A1SWQ0

PR
Gene name
napA
Protein name
Periplasmic nitrate reductase
Names
Species
Psychromonas ingrahamii (strain 37)
KEGG Pathway
pin:Ping_2174
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)

1-64 (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 A1SWQ0

Entry ID Method Resolution Chain Position Source
AF-A1SWQ0-F1 Predicted AlphaFoldDB

No variants for A1SWQ0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1SWQ0

No associated diseases with A1SWQ0

2 regional properties for A1SWQ0

Type Name Position InterPro Accession
domain Glucosamine/galactosamine-6-phosphate isomerase 17 - 229 IPR006148
conserved_site Glucosamine-6-phosphate isomerase, conserved site 125 - 143 IPR018321

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
MKFTRREFMK AQAAASAAAV AGIALPATAS NLIASQDLTK IKWEKAPCRF CGTGCSVLVG
70 80 90 100 110 120
TQHGRVVATQ GDPESPVNKG LNCVKGYFLS KIMYGKDRLT TPLLRMTEGV YDKNGQFEPV
130 140 150 160 170 180
SWDAAFDIMA DKFKDALKKK GPTAVGMFGS GQWTLWEGYA ASKLMKAGFR TNNLDPNARH
190 200 210 220 230 240
CMASAVGGFM RTFGIDEPMG CYDDLENADV FVLWGSNMAE MHPILWSRLA DRRLSNPDVS
250 260 270 280 290 300
VHVLSTYTHR SFELADNGMI FTPQSDLAIL NFIANYIIQN DAVDKDFIEK HTNFRKGVTD
310 320 330 340 350 360
IGYGLRPTDP LQKAAENPDS GASSPITFEE FAEYVSEFDV DYAVKMSGVP AEKLIELAKV
370 380 390 400 410 420
YADPAKKVVS YWTMGFNQHT RGVWANNLMY NVHLLTGKIS KPGSGPFSLT GQPSACGTAR
430 440 450 460 470 480
EVGTFSHRLP ADLVVANPKH RAIAEKLWKL PEGTIEPKPG YHAVLQNRML KDSKLNAYWV
490 500 510 520 530 540
MCNNNVQAGA NINEEIIPGY RNPENFIVVS DPYPTVTAQM GDLILPTAMW VEKEGAYGNA
550 560 570 580 590 600
ERRTQFWHQQ VKAPEGAKSD LWQLVEFSKR FKIEEVWTED LIAKMPEVRG ETLFDVLYKN
610 620 630 640 650 660
GQVDAFGLDE VADERLNDEA RDFGFYIQKG LFEEYASFGR GHGHDLAPFD QYHEARGLRW
670 680 690 700 710 720
PVVNGKETLW RFREGYDPYV EKGSEVQFYG HPDKKAVIFA LPYEPPAESP DQEYDLWLST
730 740 750 760 770 780
GRVLEHWHSG SMTRRVPELY KAFPDAVVFM HPDDATARGV RRGDEIVLAS RRGELTSRVE
790 800 810 820 830
TRGRNRPPRG LVFMPWFDAK QLVNKITLDA TDPLSKQTDY KKCAVKITKK V