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 Q1LTP1

Entry ID Method Resolution Chain Position Source
AF-Q1LTP1-F1 Predicted AlphaFoldDB

No variants for Q1LTP1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q1LTP1

No associated diseases with Q1LTP1

15 regional properties for Q1LTP1

Type Name Position InterPro Accession
domain Flavodoxin-like 60 - 73 IPR001094-1
domain Flavodoxin-like 108 - 119 IPR001094-2
domain Flavodoxin-like 140 - 150 IPR001094-3
domain Flavodoxin-like 164 - 183 IPR001094-4
domain Oxidoreductase FAD/NAD(P)-binding 453 - 559 IPR001433
domain Flavoprotein pyridine nucleotide cytochrome reductase 266 - 276 IPR001709-1
domain Flavoprotein pyridine nucleotide cytochrome reductase 382 - 389 IPR001709-2
domain Flavoprotein pyridine nucleotide cytochrome reductase 452 - 471 IPR001709-3
domain Flavoprotein pyridine nucleotide cytochrome reductase 477 - 486 IPR001709-4
domain Flavoprotein pyridine nucleotide cytochrome reductase 490 - 501 IPR001709-5
domain Flavoprotein pyridine nucleotide cytochrome reductase 521 - 537 IPR001709-6
domain Flavoprotein pyridine nucleotide cytochrome reductase 544 - 552 IPR001709-7
domain Sulfite reductase [NADPH] flavoprotein alpha-component-like, FAD-binding 229 - 420 IPR003097
domain Flavodoxin/nitric oxide synthase 59 - 197 IPR008254
domain FAD-binding domain, ferredoxin reductase-type 230 - 444 IPR017927

Functions

Description
EC Number 1.8.1.2 With NAD(+) or NADP(+) as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

3 GO annotations of molecular function

Name Definition
flavin adenine dinucleotide binding Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
FMN binding Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
sulfite reductase (NADPH) activity Catalysis of the reaction: hydrogen sulfide + 3 NADP+ + 3 H2O = sulfite + 3 NADPH + 3 H+.

3 GO annotations of biological process

Name Definition
cysteine biosynthetic process The chemical reactions and pathways resulting in the formation of cysteine, 2-amino-3-mercaptopropanoic acid.
hydrogen sulfide biosynthetic process The chemical reactions and pathways resulting in the formation of hydrogen sulfide, H2S.
sulfate assimilation The pathways by which inorganic sulfate is processed and incorporated into sulfated compounds.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTQQNAPKDL PPLSAEQLDR LQAISSDLSN LQLAWASGYL WNKASHSIPI DYTASQQVIT
70 80 90 100 110 120
VLSASQTGNA RRLAVQLYED LLAAQLSVVI INAGDYKFKQ IAQEKWLLIV TSTQGDGDPP
130 140 150 160 170 180
EEAIALYKYL FSKKAPVLNN IQFAIFGLGD SSYTYFAKIG KDFDSRLAEL GAQRLYDRVD
190 200 210 220 230 240
ADVDYQEKAD IWRREIVKIL QTKLVTVNAK QQLSVINNRI EVKNNLYTKE EPFTAHLVVK
250 260 270 280 290 300
QKITSRSSKK DIRHLEIDIA GSGLNYQPGD ALGVWYENDP VLISEILELL GLTGNELVQV
310 320 330 340 350 360
KEKNIPLNEA LQKHYELTNN TAEIVKSYAY ITRNSSLLAL VDDQQQLKQF AFSTPFIDMI
370 380 390 400 410 420
QRIPVELHPK QLLTLLRPLM PRLYSIASSQ AEVGDEVHLT VSVVRYEIDG KIRTGGASSY
430 440 450 460 470 480
LAYRLQESEP IRVFIEHNDN FRLPNNPNTA IIMIGSGTGI APFRGFMQQR EATTAKGKNW
490 500 510 520 530 540
LFFGNQHLTD DFLYQVEWQR YIKNGLLNKI DVAWSQDQNK KIYVQDRLLE KGIELWNWIQ
550 560 570 580 590
DGAHIYVCGN ANLMARDVEK ALVKLIAIHG RMDYEQADEF LSELRIARRF QRDTY