FAHD1

FAHD1
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	1SAW
Identifikatori
Aliasi	FAHD1
Vanjski ID-jevi	OMIM: 616320 MGI: 1915886 HomoloGene: 6774 GeneCards: FAHD1
EC broj	4.1.1.112
Lokacija gena (miš)
Hrom.	Hromosom 17 (miš)
Kraj	25,069,338 bp
Ontologija gena
Molekularna funkcija	• acetylpyruvate hydrolase activity; • acylpyruvate hydrolase activity; • catalytic activity; • hydrolase activity; • fumarylpyruvate hydrolase activity; • vezivanje iona metala; • lyase activity; • oxaloacetate decarboxylase activity;
Ćelijska komponenta	• citosol; • mitohondrija; • nukleoplazma; • citoplazma; • mitochondrial matrix;
Biološki proces	• metabolizam; • Krebsov ciklus;
	Izvori:Amigo / QuickGO
Ortolozi
	81889
	68636
	n/a
	ENSMUSG00000045316
	Q6P587
	Q8R0F8
	NM_031208; NM_001018104; NM_001142398
	NM_023480
	NP_001018114; NP_001135870; NP_112485
	NP_075969
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Protein 1 fumarilacetoacetat-hidrolaznog domena, znan i kao protein FLJ36880, je enzim koji jr kod ljudi kodiran genom FAHD1 sa hromosoma 16.^[4]

Struktura

Gen FAHD1 kodira protein od 24 kDa koji je lokaliziran u mitohondrijama i pripada proteinskoj porodici fumarilacetoacetat-hidrolaza.^[5] Struktura FAHD1 razriješena je primjenom rendgenske kristalografije pri rezoluciji od 2,2 Å. Ukupna struktura slična je C-terminalnom domenu bifunkcionalnog enzima HpcE iz Escherichia coli C, fumarilacetoacetat-hidrolaze Mus musculus i YcgM (Apc5008) iz E. coli 1262.^[5] Za njegovu katalitsku aktivnost , čini se važnim broj konzerviranih aminokiselina, uključujući Asp-102 i Arg-106 FAHD1.^[6]

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 224 aminokiseline, a molekulska težina 24.843 Da.^[7].

10	20	30	40	50
MGIMAASRPL	SRFWEWGKNI	VCVGRNYADH	VREMRSAVLS	EPVLFLKPST
AYAPEGSPIL	MPAYTRNLHH	ELELGVVMGK	RCRAVPEAAA	MDYVGGYALC
LDMTARDVQD	ECKKKGLPWT	LAKSFTASCP	VSAFVPKEKI	PDPHKLKLWL
KVNGELRQEG	ETSSMIFSIP	YIISYVSKII	TLEEGDIILT	GTPKGVGPVK
ENDEIEAGIH	GLVSMTFKVE	KPEY

Simboli

C: Cistein
D: Asparaginska kiselina
E: Glutaminska kiselina
F: Fenilalanin
G: Glicin
H: Histidin
I: Izoleucin
K: Lizin
L: Leucin
M: Metionin
N: Asparagin
P: Prolin
Q: Glutamin
R: Arginin
S: Serin
T: Treonin
V: Valin
W: Triptofan
Y: Tirozin

Funkcija

Pokazalo se da u eukariota protein FAHD1 funkcionira kao oksaloacetat-dekarboksilaza s.^[8] Protein FAHD1 vjerovatno također funkcionira kao acilpiruvaza, a pokazalo se da katalizira hidrolizu acetilpiruvata i fumarilpiruvata u in vitro eksperimentima.^[5] Za maksimalnu aktivnost enzima bio je potreban Mg (2+).^[6]

Reference

1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000045316 - Ensembl, maj 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Entrez Gene: FAHD1 fumarylacetoacetate hydrolase domain containing 1".
1 2 3 Manjasetty BA, Niesen FH, Delbrück H, Götz F, Sievert V, Büssow K, Behlke J, Heinemann U (2004). "X-ray structure of fumarylacetoacetate hydrolase family member Homo sapiens FLJ36880". Biol. Chem. 385 (10): 935–42. doi:10.1515/BC.2004.122. PMID 15551868. S2CID 16759973.
1 2 Pircher H, Straganz GD, Ehehalt D, Morrow G, Tanguay RM, Jansen-Dürr P (2011). "Identification of human fumarylacetoacetate hydrolase domain-containing protein 1 (FAHD1) as a novel mitochondrial acylpyruvase". J. Biol. Chem. 286 (42): 36500–8. doi:10.1074/jbc.M111.264770. PMC 3196145. PMID 21878618.
↑ "UniProt, Q6P587". Pristupljeno 5. 7. 2021.
↑ Pircher H, von Grafenstein S, Diener T, Metzger C, Albertini E, Taferner A, Unterluggauer H, Kramer C, Liedl KR, Jansen-Dürr P (2015). "Identification of FAH domain-containing protein 1 (FAHD1) as oxaloacetate decarboxylase". J. Biol. Chem. 290 (11): 6755–62. doi:10.1074/jbc.M114.609305. PMC 4358102. PMID 25575590.

Dopunska literatura

Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
Daniels RJ, Peden JF, Lloyd C, et al. (2001). "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16". Hum. Mol. Genet. 10 (4): 339–52. doi:10.1093/hmg/10.4.339. PMID 11157797.
Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
Simpson JC, Wellenreuther R, Poustka A, et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Lehner B, Sanderson CM (2004). "A protein interaction framework for human mRNA degradation". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to biology: a functional genomics pipeline". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
Manjasetty BA, Niesen FH, Delbrück H, et al. (2005). "X-ray structure of fumarylacetoacetate hydrolase family member Homo sapiens FLJ36880". Biol. Chem. 385 (10): 935–42. doi:10.1515/BC.2004.122. PMID 15551868. S2CID 16759973.
Mehrle A, Rosenfelder H, Schupp I, et al. (2006). "The LIFEdb database in 2006". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.

Vanjski linkovi

[refGRCm38Ensembl-1] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000045316 - Ensembl, maj 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-4] "Entrez Gene: FAHD1 fumarylacetoacetate hydrolase domain containing 1".

[Manjasetty_BA_2004-5] 1 2 3 Manjasetty BA, Niesen FH, Delbrück H, Götz F, Sievert V, Büssow K, Behlke J, Heinemann U (2004). "X-ray structure of fumarylacetoacetate hydrolase family member Homo sapiens FLJ36880". Biol. Chem. 385 (10): 935–42. doi:10.1515/BC.2004.122. PMID 15551868. S2CID 16759973.

[ReferenceA-6] 1 2 Pircher H, Straganz GD, Ehehalt D, Morrow G, Tanguay RM, Jansen-Dürr P (2011). "Identification of human fumarylacetoacetate hydrolase domain-containing protein 1 (FAHD1) as a novel mitochondrial acylpyruvase". J. Biol. Chem. 286 (42): 36500–8. doi:10.1074/jbc.M111.264770. PMC 3196145. PMID 21878618.

[UniProt-7] "UniProt, Q6P587". Pristupljeno 5. 7. 2021.

[8] Pircher H, von Grafenstein S, Diener T, Metzger C, Albertini E, Taferner A, Unterluggauer H, Kramer C, Liedl KR, Jansen-Dürr P (2015). "Identification of FAH domain-containing protein 1 (FAHD1) as oxaloacetate decarboxylase". J. Biol. Chem. 290 (11): 6755–62. doi:10.1074/jbc.M114.609305. PMC 4358102. PMID 25575590.

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]