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 B7H1I0

Entry ID Method Resolution Chain Position Source
AF-B7H1I0-F1 Predicted AlphaFoldDB

No variants for B7H1I0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B7H1I0

No associated diseases with B7H1I0

No regional properties for B7H1I0

Type Name Position InterPro Accession
No domain, repeats, and functional sites for B7H1I0

Functions

Description
EC Number 1.1.1.35 With NAD(+) or NADP(+) as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
fatty acid beta-oxidation multienzyme complex A multienzyme complex possessing three kinds of enzymes that catalyze the chain reactions in the fatty acid beta-oxidation cycle, enoyl-CoA hydratase (ECH), 3-hydroxyacyl-CoA dehydrogenase (HACD), and acetyl-CoA C-acyltransferase (KACT).

5 GO annotations of molecular function

Name Definition
3-hydroxyacyl-CoA dehydrogenase activity Catalysis of the reaction: (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H(+).
3-hydroxybutyryl-CoA epimerase activity Catalysis of the reaction: (S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA.
delta(3)-delta(2)-enoyl-CoA isomerase activity Catalysis of the reactions: a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA or a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA.
enoyl-CoA hydratase activity Catalysis of the reaction: (3S)-3-hydroxyacyl-CoA = trans-2-enoyl-CoA + H2O.
NAD+ binding Binding to the oxidized form, NAD, of nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions.

1 GO annotations of biological process

Name Definition
fatty acid beta-oxidation A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MIHAGNAITV QMLADGIAEF RFDLQGESVN KFNRATIEDF KAAIAAVKAN NDIKGLVVTS
70 80 90 100 110 120
GKSTFIVGAD ITEFGQNFAQ GEKAIVDWLM PVHEIFNSFE DLDLPKVAAI NGMALGGGFE
130 140 150 160 170 180
MCLVCDYRVM SEAAQVGLPE IKLGIYPGFG GSVRLSRLIG IDNAVEWMAM ATPKKPAAAL
190 200 210 220 230 240
KDGAVDAVVA ADKLLDAATD LVKQAISGRL NWKAKRQEKL EAVKLNPLEQ MMAFNTAKGA
250 260 270 280 290 300
VLAKANPAQY PAPKLLLDSL QAGASLARDE ALKAEAEGFA KAAVTPQAEA LIGLFINDQV
310 320 330 340 350 360
VKKASKQHEK GAHPVNQAAV LGAGIMGGGI AYQAASKGTP IIMKDIGNPQ LALGMKEANN
370 380 390 400 410 420
LLTKQVERKK MKPVQMGETL ARIRPTLSYE EFKEVDIVIE AVTENPKVKE IVLAETEKNV
430 440 450 460 470 480
RENTIIASNT STISITRLAK ALQRPENFVG MHFFNPVHMM PLVEVIRGEK TSEEAIATTV
490 500 510 520 530 540
VLAQKMGKTP IVVNDCPGFL VNRVLFPYFG AFDLLVKDGA DFQQIDNVMS KFGWPMGPAY
550 560 570 580 590 600
LIDVVGIDTG VHGAEVMAEG FPDRMKPDYK GAIEAMYEAK RLGQKNDVGF YKYELDKKGK
610 620 630 640 650 660
KAKTVDPTAY EVIAPFVTGE KREFDNQEII DRMMLALCNE TVRCLEDNIV ATASEADMAM
670 680 690 700 710
IMGIGFPPFR GGPCRYIDQT GVAEYVALCD KYAHLGKAYE APQMLRDMAA NNKKFYG