Q5HV12

PR
Gene name
napA
Protein name
Periplasmic nitrate reductase
Names
Species
Campylobacter jejuni (strain RM1221)
KEGG Pathway
cjr:CJE0871
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)

1-61 (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 Q5HV12

Entry ID Method Resolution Chain Position Source
AF-Q5HV12-F1 Predicted AlphaFoldDB

No variants for Q5HV12

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5HV12

No associated diseases with Q5HV12

7 regional properties for Q5HV12

Type Name Position InterPro Accession
conserved_site Twin-arginine translocation pathway, signal sequence 1 - 31 IPR006311
domain Molybdopterin oxidoreductase 96 - 567 IPR006656
domain Molybdopterin dinucleotide-binding domain 714 - 822 IPR006657
domain Molybdopterin oxidoreductase, 4Fe-4S domain 39 - 95 IPR006963
conserved_site Twin-arginine translocation pathway, signal sequence, bacterial/archaeal 3 - 31 IPR019546
binding_site Molybdopterin oxidoreductase, molybdopterin cofactor binding site 44 - 61 IPR027467
domain Nitrate reductase NapA-like, molybdopterin-binding domain 711 - 828 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
MNRRDFIKNT AIASAASVAG LSVPSSMLGA QEEDWKWDKA VCRFCGTGCG IMIARKDGKI
70 80 90 100 110 120
VATKGDPAAP VNRGLNCIKG YFNAKIMYGE DRLVMPLLRM NEKGEFDKKG KFQQVSWQRA
130 140 150 160 170 180
FDEMEKQFKK AYNELGVTGI GIFGSGQYTI QEGYAALKLA KAGFRTNNID PNARHCMASA
190 200 210 220 230 240
VVGFMQTFGV DEPSGCYDDI ELTDTIITWG ANMAEMHPIL WSRVSDRKLS NLDKVKVVNL
250 260 270 280 290 300
STFSNRTSNI ADIEIIFKPN TDLAIWNYIA REIVYNHPEA MDMKFIKDHC VFATGYADIG
310 320 330 340 350 360
YGMRNNPNHP KFKESEKDTV EKENVITLDD EEATSLSYLG VKAGDKFEMK HQGVADKNWE
370 380 390 400 410 420
ISFDEFKKGL APYTLEYTAR VAKGDDNESL EDFKKKLQEL ANLYIEKNRK VVSFWTMGFN
430 440 450 460 470 480
QHTRGSWVNE QAYMVHFLLG KQAKPGSGAF SLTGQPSACG TAREVGTFSH RLPADMVVAN
490 500 510 520 530 540
PKHREISEKI WKVPAKTINP KPGSPYLNIM RDLEDGKIKF AWVQVNNPWQ NTANANHWIA
550 560 570 580 590 600
AAREMDNFIV VSDCYPGISA KVADLILPSA MIYEKWGAYG NAERRTQHWK QQVLPVGAAM
610 620 630 640 650 660
SDTWQILEFA KRFKLKEVWK EQKVDNKLTL PSVLEEAKAM GYSEDDTLFD VLFANKEAKS
670 680 690 700 710 720
FNPNDAIAKG FDNTDVKGDE RKIQGSDGKE FTGYGFFVQK YLWEEYRKFG LGHGHDLADF
730 740 750 760 770 780
DTYHKVRGLR WPVVNGKETQ WRFNTKFDYY AKKAAPNSDF AFYGDFNKML TNGDLIAPKD
790 800 810 820 830 840
EKEHSIKNKA KIFFRPFMKA PERPSKEYPF WLATGRVLEH WHSGTMTMRV PELYRAVPEA
850 860 870 880 890 900
LCYMSEKDGE KLGLNQGDLV WVESRRGKVK ARVDMRGRNK PPVGLVYVPW FDENVYINKV
910 920
TLDATCPLSK QTDFKKCAVK IYKA