| Basic Information | |
|---|---|
| Species | Volvox carteri |
| Cazyme ID | Vocar20001335m |
| Family | GT77 |
| Protein Properties | Length: 1035 Molecular Weight: 114194 Isoelectric Point: 9.0784 |
| Chromosome | Chromosome/Scaffold: 24 Start: 821917 End: 830010 |
| Description | FAD/NAD(P)-binding oxidoreductase |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GT77 | 142 | 379 | 4e-35 |
| YWLIAALDPETSMALASMGVKQCFNAPQDRLKYKGSDTKYQWGGHHWSMTTWNKVHIMKSVYEMGVHVVHSDMDVVWFNDPLPYFKSLLEKPVHIVIATD AVTSENPKGDTGLEALTSPHANINTGIYFMRQWPGGLEFFNIWLSWQDKRIGHDQDGFNFVSRGYYFHGDADMPLATQTQDRMFYCAYSNTTAVSFLPAS MFGNTYTYVNARLWEKLDHPLYEVHWVWGGSTMESKRQ | |||
| Full Sequence |
|---|
| Protein Sequence Length: 1035 Download |
| MKGILSVETA QPGSNLRTCS QLIHGHSMPG LHLFPFSFSV MLHFCVMIFS AVLFASAQSR 60 HVHPAWFFNT QSEWHLPFSQ SNRALLSEVA GAKTAHCGPL TRKLVQGVAR ENTVLVTVVD 120 KIIWKCFGPS YVENIQAANI SYWLIAALDP ETSMALASMG VKQCFNAPQD RLKYKGSDTK 180 YQWGGHHWSM TTWNKVHIMK SVYEMGVHVV HSDMDVVWFN DPLPYFKSLL EKPVHIVIAT 240 DAVTSENPKG DTGLEALTSP HANINTGIYF MRQWPGGLEF FNIWLSWQDK RIGHDQDGFN 300 FVSRGYYFHG DADMPLATQT QDRMFYCAYS NTTAVSFLPA SMFGNTYTYV NARLWEKLDH 360 PLYEVHWVWG GSTMESKRQN MRDAMKFHDE PEYYTSPYLI TFALEQLKMP EGFNSWEVPR 420 TEEMIRFHVT AANHQLQQAY YAFAAALITN RTLVMPRFLC YCSKNWYQTQ SCRINDEKLA 480 TFPFVCALSH VLRVKKLQQG FELPANTDYS GHKVFIREYS FLENPKVPDE IKRSYLEVVP 540 SAVPRPPGQL TADQLVLSTD DTSSRGYGRR ITVAAPLSDW EFHKVLERYG DVRVVHLPQP 600 SRTLSGFSKP ETAKQFDVEI QRRVTYWCCR SPPVMATKNL TEGVQLVGLP QNRWENLPLL 660 GKRYSYLHQT PPLSGTNVGA SVGMGLPLLG EPKRCTVERQ ADVKLTIGAI MQNSTLRAKS 720 FSGGPAVAGR AARQTSAVAR PRLQTWSAVS PNAVAAACTV TGAIPPPRRS TTSSRAPAFS 780 AAQPPRHPGR RSSVKVHANW GAPVEFKPAK IVSNTSAAAG PLHKLVIDVG PLAAGYAVPG 840 QFIQIKVGDS KPGFFAIASA PGAHSDGLLE FLIKGAPGTT AELLCNAGDG TEVAVSPVMG 900 KGFPLDRLPA SNTTAVLMFA TGSGISPIRA VIDSGTLAGR DITLYYGTRN TDSTAYRELL 960 PDWQAKGVKV VQVFSESKQG YVHDVFEREG LSKLPADAAS AVGALLCGHK GMCQAITSLL 1020 TAKGVPPEKI LLNF* 1080 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd06221 | sulfite_reductase_like | 6.0e-18 | 839 | 1032 | 204 | + 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+. | ||
| cd06218 | DHOD_e_trans | 2.0e-18 | 811 | 1026 | 228 | + 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. | ||
| cd06187 | O2ase_reductase_like | 4.0e-19 | 839 | 1030 | 206 | + 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. | ||
| pfam03407 | Nucleotid_trans | 4.0e-24 | 139 | 381 | 246 | + Nucleotide-diphospho-sugar transferase. Proteins in this family have been been predicted to be nucleotide-diphospho-sugar transferases. | ||
| cd00322 | FNR_like | 9.0e-27 | 839 | 1031 | 204 | + 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). | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0005783 | endoplasmic reticulum |
| GO:0016491 | oxidoreductase activity |
| GO:0055114 | oxidation-reduction process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| RefSeq | XP_001697686.1 | 0 | 178 | 635 | 26 | 566 | hypothetical protein CHLREDRAFT_195312 [Chlamydomonas reinhardtii] |
| RefSeq | XP_001700329.1 | 0 | 156 | 673 | 1 | 520 | predicted protein [Chlamydomonas reinhardtii] |
| RefSeq | XP_001700357.1 | 0 | 711 | 1034 | 1 | 321 | predicted protein [Chlamydomonas reinhardtii] |
| RefSeq | XP_001700358.1 | 0 | 103 | 679 | 19 | 628 | predicted protein [Chlamydomonas reinhardtii] |
| RefSeq | XP_001701267.1 | 0 | 100 | 647 | 194 | 692 | hypothetical protein CHLREDRAFT_179139 [Chlamydomonas reinhardtii] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2bpo_B | 0.0004 | 907 | 1022 | 518 | 651 | A Chain A, Crystal Structure Of The Yeast Cpr Triple Mutant: D74g, Y75f, K78a. |
| PDB | 2bpo_A | 0.0004 | 907 | 1022 | 518 | 651 | A Chain A, Crystal Structure Of The Yeast Cpr Triple Mutant: D74g, Y75f, K78a. |
| PDB | 2bn4_B | 0.0004 | 907 | 1022 | 518 | 651 | A Chain A, Crystal Structure Of The Yeast Cpr Triple Mutant: D74g, Y75f, K78a. |
| PDB | 2bn4_A | 0.0004 | 907 | 1022 | 518 | 651 | A Chain A, Crystal Structure Of The Yeast Cpr Triple Mutant: D74g, Y75f, K78a. |
| PDB | 2bf4_B | 0.0004 | 907 | 1022 | 518 | 651 | A Chain A, A Second Fmn-Binding Site In Yeast Nadph-Cytochrome P450 Reductase Suggests A Novel Mechanism Of Electron Transfer By Diflavin Reductases. |
