Q67QZ1

PR
Gene name
napA
Protein name
Nitrate reductase
Names
Species
Symbiobacterium thermophilum (strain T / IAM 14863)
KEGG Pathway
sth:STH917
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 Q67QZ1

Entry ID Method Resolution Chain Position Source
AF-Q67QZ1-F1 Predicted AlphaFoldDB

No variants for Q67QZ1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q67QZ1

No associated diseases with Q67QZ1

No regional properties for Q67QZ1

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q67QZ1

Functions

Description
EC Number 1.9.6.1 With a nitrogenous group as acceptor
Subcellular Localization
  • Secreted
  • Membrane-associated
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.

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
MKFTRRSFVK ASALATAMVA AGCSPQPVAP KQNPETEGAT WYKTVCRYCG VGCGVMVAAK
70 80 90 100 110 120
DNRVVAVKGD TENPVNKGLL CVKGYYLDRI MNTEEGRILK PLIRKNGQLT EASWDEALDL
130 140 150 160 170 180
VAARFREAID QHGPDSVGFY GSGQNLAEET YIANKLFKGC IGTNNVEGNP RTCMASAVAG
190 200 210 220 230 240
FLSTFGKDEP MGNLDDIEHA DTFFIIGSNT AEAHPIIYSR ITTRKQTGKD VKVILADPRR
250 260 270 280 290 300
HRVADIADIF LPFRPGTDLA LLNAFAQVII EEGLHDPDFI ERHTTFQDGN GAITFEQYVA
310 320 330 340 350 360
FLQDYTPEKV APITGLSPDD IRAAAREIGA RGRKTMTLWC MGINQRTVGT WLNNAIYNLH
370 380 390 400 410 420
LLTGKICQPG NSPFSLTGQP SACGSVREGG GLSHLLPCGR QVTNEQHRKE VAAVWGVDYT
430 440 450 460 470 480
RMSDKVGYHT MEMFRAAGDG RIKALLISCT NPGHSLPNLN SVRASLEKTF LVVMDAFHNR
490 500 510 520 530 540
TTELADVVLP SALWCEKEGI YGNTERRTQH LAKAVEPKGE ARPDVWILLE IAKRLGYGEY
550 560 570 580 590 600
FSHYTSNEVI WEEFRKMGGG GTGYDYAPYE RYKQERGLRW PVNDKQPAGT TLRYVEGDDP
610 620 630 640 650 660
FVPEGAGIYF YGKPDGKAVI YARPHRDPAE VPDAEYPFYL STGRILEHWH TITMTKRVPE
670 680 690 700 710 720
IMKGAGEFYC EIHEEDAARL GIQNGDLVKL TSRRGQVVAT ARVGGRAVPQ KGLVFLLMHD
730 740 750
DRTERLANFL TNDAVDETSK QMEYKVCAVR VEKA