CAZyme Information: PTTG_30347-t43_1-p1

Basic Information

• Species: Puccinia triticina
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia triticina
• CAZyme ID: PTTG_30347-t43_1-p1
• CAZy Family: GT90
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
405		44072.95	8.7359

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ptriticina1-1BBBDRace1	15692	630390	814	14878

• Gene Location: location=ADAS02003024.1:161-1617(-)

Full Sequence      

MPRIQSHATARLFQSIYPHDPKIAAGNPTPSPSDDPHSPLRRSRPHRPLASVNGDRQTTT
ISAVPPSPLAPAPSLSTLASTPTSPCRPTTSATTSWAPLAIDELAKRFQPVWITQSPLSC
RLSPKTEALIWMRFLDGAGRTKGALKVMIALNLHSSQQLLPVITNAILTLLRYLGAENVG
LGVQHHMRCAMEETIWMGVDRIKLLSEYRNQALLAFDNADRALDGLSNLVFINDVFLCAQ
DILELLWQRRFQGADSACGTDWWEAKTLREQYGSQTPRRPTTPARTPAYAEAACAPIDFP
IAPTLAIPMALEKAGLEFKDMTKIEINEAFPVVALASMKILGIKAEKVNVNGGAVALGHP
IGSSCCWIVVSLINSLKPGEYGVAGVCNGVSRYLSSSLFFLHRLP

Enzyme Prediction     

No EC number prediction in PTTG_30347-t43_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT69	181	272	4.7e-19	0.39748953974895396

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
397094	Thiolase_C	7.06e-42	284	389	5	112	Thiolase, C-terminal domain. Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
215347	PLN02644	4.64e-41	284	389	274	381	acetyl-CoA C-acetyltransferase
238383	thiolase	4.49e-40	284	389	268	375	Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
273881	AcCoA-C-Actrans	6.61e-37	284	389	268	375	acetyl-CoA acetyltransferases. This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation. [Fatty acid and phospholipid metabolism, Other]
181311	PRK08235	7.40e-33	278	389	270	381	acetyl-CoA C-acetyltransferase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDR42100.1|GT69	7.64e-17	146	262	35	172
CED82005.1|GT69	1.42e-14	149	265	170	327
CDR42098.1|GT69	6.54e-14	95	262	182	376
QRC99639.1|GT69	2.63e-10	150	262	134	271
CAK43148.1|GT69	1.37e-08	150	275	116	270

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2IBU_A	8.21e-29	284	389	278	383	Chain A, Acetyl-CoA acetyltransferase [Homo sapiens],2IBU_B Chain B, Acetyl-CoA acetyltransferase [Homo sapiens],2IBU_C Chain C, Acetyl-CoA acetyltransferase [Homo sapiens],2IBU_D Chain D, Acetyl-CoA acetyltransferase [Homo sapiens],2IBW_A Chain A, Acetyl-CoA acetyltransferase [Homo sapiens],2IBW_B Chain B, Acetyl-CoA acetyltransferase [Homo sapiens],2IBW_C Chain C, Acetyl-CoA acetyltransferase [Homo sapiens],2IBW_D Chain D, Acetyl-CoA acetyltransferase [Homo sapiens],2IBY_A Chain A, Acetyl-CoA acetyltransferase [Homo sapiens],2IBY_B Chain B, Acetyl-CoA acetyltransferase [Homo sapiens],2IBY_C Chain C, Acetyl-CoA acetyltransferase [Homo sapiens],2IBY_D Chain D, Acetyl-CoA acetyltransferase [Homo sapiens]
2IB7_A	8.21e-29	284	389	278	383	Chain A, Acetyl-CoA acetyltransferase [Homo sapiens],2IB7_B Chain B, Acetyl-CoA acetyltransferase [Homo sapiens],2IB7_C Chain C, Acetyl-CoA acetyltransferase [Homo sapiens],2IB7_D Chain D, Acetyl-CoA acetyltransferase [Homo sapiens],2IB8_A Chain A, Acetyl-CoA acetyltransferase [Homo sapiens],2IB8_B Chain B, Acetyl-CoA acetyltransferase [Homo sapiens],2IB8_C Chain C, Acetyl-CoA acetyltransferase [Homo sapiens],2IB8_D Chain D, Acetyl-CoA acetyltransferase [Homo sapiens],2IB9_A Chain A, Acetyl-CoA acetyltransferase [Homo sapiens],2IB9_B Chain B, Acetyl-CoA acetyltransferase [Homo sapiens],2IB9_C Chain C, Acetyl-CoA acetyltransferase [Homo sapiens],2IB9_D Chain D, Acetyl-CoA acetyltransferase [Homo sapiens]
2F2S_A	9.57e-29	284	389	289	394	Human mitochondrial acetoacetyl-CoA thiolase [Homo sapiens],2F2S_B Human mitochondrial acetoacetyl-CoA thiolase [Homo sapiens],2F2S_C Human mitochondrial acetoacetyl-CoA thiolase [Homo sapiens],2F2S_D Human mitochondrial acetoacetyl-CoA thiolase [Homo sapiens]
6BJ9_A	2.84e-28	284	389	276	381	Crystal structure of Acat2 thiolase from Ascaris suum [Ascaris suum],6BJ9_B Crystal structure of Acat2 thiolase from Ascaris suum [Ascaris suum]
6BJB_A	2.84e-28	284	389	276	381	Crystal structure of Acat2-C91S thiolase from Ascaris suum in complex with propionyl-CoA and nitrate [Ascaris suum],6BJB_B Crystal structure of Acat2-C91S thiolase from Ascaris suum in complex with propionyl-CoA and nitrate [Ascaris suum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q6L8K7|THIL_YARLI	5.56e-32	284	389	276	381	Acetyl-CoA acetyltransferase OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=PAT1 PE=3 SV=1
sp|Q29RZ0|THIL_BOVIN	7.70e-31	284	389	305	410	Acetyl-CoA acetyltransferase, mitochondrial OS=Bos taurus OX=9913 GN=ACAT1 PE=2 SV=1
sp|Q6AZA0|THIL_DANRE	1.95e-30	284	389	303	408	Acetyl-CoA acetyltransferase, mitochondrial OS=Danio rerio OX=7955 GN=acat1 PE=2 SV=1
sp|Q8QZT1|THIL_MOUSE	7.37e-30	284	389	307	412	Acetyl-CoA acetyltransferase, mitochondrial OS=Mus musculus OX=10090 GN=Acat1 PE=1 SV=1
sp|I1RMA2|ER10A_GIBZE	1.10e-29	265	389	295	415	Acetyl-CoA acetyltransferase FG05087, mitochondrial OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FG05087 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000046	0.000000

TMHMM  Annotations     

There is no transmembrane helices in PTTG_30347-t43_1-p1.