Q88FX8
Gene name |
nicB (ndhL, PP_3948) |
Protein name |
Nicotinate dehydrogenase subunit B |
Names |
Nicotinate degradation protein B, Nicotinate dehydrogenase large subunit |
Species |
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) |
KEGG Pathway |
ppu:PP_3948 |
EC number |
1.17.2.1: With a cytochrome as acceptor |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q88FX8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q88FX8-F1 | Predicted | AlphaFoldDB |
No variants for Q88FX8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q88FX8 | |||||
No associated diseases with Q88FX8
7 regional properties for Q88FX8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead | 204 - 290 | IPR000674 |
| domain | Aldehyde oxidase/xanthine dehydrogenase, first molybdopterin binding domain | 313 - 550 | IPR008274 |
| domain | Cytochrome c-like domain | 804 - 907 | IPR009056-1 |
| domain | Cytochrome c-like domain | 949 - 1057 | IPR009056-2 |
| domain | Cytochrome c-like domain | 1075 - 1163 | IPR009056-3 |
| domain | Aldehyde oxidase/xanthine dehydrogenase, second molybdopterin binding domain | 48 - 188 | IPR046867-1 |
| domain | Aldehyde oxidase/xanthine dehydrogenase, second molybdopterin binding domain | 580 - 687 | IPR046867-2 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.17.2.1 | With a cytochrome as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| electron transfer activity | Any molecular entity that serves as an electron acceptor and electron donor in an electron transport chain. An electron transport chain is a process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient. |
| heme binding | Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring. |
| metal ion binding | Binding to a metal ion. |
| oxidoreductase activity, acting on CH or CH2 groups | Catalysis of an oxidation-reduction (redox) reaction in which a CH2 group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| aromatic compound catabolic process | The chemical reactions and pathways resulting in the breakdown of aromatic compounds, any substance containing an aromatic carbon ring. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNHSQQVPSR | DQLLAKTGVL | LIVDQITPPS | GPVAKGVTPT | VKERELALFI | AVSDDGMVYA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FNGHVDLGTG | IRTSLAQIVA | EELDLRMDQV | HMVLGDTERA | PNQGATIASA | TLQISAVPLR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KAAATARRYL | LQQAALRLGC | PPEMLRIEDG | TVIASNGSTL | SFAELVQGKN | HQLHIADDAP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LKAIEDYRLV | GRSAPRVDIP | GKATGELTYV | HDMRLPNMLH | GRVIRPPYAG | HDSGDFVGNS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LLAVDESSIA | HLPGVVAVVV | IRDFVGVVAE | REEQAIRAAH | ELKVSWKPFT | GKLPDLSDVA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| QAIRDNPRVQ | RTVLDQGDVD | GGIANASQRL | SRSYLWPYQL | HASIGPSCAL | ADFTAGQIRV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| WSGTQNPHLL | RADLAWLLAC | DEARIEIIRM | EAAGCYGRNC | ADDVCADAVL | LSRAVQRPVR |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VQLTREQEHV | WEPKGTAQLM | EIDGGLNADG | SVAAYDFQTS | YPSNGAPTLA | LLLTGAVEPV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| PALFEMGDRT | SIPPYDYEHM | RVTINDMTPL | VRASWMRGVS | AMPNSFAHES | YIDELAFAAG |
| 550 | 560 | 570 | 580 | 590 | 600 |
| VDPVEYRLKH | LSDPRAIDLV | KATAERAQWQ | PHTRPMQTQA | EGDVLRGRGF | AYARYIHSKF |
| 610 | 620 | 630 | 640 | 650 | 660 |
| PGFGAAWAAW | VADVAVDRRT | GEVAVTRVVI | GHDAGMMVNP | EGVRHQIHGN | VIQSTSRVLK |
| 670 | 680 | 690 | 700 | 710 | 720 |
| EQVSFEESTV | ASKEWGGYPI | LTFPELPAID | VMMLPRQHEP | PMGSGESASV | PSAAAIANAI |
| 730 | 740 | 750 | 760 | 770 | 780 |
| FDATGIRFRE | LPITAERVRA | ALGGEGQGPD | APAPAQPSTK | RSKWWFGSLA | GVFGAALGML |
| 790 | 800 | 810 | 820 | 830 | 840 |
| ATALPWRAEI | APVTPPGVGS | WSAAMLERGR | QVAAAGDCAV | CHTVSGGKAN | AGGLAMDTPF |
| 850 | 860 | 870 | 880 | 890 | 900 |
| GTLYSTNITP | DPETGIGRWS | FAAFERAMRE | GISRDGRHLY | PAFPYTSFRN | INDADMQALY |
| 910 | 920 | 930 | 940 | 950 | 960 |
| AYLMSQTPVR | QEAPANQMRF | PFNQRPLMAG | WNARFLQRGE | YQPDPQRSAQ | WNRGAYLVDG |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| LGHCTACHSP | RNLMGAEKGG | SSYLAGGMVD | GWEAPALNAL | GKSSTPWSED | ELFNYLSTGF |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| SEKHGVAAGP | MGPVVSELAT | LPKSDVRAIA | HYLSSLEGEP | QALAANAAPQ | VDTHVSLSNG |
| 1090 | 1100 | 1110 | 1120 | 1130 | 1140 |
| ERVFKGACLG | CHSDGLGPKL | FGVSPSMAVN | SNVHSDLPDN | LLRVVLHGIP | TPATRDLGYM |
| 1150 | 1160 | 1170 | 1180 | ||
| PGFKDSLSDR | QVADLAAYLR | HRFAADKPAW | QGLASKAAQV | RANPGSH |