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 B9L8L4

Entry ID Method Resolution Chain Position Source
AF-B9L8L4-F1 Predicted AlphaFoldDB

No variants for B9L8L4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B9L8L4

No associated diseases with B9L8L4

7 regional properties for B9L8L4

Type Name Position InterPro Accession
conserved_site Twin-arginine translocation pathway, signal sequence 1 - 31 IPR006311
domain Molybdopterin oxidoreductase 97 - 617 IPR006656
domain Molybdopterin dinucleotide-binding domain 823 - 930 IPR006657
domain Molybdopterin oxidoreductase, 4Fe-4S domain 40 - 96 IPR006963
conserved_site Twin-arginine translocation pathway, signal sequence, bacterial/archaeal 2 - 29 IPR019546
binding_site Molybdopterin oxidoreductase, molybdopterin cofactor binding site 45 - 63 IPR027467
domain Nitrate reductase NapA-like, molybdopterin-binding domain 821 - 937 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
MSMNRREFLK TTAAAAAASA VGISIPSEAK AAAENTQAGW QWDKAVCRFC GTGCGIMVAV
70 80 90 100 110 120
KDDKIVAVKG DPESPVNRGI NCIKGYFNAK IMYGADRLTQ PLLRMNDKGE FDKNGKFRPV
130 140 150 160 170 180
SWKRAFDEME KQFKKYYNEL GPTGVAVFGS GQYTIQEGYA AVKLVKAGWR SNNIDPNARH
190 200 210 220 230 240
CMASAVVGFY QTFGIDEPAG CYDDIEITDT VFVWGANMAE MHPILWSRVS DAKLNNPDKY
250 260 270 280 290 300
FIVNLSTYRN RCSNLADMEI IFRPNADLAI MNYLGREILK RNAVNWDFVK KHTIFATGHA
310 320 330 340 350 360
DIGYGMRNPN SPHVTDKERD TVAKQVAKVV TEEEAVALSP IGKWKAGDEM QMTHTAGKKP
370 380 390 400 410 420
FWHWQISFDD FKKAVEPYTL DYVAKVAKGD PDESLDSFKR KLQKLADLYC DPNRKALSFW
430 440 450 460 470 480
TMGFNQHVRG SWINELVYMV HLLLGKQSQP GSGAFSLTGQ PSACGTAREV GTFAHRLPAD
490 500 510 520 530 540
MLVGNPKHRK ITEKMWKIPE GTLNPKVGSH FLKIMRDIED GKIKWAWVHV NNPWQNTANA
550 560 570 580 590 600
NHWIKAARTM DNFIVVNEAY PGVSARVADL ILPVSMIYEK WGAYGNAERR TQHWRQQVTP
610 620 630 640 650 660
PGEAMPDLWT IMEFSKRFKL KEVWKAHPQA KLPSVLDKAQ AMGYDPEMTL FDVLFNRPEY
670 680 690 700 710 720
RKNFPWPDPI AKNPQTGKLH ANTEAGGDGR TIIGADGKEW KGYGFFVHKA LWEEYRKFGL
730 740 750 760 770 780
GHAHDLADFD TYHKVRGLRW PVVNGKETKW RFNAEYDPYA RKYAKPGEKF AFYGPLLKAL
790 800 810 820 830 840
KRGDLKGPKT KQKYSLKNKA KIFWRPFMVH PEDPKYDTKG YNFWLCTGRV LEHWHSGTMT
850 860 870 880 890 900
MRVPELYRAM PEALCYMNPK DAKELGLNRF DLVVVESRRG KVKARVETRG RNKPPRGLVY
910 920 930
VPWFDEKVLI NKVCLDATCP LSKETDYKKA AVKVYKA