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 A4XWM0

Entry ID Method Resolution Chain Position Source
AF-A4XWM0-F1 Predicted AlphaFoldDB

No variants for A4XWM0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A4XWM0

No associated diseases with A4XWM0

7 regional properties for A4XWM0

Type Name Position InterPro Accession
conserved_site Twin-arginine translocation pathway, signal sequence 1 - 30 IPR006311
domain Molybdopterin oxidoreductase 98 - 570 IPR006656
domain Molybdopterin dinucleotide-binding domain 715 - 823 IPR006657
domain Molybdopterin oxidoreductase, 4Fe-4S domain 41 - 97 IPR006963
conserved_site Twin-arginine translocation pathway, signal sequence, bacterial/archaeal 2 - 25 IPR019546
binding_site Molybdopterin oxidoreductase, molybdopterin cofactor binding site 46 - 63 IPR027467
domain Nitrate reductase NapA-like, molybdopterin-binding domain 712 - 829 IPR041957

Functions

Description
EC Number 1.9.6.1 With a nitrogenous group as acceptor
Subcellular Localization
  • Periplasm
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
MKLSRREFAK ANAAAIAAAA AGLPLASTAS NLITEADMTR LDWNKAPCRF CGTGCSVMVA
70 80 90 100 110 120
TRDNRVVATH GDVKAEVNRG LNCVKGYFLS KIMYGVDRLT QPLLRMKNGV YDKQGEFQPV
130 140 150 160 170 180
SWDQAFDIMA QKIKQAIAEQ GPEAVGMFGS GQWTVWEGYA ANKLMKAGFR SNNIDPNARH
190 200 210 220 230 240
CMASAVMGFM RTFGMDEPMG CYDDIEAADA FVLWGSNMAE MHPILWSRVT DRRLSHPNTR
250 260 270 280 290 300
VAVLSTFEHR SFDLADIPLV FKPQTDLLIL NYIANHIIES GAVNKDFVGK HTKFARGADD
310 320 330 340 350 360
IGYGLRADNP LEMQAKNAAK ANTWEDMSFE QFAAFVKPYT LERTAKESGV AAERLKALAK
370 380 390 400 410 420
LYADPKRKVM SFWTMGFNQH TRGVWANNLI YNLHLLTGKI SEPGNSPFSL TGQPSACGTA
430 440 450 460 470 480
REVGTFSHRL PADMLVANPK HRETAEKIWK LPPGTIQEKP GFHAVEQSRK LKDGVLKVYW
490 500 510 520 530 540
TQVSNNMQAG PNVMQEILPG WRNPQAFVIV SDVYPTVSAQ AADLILPSAM WVEKEGAYGN
550 560 570 580 590 600
AERRTQFWHQ LVKAPGEAKS DLWQLVEFSK RFTTDEVWPA ELLAKAPDYK GKTLYQVLFA
610 620 630 640 650 660
NGQVDQFPSE QIEAGYANDE AEAFGFYLQK GLFEEYARFG RGHAHDLAPF DSYHAERGLR
670 680 690 700 710 720
WPVVDGKETR WRYREGHDPY VEKGSGVQFY GYPDKRALIF ALPYEPPAEA PDDEFPFWLS
730 740 750 760 770 780
TGRVLEHWHT GSMTQRVEEL HGAVPDALVY MHPDDAKALK ARRGSEVKVI SRRGEIRARI
790 800 810 820 830
ETRGRNKPPR GLVFVPFFDA NKLINKVTLD ATDPISKQTD YKKCAVKIEL VSLA