
|
|
| DHOD_e_trans |
cd06218 |
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ... |
54-285 |
6.19e-11 |
|
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.
Pssm-ID: 99814 [Multi-domain] Cd Length: 246 Bit Score: 61.41 E-value: 6.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 54 IDKEIISHDTRRFRFALPSPQHIlGLPiGQ--HIYLSTRIDgNLVIRPYTPVSSDDDKGFVDLVVKVYfkdthpkfpagG 131
Cdd:cd06218 2 LSNREIADDIYRLVLEAPEIAAA-AKP-GQfvMLRVPDGSD-PLLRRPISIHDVDPEEGTITLLYKVV-----------G 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 132 KMSQYLENMNIGDTIEFRGPngllvyQGKGkFAIraDKKSNPVVrtvksvgMIAGGTGITPMLQVIRAVLKDPNDHTVcY 211
Cdd:cd06218 68 KGTRLLSELKAGDELDVLGP------LGNG-FDL--PDDDGKVL-------LVGGGIGIAPLLFLAKQLAERGIKVTV-L 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564361154 212 LLFAnqSEKDILLRPELEELRNEHSsrfklWYTVDKAPDAwdysQGFVnEEMIRDHLpPPGEETLILMCGPPPM 285
Cdd:cd06218 131 LGFR--SADDLFLVEEFEALGAEVY-----VATDDGSAGT----KGFV-TDLLKELL-AEARPDVVYACGPEPM 191
|
|
| antC |
PRK11872 |
anthranilate 1,2-dioxygenase electron transfer component AntC; |
130-287 |
1.04e-10 |
|
anthranilate 1,2-dioxygenase electron transfer component AntC;
Pssm-ID: 183350 [Multi-domain] Cd Length: 340 Bit Score: 61.68 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 130 GGKMSQYL-ENMNIGDTIEFRGPngllvyqgKGKFAIRADKKsnPVVrtvksvgMIAGGTGITPMLQVIRAVLKDPNDHT 208
Cdd:PRK11872 177 DGVMSNYLrERCQVGDEILFEAP--------LGAFYLREVER--PLV-------FVAGGTGLSAFLGMLDELAEQGCSPP 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 209 VcYLLFANQSEKDILlrpELEELRNeHSSR---FKLWYTVDKAPDAWDYSQGFVNEEMIRDHLppPGEETLILMCGPPPM 285
Cdd:PRK11872 240 V-HLYYGVRHAADLC---ELQRLAA-YAERlpnFRYHPVVSKASADWQGKRGYIHEHFDKAQL--RDQAFDMYLCGPPPM 312
|
..
gi 564361154 286 IQ 287
Cdd:PRK11872 313 VE 314
|
|
| PRK08345 |
PRK08345 |
cytochrome-c3 hydrogenase subunit gamma; Provisional |
44-305 |
1.34e-10 |
|
cytochrome-c3 hydrogenase subunit gamma; Provisional
Pssm-ID: 236247 [Multi-domain] Cd Length: 289 Bit Score: 60.98 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 44 NPDIKYPLRLID-KEIISHDTR-RFRFALPSPQHILGLPIGQHIYLSTRIDGNLvirPYTPVSSDDDKGFVDLVVKvyfk 121
Cdd:PRK08345 1 NPYALHDAKILEvYDLTEREKLfLLRFEDPELAESFTFKPGQFVQVTIPGVGEV---PISICSSPTRKGFFELCIR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 122 dthpkfpAGGKMSQYLENMNIGDTIEFRGP--NGLLVYQGKGKFAIradkksnpvvrtvksvgMIAGGTGITPMLQVIRA 199
Cdd:PRK08345 74 -------RAGRVTTVIHRLKEGDIVGVRGPygNGFPVDEMEGMDLL-----------------LIAGGLGMAPLRSVLLY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 200 VLKDPNDHTVCYLLFANQSEKDILLRPELEELRnEHSSRFKLWYTVDKAPDAWDY-----------SQGFVNEEMIRDHL 268
Cdd:PRK08345 130 AMDNRWKYGNITLIYGAKYYEDLLFYDELIKDL-AEAENVKIIQSVTRDPEWPGChglpqgfiervCKGVVTDLFREANT 208
|
250 260 270
....*....|....*....|....*....|....*..
gi 564361154 269 PPpgEETLILMCGPPPMIQFAcLPNLERVGHPKERCF 305
Cdd:PRK08345 209 DP--KNTYAAICGPPVMYKFV-FKELINRGYRPERIY 242
|
|
| PDR_like |
cd06185 |
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ... |
55-303 |
1.64e-10 |
|
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron transfer from NADH to FMN to an iron sulfur cluster. PDR has an an N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding domain and a C-terminal iron-sulfur [2Fe-2S] cluster domain. Although structurally homologous to FNR, PDR binds FMN rather than FAD in it's FNR-like domain. Electron transfer between pyrimidines and iron-sulfur clusters (Rieske center [2Fe-2S]) or heme groups is mediated by flavins in respiration, photosynthesis, and oxygenase systems. Type I dioxygenase systems, including the hydroxylate phthalate system, have 2 components, a monomeric reductase consisting of a flavin and a 2Fe-2S center and a multimeric oxygenase. In contrast to other Rieske dioxygenases the ferredoxin like domain is C-, not N-terminal.
Pssm-ID: 99782 [Multi-domain] Cd Length: 211 Bit Score: 59.80 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 55 DKEIISHDTRRFRFALPSPQhilGLPI---GQHIYLSTridGNLVIRPYTPVSSDDDKGFVDLVVKvyfKDthpkfPAGG 131
Cdd:cd06185 2 RIRDEAPDIRSFELEAPDGA---PLPAfepGAHIDVHL---PNGLVRQYSLCGDPADRDRYRIAVL---RE-----PASR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 132 KMSQYL-ENMNIGDTIEFRGPNGLlvyqgkgkFAIRADKKsnpvvRTVksvgMIAGGTGITPMLQVIRAVLKDPNDHTvc 210
Cdd:cd06185 68 GGSRYMhELLRVGDELEVSAPRNL--------FPLDEAAR-----RHL----LIAGGIGITPILSMARALAARGADFE-- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 211 yLLFANQSEKDIllrPELEELRNEHSSRFKLWY-TVDKAPDawdysqgfvneemIRDHLPPPGEETLILMCGPPPMIQfA 289
Cdd:cd06185 129 -LHYAGRSREDA---AFLDELAALPGDRVHLHFdDEGGRLD-------------LAALLAAPPAGTHVYVCGPEGMMD-A 190
|
250
....*....|....
gi 564361154 290 CLPNLERVGHPKER 303
Cdd:cd06185 191 VRAAAAALGWPEAR 204
|
|
| DHOD_e_trans_like |
cd06192 |
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ... |
53-289 |
1.22e-09 |
|
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.
Pssm-ID: 99789 [Multi-domain] Cd Length: 243 Bit Score: 57.72 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 53 LIDKEIISHDTRRFRFAlpSPQHILGLPIGQHIYLSTRIDGNLVIRPYTPVSSDDDKGFVDLVVKVyfkdthpkfpaGGK 132
Cdd:cd06192 1 IVKKEQLEPNLVLLTIK--APLAARLFRPGQFVFLRNFESPGLERIPLSLAGVDPEEGTISLLVEI-----------RGP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 133 MSQYLENMNIGDTIEFRGP--NGLLVYQGKGKFAIradkksnpvvrtvksvgmIAGGTGITPMLQVIRAVLKDPNDhtVC 210
Cdd:cd06192 68 KTKLIAELKPGEKLDVMGPlgNGFEGPKKGGTVLL------------------VAGGIGLAPLLPIAKKLAANGNK--VT 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 211 YLLFANqSEKDILLRPELEELRNEHSsrfklwYTVDKAPdawdysqgFVNEEMIRDHLPPP--GEETLILMCGPPPMIQF 288
Cdd:cd06192 128 VLAGAK-KAKEEFLDEYFELPADVEI------WTTDDGE--------LGLEGKVTDSDKPIplEDVDRIIVAGSDIMMKA 192
|
.
gi 564361154 289 A 289
Cdd:cd06192 193 V 193
|
|
| PRK07609 |
PRK07609 |
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated |
48-286 |
8.01e-08 |
|
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
Pssm-ID: 181058 [Multi-domain] Cd Length: 339 Bit Score: 52.95 E-value: 8.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 48 KYPLRLIDKEIISHDTRRFRFALPSPQHILGLPiGQHIYLSTRiDGnlVIRPYTPVSSDDDKGFVDLVVKVYfkdthpkf 127
Cdd:PRK07609 102 KLPCRVASLERVAGDVMRLKLRLPATERLQYLA-GQYIEFILK-DG--KRRSYSIANAPHSGGPLELHIRHM-------- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 128 pAGGKMSQYL-ENMNIGDTIEFRGPngllvyqgKGKFAIRADkKSNPVVrtvksvgMIAGGTGITPMLQVIRAVLKDPND 206
Cdd:PRK07609 170 -PGGVFTDHVfGALKERDILRIEGP--------LGTFFLRED-SDKPIV-------LLASGTGFAPIKSIVEHLRAKGIQ 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 207 HTVcYLLFANQSEKDiLLRPELEELRNEHSSRFKLWYTVDKA--PDAWDYSQGFVNEEMIRDHlpPPGEETLILMCGPPP 284
Cdd:PRK07609 233 RPV-TLYWGARRPED-LYLSALAEQWAEELPNFRYVPVVSDAldDDAWTGRTGFVHQAVLEDF--PDLSGHQVYACGSPV 308
|
..
gi 564361154 285 MI 286
Cdd:PRK07609 309 MV 310
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
82-291 |
1.99e-07 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 52.53 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 82 GQHIYLSTRIDGNLVirPYTPVSSDDDKGFVDLVVKvyfkdthpkfpAGGKMSQYLENMNIGDTieFRGPNGLLvyqGKG 161
Cdd:PRK12779 680 GQFVRVLPWEKGELI--PLTLADWDAEKGTIDLVVQ-----------GMGTSSLEINRMAIGDA--FSGIAGPL---GRA 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 162 KFAIRADKKsnpvvrtvKSVGMIAGGTGITPMLQVIRAVLKDPNDHTvcylLFANQSEKDILL---RPE-LEELRNEHSS 237
Cdd:PRK12779 742 SELHRYEGN--------QTVVFCAGGVGLPPVYPIMRAHLRLGNHVT----LISGFRAKEFLFwtgDDErVGKLKAEFGD 809
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564361154 238 RFKLWYTVDkapDAWDYSQGFVN---EEMIRDHLPPPGEETL-ILMCGPPPMIQFACL 291
Cdd:PRK12779 810 QLDVIYTTN---DGSFGVKGFVTgplEEMLKANQQGKGRTIAeVIAIGPPLMMRAVSD 864
|
|
| SiR_like2 |
cd06201 |
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ... |
93-235 |
1.70e-06 |
|
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99798 [Multi-domain] Cd Length: 289 Bit Score: 48.48 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 93 GNLVIRPYTPVSSDDDkGFVDLVVKvyfkdTHPkfpaGGKMSQYLENMNIGDTIE-FRGPNGllvyqgkgkfAIRADKKS 171
Cdd:cd06201 96 GSDVPRFYSLASSSSD-GFLEICVR-----KHP----GGLCSGYLHGLKPGDTIKaFIRPNP----------SFRPAKGA 155
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564361154 172 NPVVrtvksvgMIAGGTGITPMLQVIRAvlkdpND-HTVCYLLF-ANQSEKDILLRPELEELRNEH 235
Cdd:cd06201 156 APVI-------LIGAGTGIAPLAGFIRA-----NAaRRPMHLYWgGRDPASDFLYEDELDQYLADG 209
|
|
| PRK06222 |
PRK06222 |
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein; |
99-291 |
2.74e-06 |
|
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;
Pssm-ID: 235747 [Multi-domain] Cd Length: 281 Bit Score: 47.87 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 99 PYTPVSSDDDKGFVDLVVKVYfkdthpkfpagGKMSQYLENMNIGDTIE-FRGPNGllvyqgkgkfairadkksNPV-VR 176
Cdd:PRK06222 46 PLTIADYDREKGTITIVFQAV-----------GKSTRKLAELKEGDSILdVVGPLG------------------KPSeIE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 177 TVKSVGMIAGGTGITPMLQVIRAvLKDPNDHTVCYLLFANqsEKDILLRPELEELRNEhssrfkLWYTVDkapdawDYS- 255
Cdd:PRK06222 97 KFGTVVCVGGGVGIAPVYPIAKA-LKEAGNKVITIIGARN--KDLLILEDEMKAVSDE------LYVTTD------DGSy 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 564361154 256 --QGFVNE---EMIRDHLPPpgeeTLILMCGPPPMIQFACL 291
Cdd:PRK06222 162 grKGFVTDvlkELLESGKKV----DRVVAIGPVIMMKFVAE 198
|
|
| PRK00054 |
PRK00054 |
dihydroorotate dehydrogenase electron transfer subunit; Reviewed |
102-285 |
5.38e-06 |
|
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
Pssm-ID: 234601 [Multi-domain] Cd Length: 250 Bit Score: 46.79 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 102 PVS-SDDDKGFVDLVVKVYfkdthpkfpagGKMSQYLENMNIGDTIEFRGPngllvyQGKGkFAIRADKksnpvvrtvKS 180
Cdd:PRK00054 52 PISiSDIDKNEITILYRKV-----------GEGTKKLSKLKEGDELDIRGP------LGNG-FDLEEIG---------GK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 181 VGMIAGGTGITPMLQVI-RAVLKDPNDHTVCYLlfanQSEKDILLRPELEELRnehssrfKLWYTVDkapdawDYS---Q 256
Cdd:PRK00054 105 VLLVGGGIGVAPLYELAkELKKKGVEVTTVLGA----RTKDEVIFEEEFAKVG-------DVYVTTD------DGSygfK 167
|
170 180
....*....|....*....|....*....
gi 564361154 257 GFVNEEMIRDHLpppgEETLILMCGPPPM 285
Cdd:PRK00054 168 GFVTDVLDELDS----EYDAIYSCGPEIM 192
|
|
| DHOD_e_trans_like1 |
cd06219 |
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ... |
99-291 |
5.63e-06 |
|
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group, as in flavoenzymes, or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD, forming FADH2 via a semiquinone intermediate, and then transfers a hydride ion to convert NADP+ to NADPH.
Pssm-ID: 99815 [Multi-domain] Cd Length: 248 Bit Score: 46.80 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 99 PYTPVSSDDDKGFVDLVVKVyfkdthpkfpaGGKMSQYLENMNIGDTIE-FRGPNGllvyqgkgkfairadkksNPV-VR 176
Cdd:cd06219 45 PLTIADWDPEKGTITIVVQV-----------VGKSTRELATLEEGDKIHdVVGPLG------------------KPSeIE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 177 TVKSVGMIAGGTGITPMLQVIRAvLKDPNDHTvcYLLFANQSEKDILLRPELEELRNEHssrfkLWYTVDKAPDawdySQ 256
Cdd:cd06219 96 NYGTVVFVGGGVGIAPIYPIAKA-LKEAGNRV--ITIIGARTKDLVILEDEFRAVSDEL-----IITTDDGSYG----EK 163
|
170 180 190
....*....|....*....|....*....|....*
gi 564361154 257 GFVNEEMiRDHLPPPGEETLILMCGPPPMIQFACL 291
Cdd:cd06219 164 GFVTDPL-KELIESGEKVDLVIAIGPPIMMKAVSE 197
|
|
| CYPOR_like_FNR |
cd06208 |
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ... |
97-285 |
6.24e-06 |
|
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but lack the FAD-binding region connecting sub-domain. Ferredoxin-NADP+ reductase (FNR) is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins, such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap between the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2, which then transfers two electrons and a proton to NADP+ to form NADPH. CYPOR serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases, sulfite reducatase, and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. CYPOR has a C-terminal FNR-like FAD and NAD binding module, an FMN-binding domain, and an additional connecting domain (inserted within the FAD binding region) that orients the FNR and FMN -binding domains. The C-terminal domain contains most of the NADP(H) binding residues, and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule, which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99804 [Multi-domain] Cd Length: 286 Bit Score: 46.93 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 97 IRPYTPVSS----DDDKGFVDLVVK--VYfkdTHPKF--PAGGKMSQYLENMNIGDTIEFRGPNGllvyqgkgKFAIRAD 168
Cdd:cd06208 64 LRLYSIASSrygdDGDGKTLSLCVKrlVY---TDPETdeTKKGVCSNYLCDLKPGDDVQITGPVG--------KTMLLPE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 169 KKSNPVVrtvksvgMIAGGTGITPMLQVIRAVL----KDPNDHTVCYLLFANQSEKDILLRPELEELRNEHSSRFKLWYT 244
Cdd:cd06208 133 DPNATLI-------MIATGTGIAPFRSFLRRLFrekhADYKFTGLAWLFFGVPNSDSLLYDDELEKYPKQYPDNFRIDYA 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564361154 245 VDKAPDAWD----YSQGFVNE--EMIRDHLppPGEETLILMCGPPPM 285
Cdd:cd06208 206 FSREQKNADggkmYVQDRIAEyaEEIWNLL--DKDNTHVYICGLKGM 250
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
52-291 |
6.29e-06 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 47.43 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 52 RLIDKEIISHDTrrFRFALPSPQHILGLPIGQHIYLSTRIDGNLVirPYTPVSSDDDKGFVDLVVKVYfkdthpkfpagG 131
Cdd:PRK12778 3 KIVEKEIFSEKV--FLLEIEAPLIAKSRKPGQFVIVRVGEKGERI--PLTIADADPEKGTITLVIQEV-----------G 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 132 KMSQYLENMNIGDTIE-FRGPNGllvyqgkgkfairadkksNPV-VRTVKSVGMIAGGTGITPMLQVIRAVLKDPNDHTV 209
Cdd:PRK12778 68 LSTTKLCELNEGDYITdVVGPLG------------------NPSeIENYGTVVCAGGGVGVAPMLPIVKALKAAGNRVIT 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 210 cylLFANQSEKDILLRPELEELRNEhssrfkLWYTVDkapDAWDYSQGFVN---EEMIRDHlpppGEETLILMCGPPPMI 286
Cdd:PRK12778 130 ---ILGGRSKELIILEDEMRESSDE------VIIMTD---DGSYGRKGLVTdglEEVIKRE----TKVDKVFAIGPAIMM 193
|
....*
gi 564361154 287 QFACL 291
Cdd:PRK12778 194 KFVCL 198
|
|
| NAD_binding_6 |
pfam08030 |
Ferric reductase NAD binding domain; |
179-287 |
1.76e-05 |
|
Ferric reductase NAD binding domain;
Pssm-ID: 429792 [Multi-domain] Cd Length: 149 Bit Score: 43.87 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 179 KSVGMIAGGTGITPMLQVIRAVLK--DPNDHTVCYLLFANQSEKDI-LLRPELEELRNEHSSRFKL--WYT-VDKAPDAW 252
Cdd:pfam08030 2 ENVLLVAGGIGITPFISILKDLGNksKKLKTKKIKFYWVVRDLSSLeWFKDVLNELEELKELNIEIhiYLTgEYEAEDAS 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564361154 253 DYSQGFVNEEMIRDHLP---------------------------PPGEETLILMCGPPPMIQ 287
Cdd:pfam08030 82 DQSDSSIRSENFDSLMNevigvdfvefhfgrpnwkevlkdiakqHPNGSIGVFSCGPPSLVD 143
|
|
| DHOD_e_trans_like2 |
cd06220 |
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ... |
131-285 |
1.78e-05 |
|
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.
Pssm-ID: 99816 [Multi-domain] Cd Length: 233 Bit Score: 44.93 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 131 GKMSQYLENMNIGDTIEFRGPngllvYqGKGkFAIRADKksnpvvrtvksVGMIAGGTGITPMLQVIRAVLKDPNDHTvc 210
Cdd:cd06220 59 GEATSALHDLKEGDKLGIRGP-----Y-GNG-FELVGGK-----------VLLIGGGIGIAPLAPLAERLKKAADVTV-- 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564361154 211 ylLFANQSEKDILLrpeLEELRNEHssrfKLWYTVDkapdawDYS---QGFVNEEMIRDHLpppGEETLILMCGPPPM 285
Cdd:cd06220 119 --LLGARTKEELLF---LDRLRKSD----ELIVTTD------DGSygfKGFVTDLLKELDL---EEYDAIYVCGPEIM 178
|
|
| NOX_Duox_like_FAD_NADP |
cd06186 |
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ... |
82-244 |
8.61e-05 |
|
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.
Pssm-ID: 99783 [Multi-domain] Cd Length: 210 Bit Score: 42.68 E-value: 8.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 82 GQHIYLS-TRIDGNLVIRPYTPVSS-DDDKGFVDLVVKVYFKDThpkfpagGKMSQYLENMNiGDTIEFR----GPngll 155
Cdd:cd06186 28 GQHVYLNfPSLLSFWQSHPFTIASSpEDEQDTLSLIIRAKKGFT-------TRLLRKALKSP-GGGVSLKvlveGP---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 156 vYQGKGKFAIRADkksnpvvrtvkSVGMIAGGTGITPMLQVIRAVLKDPNDHTVC---YLLFANQSEKDIL-LRPELEEL 231
Cdd:cd06186 96 -YGSSSEDLLSYD-----------NVLLVAGGSGITFVLPILRDLLRRSSKTSRTrrvKLVWVVRDREDLEwFLDELRAA 163
|
170
....*....|....
gi 564361154 232 RN-EHSSRFKLWYT 244
Cdd:cd06186 164 QElEVDGEIEIYVT 177
|
|
| CYPOR_like |
cd06182 |
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ... |
98-282 |
5.26e-04 |
|
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. CYPOR has a C-terminal ferredoxin reducatase (FNR)- like FAD and NAD binding module, an FMN-binding domain, and an additional conecting domain (inserted within the FAD binding region) that orients the FNR and FMN binding domains. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria and participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2, which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99779 [Multi-domain] Cd Length: 267 Bit Score: 40.78 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 98 RPYTPVSS-DDDKGFVDL-VVKVYFKDTHPKFPAGGkMSQYLENMNIGD--TIEFRGPNGLLVyqgkgkfairADKKSNP 173
Cdd:cd06182 49 RYYSIASSpDVDPGEVHLcVRVVSYEAPAGRIRKGV-CSNFLAGLQLGAkvTVFIRPAPSFRL----------PKDPTTP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 174 VVrtvksvgMIAGGTGITPM---LQVIRAVLKDPNDHTVCYLLF-ANQSEKDILLRPELEE-LRNEHSSRFKLWYTVDKA 248
Cdd:cd06182 118 II-------MVGPGTGIAPFrgfLQERAALRANGKARGPAWLFFgCRNFASDYLYREELQEaLKDGALTRLDVAFSREQA 190
|
170 180 190
....*....|....*....|....*....|....*.
gi 564361154 249 PDAwDYSQGFVNE--EMIRDHLpppGEETLILMCGP 282
Cdd:cd06182 191 EPK-VYVQDKLKEhaEELRRLL---NEGAHIYVCGD 222
|
|
| PRK05802 |
PRK05802 |
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein; |
53-209 |
1.57e-03 |
|
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;
Pssm-ID: 235613 [Multi-domain] Cd Length: 320 Bit Score: 39.58 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 53 LIDKEIISHDTRRFRFALPSPQHILGLPIGQHIYLSTRIDGNlvirpY--TPVS---SDDDKGFVDLVVKVYfkdthpkf 127
Cdd:PRK05802 69 IIKKENIEDNLIILTLKVPHKLARDLVYPGSFVFLRNKNSSS-----FfdVPISimeADTEENIIKVAIEIR-------- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361154 128 pagGKMSQYLENMNIGDTIEFRGP--NGLLVYQGkgkfaIRADKKSNPVVrtvksvgmIAGGTGITPMLQVIRAVLKDPN 205
Cdd:PRK05802 136 ---GVKTKKIAKLNKGDEILLRGPywNGILGLKN-----IKSTKNGKSLV--------IARGIGQAPGVPVIKKLYSNGN 199
|
....
gi 564361154 206 DHTV 209
Cdd:PRK05802 200 KIIV 203
|
|
| |
