Q5R1W7

PR
Gene name
HADHB
Protein name
Trifunctional enzyme subunit beta, mitochondrial
Names
TP-beta
Species
Pan troglodytes (Chimpanzee)
KEGG Pathway
ptr:459080
EC number
2.3.1.16: Transferring groups other than amino-acyl groups
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-73 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q5R1W7

Entry ID Method Resolution Chain Position Source
AF-Q5R1W7-F1 Predicted AlphaFoldDB

No variants for Q5R1W7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5R1W7

No associated diseases with Q5R1W7

5 regional properties for Q5R1W7

Type Name Position InterPro Accession
active_site Thiolase, active site 454 - 467 IPR020610
conserved_site Thiolase, conserved site 419 - 435 IPR020613
active_site Thiolase, acyl-enzyme intermediate active site 135 - 153 IPR020615
domain Thiolase, N-terminal 55 - 325 IPR020616
domain Thiolase, C-terminal 332 - 471 IPR020617

Functions

Description
EC Number 2.3.1.16 Transferring groups other than amino-acyl groups
Subcellular Localization
  • Mitochondrion
  • Mitochondrion inner membrane
  • Mitochondrion outer membrane
  • Endoplasmic reticulum
  • Protein stability and association with membranes require HADHA
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
mitochondrial fatty acid beta-oxidation multienzyme complex A complex that includes the long-chain 3-hydroxyacyl-CoA dehydrogenase and long-chain enoyl-CoA hydratase activities in two subunits (alpha and beta), catalyzing two steps of the fatty acid beta-oxidation cycle within the mitochondrial matrix.
mitochondrial inner membrane The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
mitochondrial nucleoid The region of a mitochondrion to which the DNA is confined.
mitochondrial outer membrane The outer, i.e. cytoplasm-facing, lipid bilayer of the mitochondrial envelope.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

2 GO annotations of molecular function

Name Definition
acetyl-CoA C-acyltransferase activity Catalysis of the reaction: acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.
acetyl-CoA C-myristoyltransferase activity Catalysis of the reaction: myristoyl-CoA + acetyl-CoA = 3-oxopalmitoyl-CoA + CoA.

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).

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P55084 HADHB Trifunctional enzyme subunit beta, mitochondrial Homo sapiens (Human) PR
P34255 B0303.3 Probable 3-ketoacyl-CoA thiolase Caenorhabditis elegans PR
10 20 30 40 50 60
MTTILTYPFK NLPTASKWAL RFSIRPLSCS SQLRAAPAVQ TKTKKTLAKP NIRNVVVVDG
70 80 90 100 110 120
VRTPFLLSGT SYKDLMPHDL ARAALTGLLH RTSVPKEVVD YIIFGTVIQE VKTSNVAREA
130 140 150 160 170 180
ALGAGFSDKT PAHTVTMACI SANQAMTTGV GLIASGQCDV IVAGGVELMS DVPIRHSRKM
190 200 210 220 230 240
RKLMLDLNKA KSMGQRLSLI SKFRFNFLAP ELPAVSEFST SETMGHSADR LAAAFAVSRL
250 260 270 280 290 300
EQDEYALRSH SLAKKAQDEG LLSDVVPFKV PGKDTVTKDN GIRPSSLEQM AKLKPAFIKP
310 320 330 340 350 360
YGTVTAANSS FLTDGASAML IMAEEKALAM GYKPKAYLRD FMYVSQDPKD QLLLGPTYAT
370 380 390 400 410 420
PKVLEKAGLT MNDIDAFEFH EAFSGQILAN FKAMDSDWFA ENYMGRKTKV GLPPLEKFNN
430 440 450 460 470
WGGSLSLGHP FGATGCRLVM AAANRLRKEG GQYGLVAACA AGGQGHAMIV EAYPK