A7GZP5
Gene name |
napA |
Protein name |
Periplasmic nitrate reductase |
Names |
|
Species |
Campylobacter curvus (strain 52592) |
KEGG Pathway |
ccv:CCV52592_1928 |
EC number |
1.9.6.1: With a nitrogenous group 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 A7GZP5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A7GZP5-F1 | Predicted | AlphaFoldDB |
No variants for A7GZP5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A7GZP5 | |||||
No associated diseases with A7GZP5
6 regional properties for A7GZP5
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Twin-arginine translocation pathway, signal sequence | 1 - 30 | IPR006311 |
| domain | Molybdopterin oxidoreductase | 94 - 614 | IPR006656 |
| domain | Molybdopterin dinucleotide-binding domain | 812 - 920 | IPR006657 |
| domain | Molybdopterin oxidoreductase, 4Fe-4S domain | 37 - 93 | IPR006963 |
| binding_site | Molybdopterin oxidoreductase, molybdopterin cofactor binding site | 42 - 59 | IPR027467 |
| domain | Nitrate reductase NapA-like, molybdopterin-binding domain | 809 - 926 | IPR041957 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.9.6.1 | With a nitrogenous group 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 |
|---|---|
| periplasmic space | The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria). |
7 GO annotations of molecular function
| Name | Definition |
|---|---|
| 4 iron, 4 sulfur cluster binding | Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. |
| 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. |
| iron ion binding | Binding to an iron (Fe) ion. |
| molybdenum ion binding | Binding to a molybdenum ion (Mo). |
| molybdopterin cofactor binding | Binding to a molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands. |
| nitrate reductase (cytochrome) activity | Catalysis of the reaction: ferrocytochrome + nitrate = ferricytochrome + nitrite. |
| nitrate reductase activity | Catalysis of the reaction: nitrite + acceptor = nitrate + reduced acceptor. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| Mo-molybdopterin cofactor biosynthetic process | The chemical reactions and pathways resulting in the formation of the Mo-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear molybdenum (Mo) ion coordinated by one or two molybdopterin ligands. |
| nitrate assimilation | The nitrogen metabolic process that encompasses the uptake of nitrate from the environment and reduction to ammonia, and results in the incorporation of nitrogen derived from nitrate into cellular substances. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNRRDFIKSA | AASAACASAG | IAIPANLSAA | SEAEKGWRWD | KAACRFCGTG | CGIMVATKEG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KIVAVKGDPE | APVNRGLNCI | KGYFNAKIMY | GEDRITHPLL | RVNEKGEFDK | KGKFKQVSWK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QAFDVMEAQF | RKTYDELGPH | GVGVLGSGQY | TIPEGYTAAK | MMKAGFRSNS | IDPNARHCMA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SAVVGFIQVF | GIDEPSGCFD | DIELTDTIVA | WGANMAEMHP | ILWARVSDRK | LSNPDRVKVV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NLSTYSTRTS | NLADIEIIFA | PSADLAIWNY | IAREIVYNHP | EMIDEEFVKK | HCIFTTGPAD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IGYGLRPDIK | YKKYLSSELD | TAATEKSKVL | SEAEGVTLSY | LGLKAGDTME | NKNTATAGNH |
| 370 | 380 | 390 | 400 | 410 | 420 |
| WHISFEEFKK | ALAPYTLEFT | AKVAKGDPNE | DIEEFKGKLK | ALADLYIEKN | RKVVSFWTMG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| FNQHQRGTWV | NEQAYMVHFL | LGKQALPGSG | AFSLTGQPSA | CGTAREVGTF | VHRLPADMVV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NNPKHREISE | KIWKLPAGTL | NGIPGSHYVK | MMRDLEDGKV | KFIWVQVNNP | WQNTANANHW |
| 550 | 560 | 570 | 580 | 590 | 600 |
| IKAAREMDNF | IVVSDPYPGI | SAKVADLILP | TAMIYEKWGA | YGNAERRTQH | WRQQVLPVGE |
| 610 | 620 | 630 | 640 | 650 | 660 |
| AMPDIWQMLE | FSKRFKLKDV | WGEKKLNDKV | TLPSVLDAAK | AMGYSEEDTL | FDVLFANEEA |
| 670 | 680 | 690 | 700 | 710 | 720 |
| KSYPANDPIM | ENFDNTEVFG | DKRGVIGSDG | KEFKGYGFFV | HKYLWEEYRK | FGLGHGHDLA |
| 730 | 740 | 750 | 760 | 770 | 780 |
| DFDTYHRVRG | LRWPVVDGKE | TQWRFNTKFD | PYAKKAAPND | KFAFYGNKAA | ALPSGDLKGV |
| 790 | 800 | 810 | 820 | 830 | 840 |
| TDKEKTPLTN | KAKIFFRPYM | DPCEMPSSEY | PFWLCTGRVL | EHWHSGTMTM | RVPELYRAVP |
| 850 | 860 | 870 | 880 | 890 | 900 |
| EALCYMHEQD | AAKLGVLQNE | IVWIESRRGK | VKARVDLKGR | NKPPVGLVYV | PWFDENVFIN |
| 910 | 920 | ||||
| KVTLDSTCPI | SKETDYKKCA | VKIYKA |