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

3 structures for P49050

Entry ID Method Resolution Chain Position Source
2BIH X-ray 260 A A 19-478 PDB
2BII X-ray 170 A A/B 59-478 PDB
AF-P49050-F1 Predicted AlphaFoldDB

No variants for P49050

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P49050

No associated diseases with P49050

14 regional properties for P49050

Type Name Position InterPro Accession
domain Oxidoreductase, molybdopterin-binding domain 89 - 265 IPR000572
domain Cytochrome b5-like heme/steroid binding domain 502 - 578 IPR001199
domain Oxidoreductase FAD/NAD(P)-binding 732 - 842 IPR001433
domain Flavoprotein pyridine nucleotide cytochrome reductase 537 - 547 IPR001709-1
domain Flavoprotein pyridine nucleotide cytochrome reductase 655 - 662 IPR001709-2
domain Flavoprotein pyridine nucleotide cytochrome reductase 731 - 750 IPR001709-3
domain Flavoprotein pyridine nucleotide cytochrome reductase 757 - 766 IPR001709-4
domain Flavoprotein pyridine nucleotide cytochrome reductase 769 - 780 IPR001709-5
domain Flavoprotein pyridine nucleotide cytochrome reductase 829 - 837 IPR001709-6
domain Moybdenum cofactor oxidoreductase, dimerisation 293 - 437 IPR005066
domain Flavoprotein pyridine nucleotide cytochrome reductase-like, FAD-binding domain 607 - 712 IPR008333
domain FAD-binding domain, ferredoxin reductase-type 602 - 713 IPR017927
binding_site Cytochrome b5, heme-binding site 534 - 541 IPR018506
binding_site Oxidoreductase, molybdopterin binding site 109 - 144 IPR022407

Functions

Description
EC Number 1.7.1.3 With NAD(+) or NADP(+) as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

5 GO annotations of molecular function

Name Definition
FAD binding Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
heme binding Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
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 (NADPH) activity Catalysis of the reaction: nitrite + NADP+ + H2O = nitrate + NADPH + H+.

2 GO annotations of biological process

Name Definition
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.
nitric oxide biosynthetic process The chemical reactions and pathways resulting in the formation of nitric oxide, nitrogen monoxide (NO), a colorless gas only slightly soluble in water.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MDSIVTEVTY GLEIKKIKDI TELPFPVRQD SPLTEVLPTD LKTKDNFVAR DPDLLRLTGS
70 80 90 100 110 120
HPFNSEPPLT KLYDSGFLTP VSLHFVRNHG PVPYVPDENI LDWEVSIEGM VETPYKIKLS
130 140 150 160 170 180
DIMEQFDIYS TPVTMVCAGN RRKEQNMVKK GAGFNWGAAG TSTSLWTGCM LGDVIGKARP
190 200 210 220 230 240
SKRARFVWME GADNPANGAY RTCIRLSWCM DPERCIMIAY QQNGEWLHPD HGKPLRVVIP
250 260 270 280 290 300
GVIGGRSVKW LKKLVVSDRP SENWYHYFDN RVLPTMVTPE MAKSDDRWWK DERYAIYDLN
310 320 330 340 350 360
LQTIICKPEN QQVIKISEDE YEIAGFGYNG GGVRIGRIEV SLDKGKSWKL ADIDYPEDRY
370 380 390 400 410 420
REAGYFRLFG GLVNVCDRMS CLCWCFWKLK VPLSELARSK DILIRGMDER MMVQPRTMYW
430 440 450 460 470 480
NVTSMLNNWW YRVAIIREGE SLRFEHPVVA NKPGGWMDRV KAEGGDILDN NWGEVDDTVK
490 500 510 520 530 540
QAERRPHIDE DLEMMCNREK MDVVIKYSEF EAHKDSETEP WFAVKGQVFD GSSYLEDHPG
550 560 570 580 590 600
GAQSILMVSG EDATDDFIAI HSSFAKKLLP SMHLGRLEEV SSVTKVKSVE QNVKREVLLD
610 620 630 640 650 660
PRKWHKITLA EKEVISSDSR IFKFDLEHSE QLSGLPTGKH LFLRLKDSSG KYVMRAYTPK
670 680 690 700 710 720
SSNSLRGRLE ILIKVYFPNR EYPNGGIMTN LIENLQVGNQ IEVKGPVGEF EYVKCGHCSF
730 740 750 760 770 780
NNKPYQMKHF VMISGGSGIT PTYQVLQAIF SDPEDRTSVQ LFFGNKKVDD ILLREELDHI
790 800 810 820 830 840
QEKYPEQFKV DYSLSDLDHL PENWSGVRGR LTFDILDTYV RGKKMGEYML LVCGPPGMNG
850
VVENWCNARK LDKQYVVYF