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 B5XVW2

Entry ID Method Resolution Chain Position Source
AF-B5XVW2-F1 Predicted AlphaFoldDB

No variants for B5XVW2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B5XVW2

No associated diseases with B5XVW2

4 regional properties for B5XVW2

Type Name Position InterPro Accession
domain 3-hydroxyacyl-CoA dehydrogenase, C-terminal 492 - 586 IPR006108-1
domain 3-hydroxyacyl-CoA dehydrogenase, C-terminal 619 - 703 IPR006108-2
domain 3-hydroxyacyl-CoA dehydrogenase, NAD binding 311 - 489 IPR006176
conserved_site 3-hydroxyacyl-CoA dehydrogenase, conserved site 489 - 514 IPR006180

Functions

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

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

4 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.
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
MDTVSAFKLE VRADKIAVIT IDAPGEKMNT LKAEFGNQVR GLIRQVRDDK SVRGVVFISA
70 80 90 100 110 120
KTDNFIAGAD INMIARCRSA QEAEALARQG QQIMAEIHGL SIPVIAAIHG ACLGGGLELA
130 140 150 160 170 180
LACHGRICSD DEKTRLGLPE VQLGLLPGSG GTQRLPRLIG VSTALDMMLT GRQLRARQAL
190 200 210 220 230 240
KAGLVDEVVP QAILLQAAVE LALKGRPASR DMPVRERVLA GPLGRHLLFH FVGKQTQRKT
250 260 270 280 290 300
QGNYPAVKRI LQVVENGLAH GCSSGYAEEA RAFGELAMTP QSQALRSIFF ASTDLKKDRG
310 320 330 340 350 360
AEAEPGPLTS IAVLGGGLMG GGIAYVTACK GGLPVRIKDI QPRGINHALK YSWDLLNKQV
370 380 390 400 410 420
RQRRLRPSER DRQMAMISGA TDYQGFAHRD VVIEAVFEDL ALKQRMVSEV EQYCGPQTIF
430 440 450 460 470 480
ASNTSSLPIG DIAAQARRPG RVIGLHFFSP VEKMPLVEVI PHKGTDPQAI ATVVQLAKRQ
490 500 510 520 530 540
GKTPIVVADK AGFYVNRILA PYINEAMRLL VEGEPVEEID KALVKFGFPV GPIQLLDEVG
550 560 570 580 590 600
IDTGTKIIPV LESAFGERFS SPANIIDAIL KDDRKGRKNN RGFYLYETKG RKSKKRPDPA
610 620 630 640 650 660
VYPLLGIDRP QSRLSAQQVA ERCVMMMLNE AARCFDEQII RSARDGDIGA VFGIGFPPFL
670 680 690 700 710
GGPFRYMDTI GAGEVAAILQ RLAAQYGPRF TPCDTLLRMA EQGTTFWPAD ERLT