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

6 structures for P16099

Entry ID Method Resolution Chain Position Source
1DJN X-ray 220 A A/B 2-730 PDB
1DJQ X-ray 220 A A/B 2-730 PDB
1O94 X-ray 200 A A/B 2-730 PDB
1O95 X-ray 370 A A/B 2-730 PDB
2TMD X-ray 240 A A/B 2-730 PDB
AF-P16099-F1 Predicted AlphaFoldDB

No variants for P16099

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P16099

No associated diseases with P16099

No regional properties for P16099

Type Name Position InterPro Accession
No domain, repeats, and functional sites for P16099

Functions

Description
EC Number 1.5.8.2 With a flavin 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

4 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.
FMN binding Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
metal ion binding Binding to a metal ion.
trimethylamine dehydrogenase activity Catalysis of the reaction: trimethylamine + H2O + electron-transferring flavoprotein = dimethylamine + formaldehyde + reduced electron-transferring flavoprotein.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MARDPKHDIL FEPIQIGPKT LRNRFYQVPH CIGAGSDKPG FQSAHRSVKA EGGWAALNTE
70 80 90 100 110 120
YCSINPESDD THRLSARIWD EGDVRNLKAM TDEVHKYGAL AGVELWYGGA HAPNMESRAT
130 140 150 160 170 180
PRGPSQYASE FETLSYCKEM DLSDIAQVQQ FYVDAAKRSR DAGFDIVYVY GAHSYLPLQF
190 200 210 220 230 240
LNPYYNKRTD KYGGSLENRA RFWLETLEKV KHAVGSDCAI ATRFGVDTVY GPGQIEAEVD
250 260 270 280 290 300
GQKFVEMADS LVDMWDITIG DIAEWGEDAG PSRFYQQGHT IPWVKLVKQV SKKPVLGVGR
310 320 330 340 350 360
YTDPEKMIEI VTKGYADIIG CARPSIADPF LPQKVEQGRY DDIRVCIGCN VCISRWEIGG
370 380 390 400 410 420
PPMICTQNAT AGEEYRRGWH PEKFRQTKNK DSVLIVGAGP SGSEAARVLM ESGYTVHLTD
430 440 450 460 470 480
TAEKIGGHLN QVAALPGLGE WSYHRDYRET QITKLLKKNK ESQLALGQKP MTADDVLQYG
490 500 510 520 530 540
ADKVIIATGA RWNTDGTNCL THDPIPGADA SLPDQLTPEQ VMDGKKKIGK RVVILNADTY
550 560 570 580 590 600
FMAPSLAEKL ATAGHEVTIV SGVHLANYMH FTLEYPNMMR RLHELHVEEL GDHFCSRIEP
610 620 630 640 650 660
GRMEIYNIWG DGSKRTYRGP GVSPRDANTS HRWIEFDSLV LVTGRHSECT LWNELKARES
670 680 690 700 710 720
EWAENDIKGI YLIGDAEAPR LIADATFTGH RVAREIEEAN PQIAIPYKRE TIAWGTPHMP
GGNFKIEYKV