Q8VL02

PR
Gene name
napA
Protein name
Periplasmic nitrate reductase
Names
Species
Aggregatibacter actinomycetemcomitans (Actinobacillus actinomycetemcomitans) (Haemophilus actinomycetemcomitans)
KEGG Pathway
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)

1-62 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q8VL02

Entry ID Method Resolution Chain Position Source
AF-Q8VL02-F1 Predicted AlphaFoldDB

No variants for Q8VL02

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8VL02

No associated diseases with Q8VL02

1 regional properties for Q8VL02

Type Name Position InterPro Accession
conserved_site Mrp, conserved site 184 - 200 IPR000808

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
MNLSRRDFMK ANAAMAAATA AGLSIPVKNV EAAESEIKWD KAVCRFCGTG CAVLVGTKDG
70 80 90 100 110 120
RVVASQGDPD AEVNRGLNCI KGYFLPKIMY GKDRLTQPML RMKDGKYDKN GDFTPVSWDV
130 140 150 160 170 180
AFKTMAEKFK AAVKELGPNG VGMFSSGQTT IFEGYAKSKL WKAGFRSNNI DPNARHCMAS
190 200 210 220 230 240
AAVAFMRTFG MDEPMGCYND IEQAEAFVLW GSNMAEMHPI LWSRITDRRL SNQDVKVAVL
250 260 270 280 290 300
STFEHRSFEL ADYSLIFKPH TDLVILNYII NYLIQNDAIN RDFVNKHTKF KRGETDIGYG
310 320 330 340 350 360
LRPENPLEQK AKNVKTAGKM YDSNFDELKA LVAEYTLDKA HEMSGVPKDV LENLAKLYAD
370 380 390 400 410 420
PKKKVVSYWT MGFNQHTRGV WANHLIYNIH LLTGKISIPG CGPFSLTGQP SACGTAREVG
430 440 450 460 470 480
TFIHRLPADL VVTNPKHREK AEQIWKLPAG VITDVLGFHA VAQSRALKDG KMRVLWQMCT
490 500 510 520 530 540
NNMQGGPNIN RETFPGWRNP DNFIVVSDPY PTVSCLAADL MLPTAMWVEK EGAYGNAERR
550 560 570 580 590 600
TQFWRQQVKA PGEAKSDVWQ LVEFSKYFTT DEMWPAEILD KNPEYKGKTL YDVLYRNGQV
610 620 630 640 650 660
DKFPLSELAE GQLNDESYHF GFYLQKGLFE EYASFGRGHG HDLASFDTYH KARGLRWPVV
670 680 690 700 710 720
DGKETLWRYR EGYDPYVKEG EGVAFYGYPD KKAIILAVPY EPPAESPDEE YDLWLCTGRV
730 740 750 760 770 780
LEHWHTGTMT RRVPELHRSF PNNLVWMHPT DAQKRGLRHG DKVKVASRRG EIISFLDTRG
790 800 810 820
RNKVPEGLIY TTFFDAGQLA NKLTLDATDP ISKETDFKKC AVKVEKAA