|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02252 |
PLN02252 |
nitrate reductase [NADPH] |
28-305 |
3.65e-131 |
|
nitrate reductase [NADPH]
Pssm-ID: 215141 [Multi-domain] Cd Length: 888 Bit Score: 394.04 E-value: 3.65e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 28 SPDIKYPLRLIDREIISHDTRRFRFALPSPQHILGLPVGQHIYLSARIDGNLVVRPYTPISSDDDKGFVDLVIKVYFKDT 107
Cdd:PLN02252 630 NPREKIPCRLVEKISLSHDVRLFRFALPSEDHVLGLPVGKHVFLCATINGKLCMRAYTPTSSDDEVGHFELVIKVYFKNV 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 108 HPKFPAGGKMSQYLESMQIGDTIEFRGPSGLLVYQGKGKFAIrpDKKSnpiiRTVKSVGMIAGGTglaqhvrgpagyfaG 187
Cdd:PLN02252 710 HPKFPNGGLMSQYLDSLPIGDTIDVKGPLGHIEYAGRGSFLV--NGKP----KFAKKLAMLAGGT--------------G 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 188 ITPMLQVIRAIMKDPDDHTVCHLLFANQTEKDILLRPELEELRNKHSARFKLWYTLDR-APEAWDYGQGFVNEEMIRDHL 266
Cdd:PLN02252 770 ITPMYQVIQAILRDPEDKTEMSLVYANRTEDDILLREELDRWAAEHPDRLKVWYVVSQvKREGWKYSVGRVTEAMLREHL 849
|
250 260 270
....*....|....*....|....*....|....*....
gi 119593675 267 PPPEEEPLVLMCGPPPMIQYACLPNLDHVGHPTERCFVF 305
Cdd:PLN02252 850 PEGGDETLALMCGPPPMIEFACQPNLEKMGYDKDSILVF 888
|
|
| cyt_b5_reduct_like |
cd06183 |
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ... |
35-305 |
5.30e-123 |
|
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: 351.48 E-value: 5.30e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 35 LRLIDREIISHDTRRFRFALPSPQHILGLPVGQHIYLSARIDGNLVVRPYTPISSDDDKGFVDLVIKVYFkdthpkfpaG 114
Cdd:cd06183 1 FKLVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPDDGEQVVRPYTPISPDDDKGYFDLLIKIYP---------G 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 115 GKMSQYLESMQIGDTIEFRGPSGLLVYQGKGKfairpdkksnpiirtVKSVGMIAGGTGlaqhvrgpagyfagITPMLQV 194
Cdd:cd06183 72 GKMSQYLHSLKPGDTVEIRGPFGKFEYKPNGK---------------VKHIGMIAGGTG--------------ITPMLQL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 195 IRAIMKDPDDHTVCHLLFANQTEKDILLRPELEELRNKHSARFKLWYTLDRAPEAWDYGQGFVNEEMIRDHLPP-PEEEP 273
Cdd:cd06183 123 IRAILKDPEDKTKISLLYANRTEEDILLREELDELAKKHPDRFKVHYVLSRPPEGWKGGVGFITKEMIKEHLPPpPSEDT 202
|
250 260 270
....*....|....*....|....*....|..
gi 119593675 274 LVLMCGPPPMIQYACLPNLDHVGHPTERCFVF 305
Cdd:cd06183 203 LVLVCGPPPMIEGAVKGLLKELGYKKDNVFKF 234
|
|
| PTZ00319 |
PTZ00319 |
NADH-cytochrome B5 reductase; Provisional |
1-305 |
1.65e-115 |
|
NADH-cytochrome B5 reductase; Provisional
Pssm-ID: 173521 [Multi-domain] Cd Length: 300 Bit Score: 334.88 E-value: 1.65e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 1 MVLFPVWFLYSLLMKLFQRSTPAITLEsPDIKYPLRLIDREIISHDTRRFRFALPSPQHILGLPVGQHIYLSARIDGN-- 78
Cdd:PTZ00319 3 VLAVIIALGVAAFFAFMFSRSPPVALD-PDMFQHFKLIKKTEVTHDTFIFRFALHSPTQRLGLPIGQHIVFRCDCTTPgk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 79 --LVVRPYTPISSDDDKGFVDLVIKVYFKDTHPKFPAGGKMSQYLESMQIGDTIEFRGPSGLLVYQGKGKFAIRPDKKSn 156
Cdd:PTZ00319 82 peTVQHSYTPISSDDEKGYVDFLIKVYFKGVHPSFPNGGRLSQHLYHMKLGDKIEMRGPVGKFEYLGNGTYTVHKGKGG- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 157 PIIRTVKSVGMIAGGTglaqhvrgpagyfaGITPMLQVIRAIMKDPDDHTVCHLLFANQTEKDILLRPELEELRNkhSAR 236
Cdd:PTZ00319 161 LKTMHVDAFAMIAGGT--------------GITPMLQIIHAIKKNKEDRTKVFLVYANQTEDDILLRKELDEAAK--DPR 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119593675 237 FKLWYTLDR-APEAWDYGQGFVNEEMIRDHLPPP------EEEPLVLMCGPPPMIQYACLPNLDHVGHPTERCFVF 305
Cdd:PTZ00319 225 FHVWYTLDReATPEWKYGTGYVDEEMLRAHLPVPdpqnsgIKKVMALMCGPPPMLQMAVKPNLEKIGYTADNMFTF 300
|
|
| FAD_binding_6 |
pfam00970 |
Oxidoreductase FAD-binding domain; |
34-141 |
1.50e-51 |
|
Oxidoreductase FAD-binding domain;
Pssm-ID: 425968 [Multi-domain] Cd Length: 99 Bit Score: 164.68 E-value: 1.50e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 34 PLRLIDREIISHDTRRFRFALPSPQHILGLPVGQHIYLSARIDGNLVVRPYTPISSDDDKGFVDLVIKVYfkdthpkfpA 113
Cdd:pfam00970 1 PLTLVEKELVSHDTRIFRFALPHPDQVLGLPVGQHLFLRLPIDGELVIRSYTPISSDDDKGYLELLVKVY---------P 71
|
90 100
....*....|....*....|....*...
gi 119593675 114 GGKMSQYLESMQIGDTIEFRGPSGLLVY 141
Cdd:pfam00970 72 GGKMSQYLDELKIGDTIDFKGPLGRFEY 99
|
|
| FNR_like |
cd00322 |
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
41-304 |
2.89e-47 |
|
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: 157.99 E-value: 2.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 41 EIISHDTRRFRFALPSPQHILGlpvGQHIYLSARIDGNLVVRPYTPISSDDDKGFVDLVIKVYFkdthpkfpaGGKMSQY 120
Cdd:cd00322 4 EDVTDDVRLFRLQLPNGFSFKP---GQYVDLHLPGDGRGLRRAYSIASSPDEEGELELTVKIVP---------GGPFSAW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 121 LESMQIGDTIEFRGPSGllvyqgkgkFAIRPDKKSNPIIrtvksvgMIAGGTglaqhvrgpagyfaGITPMLQVIRAIMK 200
Cdd:cd00322 72 LHDLKPGDEVEVSGPGG---------DFFLPLEESGPVV-------LIAGGI--------------GITPFRSMLRHLAA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 201 DPDDHTVcHLLFANQTEKDILLRPELEELRNKHsARFKLWYTLDRAPEAWDYGQGFVNEEMIRDHLPPPEEEPLVLMCGP 280
Cdd:cd00322 122 DKPGGEI-TLLYGARTPADLLFLDELEELAKEG-PNFRLVLALSRESEAKLGPGGRIDREAEILALLPDDSGALVYICGP 199
|
250 260
....*....|....*....|....
gi 119593675 281 PPMIQyACLPNLDHVGHPTERCFV 304
Cdd:cd00322 200 PAMAK-AVREALVSLGVPEERIHT 222
|
|
| NAD_binding_1 |
pfam00175 |
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ... |
167-288 |
4.19e-47 |
|
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: 153.95 E-value: 4.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 167 MIAGGTGlaqhvrgpagyfagITPMLQVIRAIMKDPDDHTVCHLLFANQTEKDILLRPELEELRNKHSARFKLWYTLDRA 246
Cdd:pfam00175 1 MIAGGTG--------------IAPVRSMLRAILEDPKDPTQVVLVFGNRNEDDILYREELDELAEKHPGRLTVVYVVSRP 66
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 119593675 247 PEAWDYGQGFVNEEMIRDHLPPPEEEPLVLMCGPPPMIQYAC 288
Cdd:pfam00175 67 EAGWTGGKGRVQDALLEDHLSLPDEETHVYVCGPPGMIKAVR 108
|
|
| Fpr |
COG1018 |
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
33-304 |
2.43e-38 |
|
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 135.30 E-value: 2.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 33 YPLRLIDREIISHDTRRFRFALPSPQHILG-LPvGQHIYLSARIDGNLVVRPYTpISSDDDKGFVDL-VIKVyfkdthpk 110
Cdd:COG1018 4 RPLRVVEVRRETPDVVSFTLEPPDGAPLPRfRP-GQFVTLRLPIDGKPLRRAYS-LSSAPGDGRLEItVKRV-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 111 fpAGGKMSQYL-ESMQIGDTIEFRGPSGLLVYQGKGKfairpdkksnpiirtvKSVGMIAGGTglaqhvrgpagyfaGIT 189
Cdd:COG1018 74 --PGGGGSNWLhDHLKVGDTLEVSGPRGDFVLDPEPA----------------RPLLLIAGGI--------------GIT 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 190 PMLQVIRAIMKDPDDHTVcHLLFANQTEKDILLRPELEELRNKHsARFKLWYTLDRAPEAWdygQGFVNEEMIRDHLPPP 269
Cdd:COG1018 122 PFLSMLRTLLARGPFRPV-TLVYGARSPADLAFRDELEALAARH-PRLRLHPVLSREPAGL---QGRLDAELLAALLPDP 196
|
250 260 270
....*....|....*....|....*....|....*
gi 119593675 270 eEEPLVLMCGPPPMIQyACLPNLDHVGHPTERCFV 304
Cdd:COG1018 197 -ADAHVYLCGPPPMME-AVRAALAELGVPEERIHF 229
|
|
| PTZ00274 |
PTZ00274 |
cytochrome b5 reductase; Provisional |
34-286 |
5.34e-36 |
|
cytochrome b5 reductase; Provisional
Pssm-ID: 140300 Cd Length: 325 Bit Score: 131.58 E-value: 5.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 34 PLRLIDREIISHDTRRFRFALPSPQHILGLPVG--QHIYLSARIDGNLVVRPYTPISSDDDKGFVDLVIKVyfkdthpkf 111
Cdd:PTZ00274 54 PYQLGEVIPITHDTALFRFLLHSEEEFNLKPCStlQACYKYGVQPMDQCQRFYTPVTANHTKGYFDIIVKR--------- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 112 PAGGKMSQYLESMQIGDTIEFRGPSGLLVYqgkgkfaiRPDKksnpiirtVKSVGMIAGGTGLaqhvrgpagyfagiTPM 191
Cdd:PTZ00274 125 KKDGLMTNHLFGMHVGDKLLFRSVTFKIQY--------RPNR--------WKHVGMIAGGTGF--------------TPM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 192 LQVIRAIMKDP-----DDHTVCHLLFANQTEKDILLRPELEELRNKHSARFKLWYTLDRA--PEAWDYGQGFVNEEMIRD 264
Cdd:PTZ00274 175 LQIIRHSLTEPwdsgeVDRTKLSFLFCNRTERHILLKGLFDDLARRYSNRFKVYYTIDQAvePDKWNHFLGYVTKEMVRR 254
|
250 260
....*....|....*....|...
gi 119593675 265 HLPPPEEE-PLVLMCGPPPMIQY 286
Cdd:PTZ00274 255 TMPAPEEKkKIIMLCGPDQLLNH 277
|
|
| PTZ00306 |
PTZ00306 |
NADH-dependent fumarate reductase; Provisional |
47-283 |
5.16e-34 |
|
NADH-dependent fumarate reductase; Provisional
Pssm-ID: 140327 [Multi-domain] Cd Length: 1167 Bit Score: 131.44 E-value: 5.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 47 TRRFRFALPSPQHILGLPVGQHIYLSARIDGNLVVRPYTPISSDDDKGFVDLVIKvyfKDThpkfpagGKMSQYLESMQI 126
Cdd:PTZ00306 932 SRVLRFNLPGALQRSGLTLGQFIAIRGDWDGQQLIGYYSPITLPDDLGVISILAR---GDK-------GTLKEWISALRP 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 127 GDTIEFRGPSGLLVYQgkgkfaiRPDKK----SNPIIRtvkSVGMIAGGTGLAqhvrgpagyfagitPMLQVIRAIMKDP 202
Cdd:PTZ00306 1002 GDSVEMKACGGLRIER-------RPADKqfvfRGHVIR---KLALIAGGTGVA--------------PMLQIIRAALKKP 1057
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 203 --DDHTVCHLLFANQTEKDILLRPELEELRNKHSARFKLWYTLDRAPEAWDYGQGFVNEEMIRDHLPPPEEEPLVLMCGP 280
Cdd:PTZ00306 1058 yvDSIESIRLIYAAEDVSELTYRELLESYRKENPGKFKCHFVLNNPPEGWTDGVGFVDRALLQSALQPPSKDLLVAICGP 1137
|
...
gi 119593675 281 PPM 283
Cdd:PTZ00306 1138 PVM 1140
|
|
| PA_degradation_oxidoreductase_like |
cd06214 |
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ... |
33-301 |
4.39e-32 |
|
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: 119.19 E-value: 4.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 33 YPLRLIDREIISHDTRRFRFALPSP-QHILGLPVGQHIYLSARIDGNLVVRPYTpISSDDDKGFVDLVIK-Vyfkdthpk 110
Cdd:cd06214 2 HPLTVAEVVRETADAVSITFDVPEElRDAFRYRPGQFLTLRVPIDGEEVRRSYS-ICSSPGDDELRITVKrV-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 111 fpAGGKMSQYL-ESMQIGDTIEFRGPSGllvyqgkgKFAIRPDKKSNPIIrtvksvgMIAGGTGlaqhvrgpagyfagIT 189
Cdd:cd06214 73 --PGGRFSNWAnDELKAGDTLEVMPPAG--------RFTLPPLPGARHYV-------LFAAGSG--------------IT 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 190 PMLQVIRAIMKDPDDHTVcHLLFANQTEKDILLRPELEELRNKHSARFKLWYTLDRAPEAWDYGQGFVNEEMIR---DHL 266
Cdd:cd06214 122 PVLSILKTALAREPASRV-TLVYGNRTEASVIFREELADLKARYPDRLTVIHVLSREQGDPDLLRGRLDAAKLNallKNL 200
|
250 260 270
....*....|....*....|....*....|....*
gi 119593675 267 PPPEEEPLVLMCGPPPMIQyACLPNLDHVGHPTER 301
Cdd:cd06214 201 LDATEFDEAFLCGPEPMMD-AVEAALLELGVPAER 234
|
|
| FNR_iron_sulfur_binding_3 |
cd06217 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
40-301 |
2.85e-30 |
|
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: 114.29 E-value: 2.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 40 REII--SHDTRRFRFALPSPQHILGLPvGQHIYLSAR-IDGNLVVRPYTPISSDDDKGFVDLVIKVYfkdthpkfpAGGK 116
Cdd:cd06217 7 TEIIqeTPTVKTFRLAVPDGVPPPFLA-GQHVDLRLTaIDGYTAQRSYSIASSPTQRGRVELTVKRV---------PGGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 117 MSQYL-ESMQIGDTIEFRGPSgllvyqgkGKFAIRPdkksnpiiRTVKSVGMIAGGTglaqhvrgpagyfaGITPMLQVI 195
Cdd:cd06217 77 VSPYLhDEVKVGDLLEVRGPI--------GTFTWNP--------LHGDPVVLLAGGS--------------GIVPLMSMI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 196 RAImKDPDDHTVCHLLFANQTEKDILLRPELEELRNKHSArFKLWYTLDR-APEAWDYGQGFVNEEMIrDHLPPPEEEPL 274
Cdd:cd06217 127 RYR-RDLGWPVPFRLLYSARTAEDVIFRDELEQLARRHPN-LHVTEALTRaAPADWLGPAGRITADLI-AELVPPLAGRR 203
|
250 260
....*....|....*....|....*..
gi 119593675 275 VLMCGPPPMIQYaCLPNLDHVGHPTER 301
Cdd:cd06217 204 VYVCGPPAFVEA-ATRLLLELGVPRDR 229
|
|
| FNR_iron_sulfur_binding_1 |
cd06215 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
35-303 |
7.46e-30 |
|
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: 113.07 E-value: 7.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 35 LRLIDREIISHDTRRFRFALPSPQHILGLPvGQHIYLSARIDGNLVVRPYTPISSDDDKGFVDLVIKVYfkdthpkfpAG 114
Cdd:cd06215 1 LRCVKIIQETPDVKTFRFAAPDGSLFAYKP-GQFLTLELEIDGETVYRAYTLSSSPSRPDSLSITVKRV---------PG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 115 GKMSQYL-ESMQIGDTIEFRGPSgllvyqgkGKFAIRPDKKSNPIirtvksvgMIAGGTglaqhvrgpagyfaGITPMLQ 193
Cdd:cd06215 71 GLVSNWLhDNLKVGDELWASGPA--------GEFTLIDHPADKLL--------LLSAGS--------------GITPMMS 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 194 VIRAIMKDPDDHTVcHLLFANQTEKDILLRPELEELRNKHSArFKLWYTL-DRAPEAWDYGQGFVNEEMIRDhLPPPEEE 272
Cdd:cd06215 121 MARWLLDTRPDADI-VFIHSARSPADIIFADELEELARRHPN-FRLHLILeQPAPGAWGGYRGRLNAELLAL-LVPDLKE 197
|
250 260 270
....*....|....*....|....*....|.
gi 119593675 273 PLVLMCGPPPMIQYACLpNLDHVGHPTERCF 303
Cdd:cd06215 198 RTVFVCGPAGFMKAVKS-LLAELGFPMSRFH 227
|
|
| Mcr1 |
COG0543 |
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
36-304 |
2.49e-29 |
|
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];
Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 111.88 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 36 RLIDREIISHDTRRFRFALPsPQHILGLPvGQhiYLSARIDGNLVVRPYTPISSDDDKGFVDLVIKVYfkdthpkfpagG 115
Cdd:COG0543 1 KVVSVERLAPDVYLLRLEAP-LIALKFKP-GQ--FVMLRVPGDGLRRPFSIASAPREDGTIELHIRVV-----------G 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 116 KMSQYLESMQIGDTIEFRGPsgllvyQGKGkFAIRPDKKsnPIIrtvksvgMIAGGTGLAqhvrgpagyfagitPMLQVI 195
Cdd:COG0543 66 KGTRALAELKPGDELDVRGP------LGNG-FPLEDSGR--PVL-------LVAGGTGLA--------------PLRSLA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 196 RAIMKDPDDhtvCHLLFANQTEKDILLRPELEELRNkhsarFKLWYTLDrapEAWDYGQGFVNEEMIRDHlpPPEEEPLV 275
Cdd:COG0543 116 EALLARGRR---VTLYLGARTPEDLYLLDELEALAD-----FRVVVTTD---DGWYGRKGFVTDALKELL--AEDSGDDV 182
|
250 260
....*....|....*....|....*....
gi 119593675 276 LMCGPPPMIqYACLPNLDHVGHPTERCFV 304
Cdd:COG0543 183 YACGPPPMM-KAVAELLLERGVPPERIYV 210
|
|
| FNR_like_1 |
cd06196 |
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ... |
33-284 |
1.34e-23 |
|
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: 96.16 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 33 YPLRLIDREIISHDTRRFRFALPspqHILGLPVGQHIYLSARIDG-NLVVRPYTPISSDDDKgFVDLVIKVYfkdthpkf 111
Cdd:cd06196 1 HTVTLLSIEPVTHDVKRLRFDKP---EGYDFTPGQATEVAIDKPGwRDEKRPFTFTSLPEDD-VLEFVIKSY-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 112 PAGGKMSQYLESMQIGDTIEFRGPSGLLVYQGKGKFairpdkksnpiirtvksvgmIAGGtglaqhvrgpagyfAGITPM 191
Cdd:cd06196 69 PDHDGVTEQLGRLQPGDTLLIEDPWGAIEYKGPGVF--------------------IAGG--------------AGITPF 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 192 LQVIRAIMKDP--DDHtvcHLLFANQTEKDILLRPELEELRNKhsarfKLWYTLDRAP-EAWDYGQgfVNEEMIRDHLPP 268
Cdd:cd06196 115 IAILRDLAAKGklEGN---TLIFANKTEKDIILKDELEKMLGL-----KFINVVTDEKdPGYAHGR--IDKAFLKQHVTD 184
|
250
....*....|....*.
gi 119593675 269 PEEEPLVlmCGPPPMI 284
Cdd:cd06196 185 FNQHFYV--CGPPPME 198
|
|
| BenDO_FAD_NAD |
cd06209 |
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ... |
41-298 |
1.46e-23 |
|
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: 96.12 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 41 EIISHDTRRFRFALPSPQHILGLPvGQhiYLSARIDGNLVVRPYTPiSSDDDKGFVDLVIKvyfkdthpKFPaGGKMSQY 120
Cdd:cd06209 10 ERLSDSTIGLTLELDEAGALAFLP-GQ--YVNLQVPGTDETRSYSF-SSAPGDPRLEFLIR--------LLP-GGAMSSY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 121 LESM-QIGDTIEFRGPsgllvyqgKGKFAIRPDKKsnPIIrtvksvgMIAGGTGLAqhvrgpagyfagitPMLQVIRAIM 199
Cdd:cd06209 77 LRDRaQPGDRLTLTGP--------LGSFYLREVKR--PLL-------MLAGGTGLA--------------PFLSMLDVLA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 200 KDPDDHTVcHLLFANQTEKDILLRPELEELRNKHSaRFKLWYTLDRaPEAWDYGQGFVNEEMIRDHLPPPEEEplVLMCG 279
Cdd:cd06209 126 EDGSAHPV-HLVYGVTRDADLVELDRLEALAERLP-GFSFRTVVAD-PDSWHPRKGYVTDHLEAEDLNDGDVD--VYLCG 200
|
250
....*....|....*....
gi 119593675 280 PPPMIQyACLPNLDHVGHP 298
Cdd:cd06209 201 PPPMVD-AVRSWLDEQGIE 218
|
|
| FNR_iron_sulfur_binding_2 |
cd06216 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
36-288 |
5.13e-23 |
|
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: 94.98 E-value: 5.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 36 RLIDREIISHDTRRFRFAlPSPQHILGLPvGQHIYLSARIDGNLVVRPYTPISSDDDK-GFVDLVIKvyfkdTHPkfpaG 114
Cdd:cd06216 21 RVVAVRPETADMVTLTLR-PNRGWPGHRA-GQHVRLGVEIDGVRHWRSYSLSSSPTQEdGTITLTVK-----AQP----D 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 115 GKMSQYL-ESMQIGDTIEFRGPsgllvyqgKGKFAIrPDKKSNPIIrtvksvgMIAGGTglaqhvrgpagyfaGITPMLQ 193
Cdd:cd06216 90 GLVSNWLvNHLAPGDVVELSQP--------QGDFVL-PDPLPPRLL-------LIAAGS--------------GITPVMS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 194 VIRAIMKDPDDHTVCHLLFANQTEkDILLRPELEELRNKHSA-RFKLWYTLDRapeawdyGQGFVNEEMIrDHLPPPEEE 272
Cdd:cd06216 140 MLRTLLARGPTADVVLLYYARTRE-DVIFADELRALAAQHPNlRLHLLYTREE-------LDGRLSAAHL-DAVVPDLAD 210
|
250
....*....|....*.
gi 119593675 273 PLVLMCGPPPMIQYAC 288
Cdd:cd06216 211 RQVYACGPPGFLDAAE 226
|
|
| O2ase_reductase_like |
cd06187 |
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
43-304 |
1.01e-21 |
|
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: 91.12 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 43 ISHDTRRFRFALPSPQHILGlpvGQhiYLSARIDG-NLVVRPYTPISSDDDKGFVDLVIKVYfkdthpkfpAGGKMSQYL 121
Cdd:cd06187 7 LTHDIAVVRLQLDQPLPFWA---GQ--YVNVTVPGrPRTWRAYSPANPPNEDGEIEFHVRAV---------PGGRVSNAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 122 -ESMQIGDTIEFRGPSGllvyqgkgkFAIRPDKKSNPIIrtvksvgMIAGGTGLAqhvrgpagyfagitPMLQVIRAIMK 200
Cdd:cd06187 73 hDELKVGDRVRLSGPYG---------TFYLRRDHDRPVL-------CIAGGTGLA--------------PLRAIVEDALR 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 201 DPDDHTVcHLLFANQTEKDILLRPELEELRNKHsARFKLWYTLDRAPEAWDYGQGFVNEEMIRDHLPPpeEEPLVLMCGP 280
Cdd:cd06187 123 RGEPRPV-HLFFGARTERDLYDLEGLLALAARH-PWLRVVPVVSHEEGAWTGRRGLVTDVVGRDGPDW--ADHDIYICGP 198
|
250 260
....*....|....*....|....
gi 119593675 281 PPMIQyACLPNLDHVGHPTERCFV 304
Cdd:cd06187 199 PAMVD-ATVDALLARGAPPERIHF 221
|
|
| T4MO_e_transfer_like |
cd06190 |
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ... |
37-285 |
3.72e-21 |
|
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: 89.62 E-value: 3.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 37 LIDREIISHDTRRFRFALPSPQHILglPvGQHIYLSarIDGNLVVRPYTPISSDDDKGFVDLVIKVYfkdthpkfpAGGK 116
Cdd:cd06190 1 LVDVRELTHDVAEFRFALDGPADFL--P-GQYALLA--LPGVEGARAYSMANLANASGEWEFIIKRK---------PGGA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 117 MSQYL-ESMQIGDTIEFRGPSGLLVyqgkgkfaIRPDKKSNPIirtvksvgMIAGGTGLAqhvrgpagyfagitPMLQVI 195
Cdd:cd06190 67 ASNALfDNLEPGDELELDGPYGLAY--------LRPDEDRDIV--------CIAGGSGLA--------------PMLSIL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 196 RAIMKDP--DDHTVcHLLFANQTEKDILLRPELEELRNKhSARFKLWYTLDRAPEA----WDYGQGFVNEEmIRDHLPPP 269
Cdd:cd06190 117 RGAARSPylSDRPV-DLFYGGRTPSDLCALDELSALVAL-GARLRVTPAVSDAGSGsaagWDGPTGFVHEV-VEATLGDR 193
|
250
....*....|....*.
gi 119593675 270 EEEPLVLMCGPPPMIQ 285
Cdd:cd06190 194 LAEFEFYFAGPPPMVD 209
|
|
| sulfite_reductase_like |
cd06221 |
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ... |
86-288 |
5.77e-21 |
|
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: 89.59 E-value: 5.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 86 PIS---SDDDKGFVDLVIKvyfkdthpkfpAGGKMSQYLESMQIGDTIEFRGP--SGLLVYQGKGKfairpdkksnpiir 160
Cdd:cd06221 45 PISissDPTRRGPLELTIR-----------RVGRVTEALHELKPGDTVGLRGPfgNGFPVEEMKGK-------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 161 tvkSVGMIAGGTGLAqhvrgpagyfagitPMLQVIRAIMKDPDDHTVCHLLFANQTEKDILLRPELEELRNKHSarFKLW 240
Cdd:cd06221 100 ---DLLLVAGGLGLA--------------PLRSLINYILDNREDYGKVTLLYGARTPEDLLFKEELKEWAKRSD--VEVI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 119593675 241 YTLDRAPEAWDYGQGFVNEEMirDHLPPPEEEPLVLMCGPPPMIQYAC 288
Cdd:cd06221 161 LTVDRAEEGWTGNVGLVTDLL--PELTLDPDNTVAIVCGPPIMMRFVA 206
|
|
| NqrF |
COG2871 |
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ... |
32-301 |
3.09e-20 |
|
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: 89.92 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 32 KYPLRLIDREIISHDTRRFRFALPSPQHI---------LGLPVGQHIYLSARID-----------GNLVVRPYTPISSDD 91
Cdd:COG2871 131 KWEATVVSNENVTTFIKELVLELPEGEEIdfkagqyiqIEVPPYEVDFKDFDIPeeekfglfdknDEEVTRAYSMANYPA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 92 DKGFVDLVIKVyfkDTHPKFPAGGKMSQYLESMQIGDTIEFRGPSGllvyqgkgKFAIRPDKKsnPIIrtvksvgMIAGG 171
Cdd:COG2871 211 EKGIIELNIRI---ATPPMDVPPGIGSSYIFSLKPGDKVTISGPYG--------EFFLRDSDR--EMV-------FIGGG 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 172 TGLAqhvrgpagyfagitPMLQVIRAIMKDPDDHTVCHLLFANQTEKDILLRPELEELRNKHSaRFKLWYTLDRAPEA-- 249
Cdd:COG2871 271 AGMA--------------PLRSHIFDLLERGKTDRKITFWYGARSLRELFYLEEFRELEKEHP-NFKFHPALSEPLPEdn 335
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 119593675 250 WDYGQGFVNEEMIRDHL--PPPEEEPLVLMCGPPPMIQyACLPNLDHVGHPTER 301
Cdd:COG2871 336 WDGETGFIHEVLYENYLkdHPAPEDCEAYLCGPPPMID-AVIKMLDDLGVEEEN 388
|
|
| monooxygenase_like |
cd06212 |
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
41-304 |
9.85e-19 |
|
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: 83.15 E-value: 9.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 41 EIISHDTRRFRFALPSPQHILGLPvGQhiYLSARIDGNLVVRPYTPISSDDDKGFVDLVIKVYfkdthpkfpAGGKMSQY 120
Cdd:cd06212 9 EALTHDIRRLRLRLEEPEPIKFFA-GQ--YVDITVPGTEETRSFSMANTPADPGRLEFIIKKY---------PGGLFSSF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 121 LES-MQIGDTIEFRGPsgllvYqgkGKFAIRpDKKSNPIIrtvksvgMIAGGTGLAqhvrgpagyfagitPMLQVIRAIM 199
Cdd:cd06212 77 LDDgLAVGDPVTVTGP-----Y---GTCTLR-ESRDRPIV-------LIGGGSGMA--------------PLLSLLRDMA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 200 KDPDDHTVcHLLFANQTEKDILLRPELEELRNKHSaRFKLWYTLDRAP--EAWDYGQGFVNEeMIRDHLPPpEEEPLVLM 277
Cdd:cd06212 127 ASGSDRPV-RFFYGARTARDLFYLEEIAALGEKIP-DFTFIPALSESPddEGWSGETGLVTE-VVQRNEAT-LAGCDVYL 202
|
250 260
....*....|....*....|....*..
gi 119593675 278 CGPPPMIQyACLPNLDHVGHPTERCFV 304
Cdd:cd06212 203 CGPPPMID-AALPVLEMSGVPPDQIFY 228
|
|
| flavohem_like_fad_nad_binding |
cd06184 |
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ... |
66-301 |
6.19e-18 |
|
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: 81.06 E-value: 6.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 66 GQHIYLSARIDGN--LVVRPYTpISSDDDKGFvdLVIKVyfkdthpKFPAGGKMSQYL-ESMQIGDTIEFRGPSGLLVYq 142
Cdd:cd06184 40 GQYLSVRVKLPGLgyRQIRQYS-LSDAPNGDY--YRISV-------KREPGGLVSNYLhDNVKVGDVLEVSAPAGDFVL- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 143 gkgkfairPDKKSNPIIrtvksvgMIAGGTglaqhvrgpagyfaGITPMLQVIRAIMKDPDDHTVcHLLFANQTEKDILL 222
Cdd:cd06184 109 --------DEASDRPLV-------LISAGV--------------GITPMLSMLEALAAEGPGRPV-TFIHAARNSAVHAF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 223 RPELEELRNKHS-ARFKLWYtldRAPEAWDYG-----QGFVNEEMIRDHLPPPEEEplVLMCGPPPMIQyACLPNLDHVG 296
Cdd:cd06184 159 RDELEELAARLPnLKLHVFY---SEPEAGDREedydhAGRIDLALLRELLLPADAD--FYLCGPVPFMQ-AVREGLKALG 232
|
....*
gi 119593675 297 HPTER 301
Cdd:cd06184 233 VPAER 237
|
|
| COG4097 |
COG4097 |
Predicted ferric reductase [Inorganic ion transport and metabolism]; |
8-285 |
1.21e-17 |
|
Predicted ferric reductase [Inorganic ion transport and metabolism];
Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 82.63 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 8 FLYSLLMKLFQRStpaitlespdiKYPLRLIDREIISHDTRRFRFALPSPQHILGLPvGQHIYLsaRIDGNLVVR---PY 84
Cdd:COG4097 201 AVYSRLGRPLRSR-----------RHPYRVESVEPEAGDVVELTLRPEGGRWLGHRA-GQFAFL--RFDGSPFWEeahPF 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 85 TPISSDDDKGFVDLVIKvyfkdthpkfpAGGKMSQYLESMQIGDTIEFRGPsgllvYqgkGKFAIRPDKKSNPIIrtvks 164
Cdd:COG4097 267 SISSAPGGDGRLRFTIK-----------ALGDFTRRLGRLKPGTRVYVEGP-----Y---GRFTFDRRDTAPRQV----- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 165 vgMIAGGtglaqhvrgpagyfAGITPMLQVIRAIMKDPDDHTVCHLLFANQTEKDILLRPELEELRNKHsARFKLWYTLD 244
Cdd:COG4097 323 --WIAGG--------------IGITPFLALLRALAARPGDQRPVDLFYCVRDEEDAPFLEELRALAARL-AGLRLHLVVS 385
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 119593675 245 RApeawdygQGFVNEEMIRDHLPPPeEEPLVLMCGPPPMIQ 285
Cdd:COG4097 386 DE-------DGRLTAERLRRLVPDL-AEADVFFCGPPGMMD 418
|
|
| flavin_oxioreductase |
cd06189 |
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ... |
43-303 |
1.32e-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: 79.90 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 43 ISHDTRRFRfaLPSPQHILGLPvGQhiYLSARIDGNlVVRPYTPISSDDDKGFVDLVIKVYfkdthpkfpAGGKMSQY-L 121
Cdd:cd06189 9 LNDDVYRVR--LKPPAPLDFLA-GQ--YLDLLLDDG-DKRPFSIASAPHEDGEIELHIRAV---------PGGSFSDYvF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 122 ESMQIGDTIEFRGPsgllvyqgKGKFAIRPDKkSNPIIrtvksvgMIAGGTGlaqhvrgpagyFAGITPMLQvirAIMKD 201
Cdd:cd06189 74 EELKENGLVRIEGP--------LGDFFLREDS-DRPLI-------LIAGGTG-----------FAPIKSILE---HLLAQ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 202 PDDHTVcHLLFANQTEKDILLRPELEELRNKHSarfKLWYT--LDRAPEAWDYGQGFVNEEMIRDHlpPPEEEPLVLMCG 279
Cdd:cd06189 124 GSKRPI-HLYWGARTEEDLYLDELLEAWAEAHP---NFTYVpvLSEPEEGWQGRTGLVHEAVLEDF--PDLSDFDVYACG 197
|
250 260
....*....|....*....|....
gi 119593675 280 PPPMIqYACLPNLDHVGHPTERCF 303
Cdd:cd06189 198 SPEMV-YAARDDFVEKGLPEENFF 220
|
|
| FNR_iron_sulfur_binding |
cd06191 |
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
35-301 |
1.44e-17 |
|
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: 79.88 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 35 LRLIDREIISHDTRRFRFALPSPQHILGLPvGQHIYLSARIDGNLVVRPYTpISSDDDKGFVDLVIKvyfkdthpKFPaG 114
Cdd:cd06191 1 LRVAEVRSETPDAVTIVFAVPGPLQYGFRP-GQHVTLKLDFDGEELRRCYS-LCSSPAPDEISITVK--------RVP-G 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 115 GKMSQYL-ESMQIGDTIEFRGPSGLLVYQgkgkfAIRPDKksnpiirtvksVGMIAGGTglaqhvrgpagyfaGITPMLQ 193
Cdd:cd06191 70 GRVSNYLrEHIQPGMTVEVMGPQGHFVYQ-----PQPPGR-----------YLLVAAGS--------------GITPLMA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 194 VIRAIMKDPDDHTVChLLFANQTEKDILLRPELEELRNKHSA-RFKLWYTLDRAPEAWDYGQGFvNEEMIRDHLPPPEEE 272
Cdd:cd06191 120 MIRATLQTAPESDFT-LIHSARTPADMIFAQELRELADKPQRlRLLCIFTRETLDSDLLHGRID-GEQSLGAALIPDRLE 197
|
250 260
....*....|....*....|....*....
gi 119593675 273 PLVLMCGPPPMIQyACLPNLDHVGHPTER 301
Cdd:cd06191 198 REAFICGPAGMMD-AVETALKELGMPPER 225
|
|
| MMO_FAD_NAD_binding |
cd06210 |
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ... |
41-288 |
1.48e-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: 80.08 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 41 EIISHDTRRFRFAlPSPQHILGLPV----GQhiYLSARIDGNLVVRPYTPISSDDDKGFVDLVIKVyfkdtHPkfpaGGK 116
Cdd:cd06210 10 DRVSSNVVRLRLQ-PDDAEGAGIAAefvpGQ--FVEIEIPGTDTRRSYSLANTPNWDGRLEFLIRL-----LP----GGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 117 MSQYLES-MQIGDTIEFRGPSGllvyqgkgKFAIRPDkksnpiirTVKSVGMIAGGTGLAqhvrgpagyfagitPMLQVI 195
Cdd:cd06210 78 FSTYLETrAKVGQRLNLRGPLG--------AFGLREN--------GLRPRWFVAGGTGLA--------------PLLSML 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 196 RAiMKDPDDHTVCHLLFANQTEKDILLRPELEELRNKH---SARFKLWytldRAPEAWDYGQGFVnEEMIRDHLPPPEEE 272
Cdd:cd06210 128 RR-MAEWGEPQEARLFFGVNTEAELFYLDELKRLADSLpnlTVRICVW----RPGGEWEGYRGTV-VDALREDLASSDAK 201
|
250
....*....|....*.
gi 119593675 273 PLVLMCGPPPMIQYAC 288
Cdd:cd06210 202 PDIYLCGPPGMVDAAF 217
|
|
| phenol_2-monooxygenase_like |
cd06211 |
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ... |
41-303 |
4.49e-16 |
|
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: 75.82 E-value: 4.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 41 EIISHDTRRFRFALPSPQHILGLPvGQhiYLSARIDGNLVVRPYTPISSDDDKGFVDLVIKVYfkdthpkfpAGGKMSQY 120
Cdd:cd06211 15 EDLTPTIKGVRLKLDEPEEIEFQA-GQ--YVNLQAPGYEGTRAFSIASSPSDAGEIELHIRLV---------PGGIATTY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 121 L-ESMQIGDTIEFRGPSGllvyqgkgKFAIRpDKKSNPIIrtvksvgMIAGGTGLAQhvrgpagyfagitpmlqvIRAI- 198
Cdd:cd06211 83 VhKQLKEGDELEISGPYG--------DFFVR-DSDQRPII-------FIAGGSGLSS------------------PRSMi 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 199 --MKDPDDHTVCHLLFANQTEKDILLRPELEELRNKHSaRFKLWYTLDRAPEA--WDYGQGFVNEeMIRDHLPPPEEEPL 274
Cdd:cd06211 129 ldLLERGDTRKITLFFGARTRAELYYLDEFEALEKDHP-NFKYVPALSREPPEsnWKGFTGFVHD-AAKKHFKNDFRGHK 206
|
250 260
....*....|....*....|....*....
gi 119593675 275 VLMCGPPPMIQyACLPNLDHVGHPTERCF 303
Cdd:cd06211 207 AYLCGPPPMID-ACIKTLMQGRLFERDIY 234
|
|
| NADH_quinone_reductase |
cd06188 |
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ... |
80-303 |
4.92e-14 |
|
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: 70.80 E-value: 4.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 80 VVRPYTPISSDDDKGFVDLVIKVyfkDTHPKFPAG---GKMSQYLESMQIGDTIEFRGPsgllvYqgkGKFAIRPDKksn 156
Cdd:cd06188 85 VSRAYSLANYPAEEGELKLNVRI---ATPPPGNSDippGIGSSYIFNLKPGDKVTASGP-----F---GEFFIKDTD--- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 157 piirtvKSVGMIAGGTGLAqhvrgpagyfagitPMLQVIRAIMKDPDDHTVCHLLFANQTEKDILLRPELEELRNKHSaR 236
Cdd:cd06188 151 ------REMVFIGGGAGMA--------------PLRSHIFHLLKTLKSKRKISFWYGARSLKELFYQEEFEALEKEFP-N 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119593675 237 FKLWYTLDR-APE-AWDYGQGFV----NEEMIRDHLPPPEEEplVLMCGPPPMIQyACLPNLDHVGHPTERCF 303
Cdd:cd06188 210 FKYHPVLSEpQPEdNWDGYTGFIhqvlLENYLKKHPAPEDIE--FYLCGPPPMNS-AVIKMLDDLGVPRENIA 279
|
|
| oxygenase_e_transfer_subunit |
cd06213 |
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
36-287 |
1.18e-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: 68.88 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 36 RLIDREIISHDTRRFRFALPSPQHILGlpvGQhiYLSARIDGNLVVRPYTPISSDDDKGFVDLVIKvyfkdthpKFPaGG 115
Cdd:cd06213 4 TIVAQERLTHDIVRLTVQLDRPIAYKA---GQ--YAELTLPGLPAARSYSFANAPQGDGQLSFHIR--------KVP-GG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 116 KMSQYL-ESMQIGDTIEFRGPSGllvyqgkgKFAIRPDKksNPIIrtvksvgMIAGGTGLAqhvrgPagyfagITPMLQV 194
Cdd:cd06213 70 AFSGWLfGADRTGERLTVRGPFG--------DFWLRPGD--APIL-------CIAGGSGLA-----P------ILAILEQ 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 195 IRAIMKDPDdhtvCHLLFANQTEKDILLRPELEELRNKHSARFKLWYTLDRAPE--AWDYGQGFVNEEmIRDHLPPPEEE 272
Cdd:cd06213 122 ARAAGTKRD----VTLLFGARTQRDLYALDEIAAIAARWRGRFRFIPVLSEEPAdsSWKGARGLVTEH-IAEVLLAATEA 196
|
250
....*....|....*
gi 119593675 273 PLvlmCGPPPMIQYA 287
Cdd:cd06213 197 YL---CGPPAMIDAA 208
|
|
| BenC |
NF040810 |
benzoate 1,2-dioxygenase electron transfer component BenC; |
41-284 |
4.04e-13 |
|
benzoate 1,2-dioxygenase electron transfer component BenC;
Pssm-ID: 468751 [Multi-domain] Cd Length: 333 Bit Score: 68.70 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 41 EIISHDTRRFRFALPSPQHILGLPvGQhiYLSARIDGNLVVRPYTpISSDDDKGFVDLVIKvyfkdthpKFPaGGKMSQY 120
Cdd:NF040810 113 EQLSDSTIELSLDLDDDAALAFLP-GQ--YVNIQVPGTGQTRSYS-FSSLPGAREASFLIR--------NVP-GGLMSSY 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 121 L-ESMQIGDTIEFRGPSGllvyqgkgKFAIRPDKKsnPIIrtvksvgMIAGGTGLAqhvrgPagyfagITPMLQVIRAim 199
Cdd:NF040810 180 LtERAKPGDRLSLTGPLG--------SFYLREVTR--PLL-------MLAGGTGLA-----P------FLSMLEVLAE-- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 200 kDPDDHTVcHLLFANQTEKDILLRPELEELRNKHSaRFKlWYTLDRAPEAWDYGQGFVNEEMIRDHLPPPEEEplVLMCG 279
Cdd:NF040810 230 -QGSEQPV-HLIYGVTRDADLVEVERLEAFAARLP-NFT-FRTCVADAASAHPRKGYVTQHIEAEWLNDGDVD--VYLCG 303
|
....*
gi 119593675 280 PPPMI 284
Cdd:NF040810 304 PPPMV 308
|
|
| FNR_like_3 |
cd06198 |
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ... |
83-285 |
1.85e-11 |
|
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: 62.27 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 83 PYTPISSDDDKGFVDLVIKvyfkdthpkfpAGGKMSQYL-ESMQIGDTIEFRGPsgllvYqgkGKFAIRPDKKsnPIIrt 161
Cdd:cd06198 43 PFTISSAPDPDGRLRFTIK-----------ALGDYTRRLaERLKPGTRVTVEGP-----Y---GRFTFDDRRA--RQI-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 162 vksvgMIAGGtglaqhvrgpagyfAGITPMLQVIRAIMKDPDDHTVcHLLFANQTEKDILLRPELEELRNKHSARFKLwy 241
Cdd:cd06198 100 -----WIAGG--------------IGITPFLALLEALAARGDARPV-TLFYCVRDPEDAVFLDELRALAAAAGVVLHV-- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 119593675 242 tLDRAPEAWDYgqgfvnEEMIRDHLPPPEEEPLVLMCGPPPMIQ 285
Cdd:cd06198 158 -IDSPSDGRLT------LEQLVRALVPDLADADVWFCGPPGMAD 194
|
|
| FNR1 |
cd06195 |
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ... |
36-288 |
3.34e-10 |
|
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: 59.12 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 36 RLIDREIISHDTRRFRFALPSP------QHI-LGLPVGqhiylsariDGNLVVRPYTPISSDDDKGFVDLVIKVyfkdth 108
Cdd:cd06195 1 TVLKRRDWTDDLFSFRVTRDIPfrfqagQFTkLGLPND---------DGKLVRRAYSIASAPYEENLEFYIILV------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 109 pkfpAGGKMSQYLESMQIGDTIE-FRGPSGLLVyqgkgkfaIRPdkksnpiIRTVKSVGMIAGGTGLAQHvrgpagyfag 187
Cdd:cd06195 66 ----PDGPLTPRLFKLKPGDTIYvGKKPTGFLT--------LDE-------VPPGKRLWLLATGTGIAPF---------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 188 itpmlqviRAIMKDPD-----DHTVchLLFANQTEKDILLRPELEELRNKHSARFKLWYTLDRAPEAWDYGQ----GFVN 258
Cdd:cd06195 117 --------LSMLRDLEiwerfDKIV--LVHGVRYAEELAYQDEIEALAKQYNGKFRYVPIVSREKENGALTGripdLIES 186
|
250 260 270
....*....|....*....|....*....|.
gi 119593675 259 EEMIRD-HLPPPEEEPLVLMCGPPPMIQYAC 288
Cdd:cd06195 187 GELEEHaGLPLDPETSHVMLCGNPQMIDDTQ 217
|
|
| FNR_N-term_Iron_sulfur_binding |
cd06194 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
37-284 |
1.49e-09 |
|
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: 56.89 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 37 LIDREIISHDTRRFRFALPSPQHILGlpvGQHIYLsARIDGnlVVRPYTPISSDDDKGFVDLVIKVYfkdthpkfpAGGK 116
Cdd:cd06194 1 VVSLQRLSPDVLRVRLEPDRPLPYLP---GQYVNL-RRAGG--LARSYSPTSLPDGDNELEFHIRRK---------PNGA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 117 MSQYL-ESMQIGDTIEFRGPSGLLVYqgkgkfaiRPDKKSNPIIrtvksvgMIAGGTGLAqhvrgpagyfagitPMLQVI 195
Cdd:cd06194 66 FSGWLgEEARPGHALRLQGPFGQAFY--------RPEYGEGPLL-------LVGAGTGLA--------------PLWGIA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 196 R-AIMKDPDDHTvcHLLFANQTEKDILLRPELEELRNKHSArFKLWYTLDRAPEawdyGQGFVNEEMIRDHLPPPEEEPL 274
Cdd:cd06194 117 RaALRQGHQGEI--RLVHGARDPDDLYLHPALLWLAREHPN-FRYIPCVSEGSQ----GDPRVRAGRIAAHLPPLTRDDV 189
|
250
....*....|
gi 119593675 275 VLMCGPPPMI 284
Cdd:cd06194 190 VYLCGAPSMV 199
|
|
| antC |
PRK11872 |
anthranilate 1,2-dioxygenase electron transfer component AntC; |
114-285 |
6.83e-09 |
|
anthranilate 1,2-dioxygenase electron transfer component AntC;
Pssm-ID: 183350 [Multi-domain] Cd Length: 340 Bit Score: 56.29 E-value: 6.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 114 GGKMSQYL-ESMQIGDTIEFRGPSGllvyqgkgKFAIRpdKKSNPIIrtvksvgMIAGGTGLAQhvrgpagyFAGitpML 192
Cdd:PRK11872 177 DGVMSNYLrERCQVGDEILFEAPLG--------AFYLR--EVERPLV-------FVAGGTGLSA--------FLG---ML 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 193 QvirAIMKDPDDHTVcHLLFANQTEKDILlrpELEELRNkHSAR---FKLWYTLDRAPEAWDYGQGFVNEEMIRDHLppp 269
Cdd:PRK11872 229 D---ELAEQGCSPPV-HLYYGVRHAADLC---ELQRLAA-YAERlpnFRYHPVVSKASADWQGKRGYIHEHFDKAQL--- 297
|
170
....*....|....*..
gi 119593675 270 EEEPLVL-MCGPPPMIQ 285
Cdd:PRK11872 298 RDQAFDMyLCGPPPMVE 314
|
|
| DHOD_e_trans |
cd06218 |
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ... |
38-283 |
1.95e-08 |
|
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: 54.09 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 38 IDREIISHDTRRFRFALPSPQHIlGLPvGQ--HIYLSARIDgNLVVRPytpIS---SDDDKGFVDLVIKVYfkdthpkfp 112
Cdd:cd06218 2 LSNREIADDIYRLVLEAPEIAAA-AKP-GQfvMLRVPDGSD-PLLRRP---ISihdVDPEEGTITLLYKVV--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 113 agGKMSQYLESMQIGDTIEFRGPsgllvyQGKGkFAIrPDKKSNPIIrtvksvgmIAGGTGLAqhvrgpagyfagitPML 192
Cdd:cd06218 67 --GKGTRLLSELKAGDELDVLGP------LGNG-FDL-PDDDGKVLL--------VGGGIGIA--------------PLL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 193 QVIRAIMKDPDDHTVChLLFAnqTEKDILLRPELEELRNKHSarfklWYTLDRApeawdYGQ-GFVnEEMIRDHLPPpEE 271
Cdd:cd06218 115 FLAKQLAERGIKVTVL-LGFR--SADDLFLVEEFEALGAEVY-----VATDDGS-----AGTkGFV-TDLLKELLAE-AR 179
|
250
....*....|..
gi 119593675 272 EPLVLMCGPPPM 283
Cdd:cd06218 180 PDVVYACGPEPM 191
|
|
| PRK13289 |
PRK13289 |
NO-inducible flavohemoprotein; |
113-287 |
1.34e-07 |
|
NO-inducible flavohemoprotein;
Pssm-ID: 237337 [Multi-domain] Cd Length: 399 Bit Score: 52.49 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 113 AGGKMSQYL-ESMQIGDTIEFRGPSGLLVYqgkgkfAIRPDKksnPIIrtvksvgMIAGGTGlaqhvrgpagyfagITPM 191
Cdd:PRK13289 227 AGGKVSNYLhDHVNVGDVLELAAPAGDFFL------DVASDT---PVV-------LISGGVG--------------ITPM 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 192 LQVIRAIMKDPDDHTVcHLLFANQTEKDILLRPELEELRNKHsARFKL--WYT----LDRAPEAWDYgQGFVNEEMIRDH 265
Cdd:PRK13289 277 LSMLETLAAQQPKRPV-HFIHAARNGGVHAFRDEVEALAARH-PNLKAhtWYRepteQDRAGEDFDS-EGLMDLEWLEAW 353
|
170 180
....*....|....*....|..
gi 119593675 266 LPPPEEEplVLMCGPPPMIQYA 287
Cdd:PRK13289 354 LPDPDAD--FYFCGPVPFMQFV 373
|
|
| PRK07609 |
PRK07609 |
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated |
16-303 |
1.89e-07 |
|
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
Pssm-ID: 181058 [Multi-domain] Cd Length: 339 Bit Score: 51.80 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 16 LFQRSTPA--ITLESPDI---------KYPLRLIDREIISHDTRRFRFALPSPQHILGLPvGQHIYLSARiDGnlVVRPY 84
Cdd:PRK07609 75 LTCCAKPLsdLVLEAREVpalgdipvkKLPCRVASLERVAGDVMRLKLRLPATERLQYLA-GQYIEFILK-DG--KRRSY 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 85 TPISSDDDKGFVDLVIKVYfkdthpkfpAGGKMSQYL-ESMQIGDTIEFRGPsgllvyqgKGKFAIR--PDKksnPIIrt 161
Cdd:PRK07609 151 SIANAPHSGGPLELHIRHM---------PGGVFTDHVfGALKERDILRIEGP--------LGTFFLRedSDK---PIV-- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 162 vksvgMIAGGTGLAQ------HVRgpagyFAGIT-PMlqviraimkdpddhtvcHLLFANQTEKDiLLRPELEELRNKHS 234
Cdd:PRK07609 209 -----LLASGTGFAPiksiveHLR-----AKGIQrPV-----------------TLYWGARRPED-LYLSALAEQWAEEL 260
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119593675 235 ARFKLWYTL-DRAPE-AWDYGQGFVNEEMIRDHlpPPEEEPLVLMCGPPPMIqYACLPNLDHVGHPTERCF 303
Cdd:PRK07609 261 PNFRYVPVVsDALDDdAWTGRTGFVHQAVLEDF--PDLSGHQVYACGSPVMV-YAARDDFVAAGLPAEEFF 328
|
|
| DHOD_e_trans_like |
cd06192 |
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ... |
37-293 |
6.96e-06 |
|
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: 46.55 E-value: 6.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 37 LIDREIISHDTRRFRFALPSPQHiLGLPvGQHIYLSARIDGNLVVRPYTPISSDDDKGFVDLVIKVyfkdthpkfpaGGK 116
Cdd:cd06192 1 IVKKEQLEPNLVLLTIKAPLAAR-LFRP-GQFVFLRNFESPGLERIPLSLAGVDPEEGTISLLVEI-----------RGP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 117 MSQYLESMQIGDTIEFRGPSGllvyqgkgkfairpdkksNP--IIRTVKSVGMIAGGTGLAqhvrgpagyfagitPMLQV 194
Cdd:cd06192 68 KTKLIAELKPGEKLDVMGPLG------------------NGfeGPKKGGTVLLVAGGIGLA--------------PLLPI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 195 IRAIMKDPDDhtvCHLLFANQTEKDILLRPELEELRNKHsarfkLWYTldrapeawDYGQGFVNEEMIRDHLPPPEEE-P 273
Cdd:cd06192 116 AKKLAANGNK---VTVLAGAKKAKEEFLDEYFELPADVE-----IWTT--------DDGELGLEGKVTDSDKPIPLEDvD 179
|
250 260
....*....|....*....|
gi 119593675 274 LVLMCGPPPMIqYACLPNLD 293
Cdd:cd06192 180 RIIVAGSDIMM-KAVVEALD 198
|
|
| PRK08345 |
PRK08345 |
cytochrome-c3 hydrogenase subunit gamma; Provisional |
49-304 |
8.30e-06 |
|
cytochrome-c3 hydrogenase subunit gamma; Provisional
Pssm-ID: 236247 [Multi-domain] Cd Length: 289 Bit Score: 46.34 E-value: 8.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 49 RFRFALPSPQHILGLPVGQHIYLSARIDGNLvvrPYTPISSDDDKGFVDLVIKvyfkdthpkfpAGGKMSQYLESMQIGD 128
Cdd:PRK08345 24 LLRFEDPELAESFTFKPGQFVQVTIPGVGEV---PISICSSPTRKGFFELCIR-----------RAGRVTTVIHRLKEGD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 129 TIEFRGPSGllvyqgkGKFAIRPDKKSNPIIrtvksvgmIAGGTGLAqhvrgpagyfagitPMLQVIRAIMKDPDDHTVC 208
Cdd:PRK08345 90 IVGVRGPYG-------NGFPVDEMEGMDLLL--------IAGGLGMA--------------PLRSVLLYAMDNRWKYGNI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 209 HLLFANQTEKDILLRPELEELRnKHSARFKLWYTLDRAPEAWDY---GQGF---VNEEMIRDHLPPPEEEP---LVLMCG 279
Cdd:PRK08345 141 TLIYGAKYYEDLLFYDELIKDL-AEAENVKIIQSVTRDPEWPGChglPQGFierVCKGVVTDLFREANTDPkntYAAICG 219
|
250 260
....*....|....*....|....*
gi 119593675 280 PPPMIQYAcLPNLDHVGHPTERCFV 304
Cdd:PRK08345 220 PPVMYKFV-FKELINRGYRPERIYV 243
|
|
| PRK00054 |
PRK00054 |
dihydroorotate dehydrogenase electron transfer subunit; Reviewed |
86-286 |
1.01e-04 |
|
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
Pssm-ID: 234601 [Multi-domain] Cd Length: 250 Bit Score: 42.94 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 86 PIS-SDDDKGFVDLVIKVYfkdthpkfpagGKMSQYLESMQIGDTIEFRGPsgllvyQGKGkFAIRPDKksnpiirtvKS 164
Cdd:PRK00054 52 PISiSDIDKNEITILYRKV-----------GEGTKKLSKLKEGDELDIRGP------LGNG-FDLEEIG---------GK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 165 VGMIAGGTGLAqhvrgpagyfagitPMLQVIRAIMKDPDDhtVCHLLFAnQTEKDILLRPELEELRNKHSArfklwyTLD 244
Cdd:PRK00054 105 VLLVGGGIGVA--------------PLYELAKELKKKGVE--VTTVLGA-RTKDEVIFEEEFAKVGDVYVT------TDD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 119593675 245 RApeawdYGQ-GFVNEEMirdhlpPPEEEP--LVLMCGPPPMIQY 286
Cdd:PRK00054 162 GS-----YGFkGFVTDVL------DELDSEydAIYSCGPEIMMKK 195
|
|
| PDR_like |
cd06185 |
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ... |
39-285 |
1.14e-04 |
|
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: 42.47 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 39 DREIISHDTRRFRFALPSPQHILGLPVGQHI--YLsaridGNLVVRPYTPISSDDDKGFVDLVIKvyfKDthpkfPAGGK 116
Cdd:cd06185 2 RIRDEAPDIRSFELEAPDGAPLPAFEPGAHIdvHL-----PNGLVRQYSLCGDPADRDRYRIAVL---RE-----PASRG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 117 MSQYL-ESMQIGDTIEFRGPSGLlvyqgkgkFAIRPDKKsnpiiRTVksvgMIAGGTGlaqhvrgpagyfagITPMLQVI 195
Cdd:cd06185 69 GSRYMhELLRVGDELEVSAPRNL--------FPLDEAAR-----RHL----LIAGGIG--------------ITPILSMA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 196 RAIMKDPDDhtvCHLLFANQTEKDIllrPELEELRNKHSARFKLWYTLDRAPEAwdygqgfvneemIRDHLPPPEEEPLV 275
Cdd:cd06185 118 RALAARGAD---FELHYAGRSREDA---AFLDELAALPGDRVHLHFDDEGGRLD------------LAALLAAPPAGTHV 179
|
250
....*....|
gi 119593675 276 LMCGPPPMIQ 285
Cdd:cd06185 180 YVCGPEGMMD 189
|
|
| CYPOR_like_FNR |
cd06208 |
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ... |
82-261 |
2.21e-04 |
|
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: 41.92 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 82 RPYTP----ISS-----DDDKGFVDLVIK--VYfkdTHPKF--PAGGKMSQYLESMQIGDTIEFRGPSgllvyqgkGKFA 148
Cdd:cd06208 60 KPHKLrlysIASsrygdDGDGKTLSLCVKrlVY---TDPETdeTKKGVCSNYLCDLKPGDDVQITGPV--------GKTM 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 149 IRPDKKSNPIIrtvksvgMIAGGTGLAqhvrgpagyfagitPMLQVIRAI-MKDPDDHT---VCHLLFANQTEKDILLRP 224
Cdd:cd06208 129 LLPEDPNATLI-------MIATGTGIA--------------PFRSFLRRLfREKHADYKftgLAWLFFGVPNSDSLLYDD 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 119593675 225 ELEELRNKHSARFKLWYTLDRAPEAWDYGQGFVNEEM 261
Cdd:cd06208 188 ELEKYPKQYPDNFRIDYAFSREQKNADGGKMYVQDRI 224
|
|
| CYPOR_like |
cd06182 |
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ... |
64-280 |
2.24e-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: 41.94 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 64 PVGQHIYLSAriDGNLVVRPYTpISS--DDDKGFVDL-VIKVYFKDTHPKFPAGGkMSQYLESMQIGD--TIEFR-GPSG 137
Cdd:cd06182 33 QPGDHLGVIP--PNPLQPRYYS-IASspDVDPGEVHLcVRVVSYEAPAGRIRKGV-CSNFLAGLQLGAkvTVFIRpAPSF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 138 LLvyqgkgkfairPDKKSNPIIrtvksvgMIAGGTGLAqhvrgPagyFAGitpMLQVIRAIMKDPDDHTVCHLLFANQTE 217
Cdd:cd06182 109 RL-----------PKDPTTPII-------MVGPGTGIA-----P---FRG---FLQERAALRANGKARGPAWLFFGCRNF 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119593675 218 K-DILLRPELEELRnKHSARFKLWYTLDRAPEAWD-YGQGFVNE--EMIRDHLpppEEEPLVLMCGP 280
Cdd:cd06182 160 AsDYLYREELQEAL-KDGALTRLDVAFSREQAEPKvYVQDKLKEhaEELRRLL---NEGAHIYVCGD 222
|
|
| SiR_like2 |
cd06201 |
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ... |
32-230 |
9.24e-04 |
|
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: 40.39 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 32 KYPLRLIDREI----ISHDTRRFRFALP-SPQHILGLPvgqhiYLSAridGNL---------VVRPYTPISSDDDkGFVD 97
Cdd:cd06201 45 TKALELVERKDygaaVQAPTAILRFKPAkRKLSGKGLP-----SFEA---GDLlgilppgsdVPRFYSLASSSSD-GFLE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 98 LVIKvyfkdTHPkfpaGGKMSQYLESMQIGDTIE-FRGPSGllvyqgkgkfAIRPDKKSNPIIrtvksvgMIAGGTGLAq 176
Cdd:cd06201 116 ICVR-----KHP----GGLCSGYLHGLKPGDTIKaFIRPNP----------SFRPAKGAAPVI-------LIGAGTGIA- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 119593675 177 hvrgpagyfagitPMLQVIRAIMKdpddHTVCHLLFANQT-EKDILLRPELEELR 230
Cdd:cd06201 169 -------------PLAGFIRANAA----RRPMHLYWGGRDpASDFLYEDELDQYL 206
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|
| DHOD_e_trans_like1 |
cd06219 |
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ... |
83-289 |
3.52e-03 |
|
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: 38.33 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 83 PYTPISSDDDKGFVDLVIKVyfkdthpkfpaGGKMSQYLESMQIGDTIE-FRGPSGllvyqgkgkfairpdkksNPI-IR 160
Cdd:cd06219 45 PLTIADWDPEKGTITIVVQV-----------VGKSTRELATLEEGDKIHdVVGPLG------------------KPSeIE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 161 TVKSVGMIAGGTGLAqhvrgpagyfagitPMLQVIRAiMKDPDDHTVchLLFANQTEKDILLRPELEELRNKHsarfklW 240
Cdd:cd06219 96 NYGTVVFVGGGVGIA--------------PIYPIAKA-LKEAGNRVI--TIIGARTKDLVILEDEFRAVSDEL------I 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 119593675 241 YTLDRApeawDYG-QGFVNEEMiRDHLPPPEEEPLVLMCGPPPMIQYACL 289
Cdd:cd06219 153 ITTDDG----SYGeKGFVTDPL-KELIESGEKVDLVIAIGPPIMMKAVSE 197
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|
| siderophore_interacting |
cd06193 |
Siderophore interacting proteins share the domain structure of the ferredoxin reductase like ... |
24-142 |
5.87e-03 |
|
Siderophore interacting proteins share the domain structure of the ferredoxin reductase like family. Siderophores are produced in various bacteria (and some plants) to extract iron from hosts. Binding constants are high, so iron can be pilfered from transferrin and lactoferrin for bacterial uptake, contributing to pathogen virulence. 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 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 two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).
Pssm-ID: 99790 [Multi-domain] Cd Length: 235 Bit Score: 37.63 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593675 24 ITLESPDIKYPLRlidreiiSHDTRRFRFALPSPQHILGLPVGQHIYLSARIDGNLVVRPYTPISSDDDKGFVDLVIkVy 103
Cdd:cd06193 14 ITLGGPDLAGFPS-------DGPDQHVKLLFPDPGQAPPVLPVLGRRRWPPEEPRPVMRTYTVRRFDPEAGELDIDF-V- 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 119593675 104 fkdTHpkfPAGGKMSQYLESMQIGDTIEFRGPSGLLVYQ 142
Cdd:cd06193 85 ---LH---GDEGPASRWAASAQPGDTLGIAGPGGSFLPP 117
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