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CAZyme Information: QEO24085.1

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Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species [Candida] auris
Lineage Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; [Candida] auris
CAZyme ID QEO24085.1
CAZy Family GT71
CAZyme Description branched-chain-amino-acid_aminotransferase,_cytosolic
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1205 CP043536|CGC3 137576.00 7.0551
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_CaurisB11220 5494 N/A 167 5327
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.113:6

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH47 44 512 1.8e-129 0.9932735426008968

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
396217 Glyco_hydro_47 1.53e-139 43 512 1 452
Glycosyl hydrolase family 47. Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2).
237363 PRK13357 4.15e-128 843 1205 4 356
branched-chain amino acid aminotransferase; Provisional
238798 BCAT_beta_family 8.73e-126 894 1193 1 279
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the branched-chain amino acids leusine, isoleucine and valine to their respective alpha-keto acids, alpha-ketoisocaproate, alpha-keto-beta-methylvalerate and alpha-ketoisovalerate. The enzyme requires pyridoxal 5'-phosphate (PLP) as a cofactor to catalyze the reaction. It has been found that mammals have two foms of the enzyme - mitochondrial and cytosolic forms while bacteria contain only one form of the enzyme. The mitochondrial form plays a significant role in skeletal muscle glutamine and alanine synthesis and in interorgan nitrogen metabolism.Members of this subgroup are widely distributed in all three forms of life.
233278 ilvE_II 2.67e-93 882 1196 1 304
branched-chain amino acid aminotransferase, group II. Among the class IV aminotransferases are two phylogenetically separable groups of branched-chain amino acid aminotransferase (IlvE). The last common ancestor of the two lineages appears also to have given rise to a family of D-amino acid aminotransferases (DAAT). This model represents the IlvE family less similar to the DAAT family. [Amino acid biosynthesis, Pyruvate family]
238254 PLPDE_IV 8.48e-77 901 1187 3 256
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, one of five classes of PLPDE, consists of branched-chain amino acid aminotransferases (BCAT), D-amino acid transferases (DAAT), and 4-amino-4-deoxychorismate lyases (ADCL). BCAT catalyzes the reversible transamination reaction between the L-branched-chain amino and alpha-keto acids. DAAT catalyzes the synthesis of D-glutamic acid and D-alanine, and ADCL converts 4-amino-4-deoxychorismate to p-aminobenzoate and pyruvate. Except for a few enzymes, i. e., Escherichia coli and Salmonella BCATs, which are homohexamers arranged as a double trimer, the class IV PLPDEs are homodimers. Homodimer formation is required for catalytic activity.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 1205 1 1205
0.0 1 1205 1 1205
0.0 1 808 1 808
0.0 1 808 1 808
0.0 52 807 1 757

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.64e-97 841 1204 27 385
Chain A, branched chain aminotransferase 1, cytosolic [Homo sapiens],2COG_B Chain B, branched chain aminotransferase 1, cytosolic [Homo sapiens],2COI_A Chain A, branched chain aminotransferase 1, cytosolic [Homo sapiens],2COI_B Chain B, branched chain aminotransferase 1, cytosolic [Homo sapiens],2COJ_A Chain A, branched chain aminotransferase 1, cytosolic [Homo sapiens],2COJ_B Chain B, branched chain aminotransferase 1, cytosolic [Homo sapiens]
4.53e-94 841 1204 7 365
Crystal structure of human branched chain amino acid transaminase in a complex with an inhibitor, C16H10N2O4F3SCl, and pyridoxal 5' phosphate. [Homo sapiens],2ABJ_D Crystal structure of human branched chain amino acid transaminase in a complex with an inhibitor, C16H10N2O4F3SCl, and pyridoxal 5' phosphate. [Homo sapiens],2ABJ_G Crystal structure of human branched chain amino acid transaminase in a complex with an inhibitor, C16H10N2O4F3SCl, and pyridoxal 5' phosphate. [Homo sapiens],2ABJ_J Crystal structure of human branched chain amino acid transaminase in a complex with an inhibitor, C16H10N2O4F3SCl, and pyridoxal 5' phosphate. [Homo sapiens]
3.36e-87 841 1193 7 355
Chain A, Branched-chain-amino-acid aminotransferase, mitochondrial [Homo sapiens],2HDK_B Chain B, Branched-chain-amino-acid aminotransferase, mitochondrial [Homo sapiens]
6.40e-87 841 1193 7 355
Chain A, Branched-chain-amino-acid aminotransferase, mitochondrial [Homo sapiens],2HG8_B Chain B, Branched-chain-amino-acid aminotransferase, mitochondrial [Homo sapiens],2HGX_A Chain A, Branched-chain-amino-acid aminotransferase, mitochondrial [Homo sapiens],2HGX_B Chain B, Branched-chain-amino-acid aminotransferase, mitochondrial [Homo sapiens]
7.26e-87 834 1193 4 359
X-RAY CRYSTAL STRUCTURE AT 2.20A RESOLUTION OF HUMAN MITOCHONDRIAL BRANCHED CHAIN AMINOTRANSFERASE (BCATM) COMPLEXED WITH A PYRAZOLOPYRIMIDINONE FRAGMENT AND AN INTERNAL ALDIMINE LINKED PLP. [Homo sapiens],5BWR_B X-RAY CRYSTAL STRUCTURE AT 2.20A RESOLUTION OF HUMAN MITOCHONDRIAL BRANCHED CHAIN AMINOTRANSFERASE (BCATM) COMPLEXED WITH A PYRAZOLOPYRIMIDINONE FRAGMENT AND AN INTERNAL ALDIMINE LINKED PLP. [Homo sapiens],5BWT_A X-RAY CRYSTAL STRUCTURE AT 2.20A RESOLUTION OF HUMAN MITOCHONDRIAL BRANCHED CHAIN AMINOTRANSFERASE (BCATM) COMPLEXED WITH A PYRAZOLOPYRIMIDINONE FRAGMENT AND AN INTERNAL ALDIMINE LINKED PLP. [Homo sapiens],5BWT_B X-RAY CRYSTAL STRUCTURE AT 2.20A RESOLUTION OF HUMAN MITOCHONDRIAL BRANCHED CHAIN AMINOTRANSFERASE (BCATM) COMPLEXED WITH A PYRAZOLOPYRIMIDINONE FRAGMENT AND AN INTERNAL ALDIMINE LINKED PLP. [Homo sapiens],5BWU_A X-RAY CRYSTAL STRUCTURE AT 2.17A RESOLUTION OF HUMAN MITOCHONDRIAL BRANCHED CHAIN AMINOTRANSFERASE (BCATM) COMPLEXED WITH A TRIAZOLOPYRIMIDINONE COMPOUND AND AN INTERNAL ALDIMINE LINKED PLP COFACTOR. [Homo sapiens],5BWU_B X-RAY CRYSTAL STRUCTURE AT 2.17A RESOLUTION OF HUMAN MITOCHONDRIAL BRANCHED CHAIN AMINOTRANSFERASE (BCATM) COMPLEXED WITH A TRIAZOLOPYRIMIDINONE COMPOUND AND AN INTERNAL ALDIMINE LINKED PLP COFACTOR. [Homo sapiens],5BWV_A X-RAY CRYSTAL STRUCTURE AT 1.86A RESOLUTION OF HUMAN MITOCHONDRIAL BRANCHED CHAIN AMINOTRANSFERASE (BCATM) COMPLEXED WITH A PYRAZOLOPYRIMIDINONE COMPOUND AND AN INTERNAL ALDIMINE LINKED PLP COFACTOR. [Homo sapiens],5BWV_B X-RAY CRYSTAL STRUCTURE AT 1.86A RESOLUTION OF HUMAN MITOCHONDRIAL BRANCHED CHAIN AMINOTRANSFERASE (BCATM) COMPLEXED WITH A PYRAZOLOPYRIMIDINONE COMPOUND AND AN INTERNAL ALDIMINE LINKED PLP COFACTOR. [Homo sapiens],5BWW_A X-RAY CRYSTAL STRUCTURE AT 1.82A RESOLUTION OF HUMAN MITOCHONDRIAL BRANCHED CHAIN AMINOTRANSFERASE (BCATM) COMPLEXED WITH A PYRROLIDINE AMIDE COMPOUND AND AN INTERNAL ALDIMINE LINKED PLP COFACTOR. [Homo sapiens],5BWW_B X-RAY CRYSTAL STRUCTURE AT 1.82A RESOLUTION OF HUMAN MITOCHONDRIAL BRANCHED CHAIN AMINOTRANSFERASE (BCATM) COMPLEXED WITH A PYRROLIDINE AMIDE COMPOUND AND AN INTERNAL ALDIMINE LINKED PLP COFACTOR. [Homo sapiens],5BWX_A X-RAY CRYSTAL STRUCTURE AT 1.70A RESOLUTION OF HUMAN MITOCHONDRIAL BRANCHED CHAIN AMINOTRANSFERASE (BCATM) COMPLEXED WITH A 4-CHLORO-2-FLUORO SUBSTITUTED PYRAZOLOPYRIMIDINONE COMPOUND AND AN INTERNAL ALDIMINE LINKED PLP COFACTOR. [Homo sapiens],5BWX_B X-RAY CRYSTAL STRUCTURE AT 1.70A RESOLUTION OF HUMAN MITOCHONDRIAL BRANCHED CHAIN AMINOTRANSFERASE (BCATM) COMPLEXED WITH A 4-CHLORO-2-FLUORO SUBSTITUTED PYRAZOLOPYRIMIDINONE COMPOUND AND AN INTERNAL ALDIMINE LINKED PLP COFACTOR. [Homo sapiens],5CR5_A X-ray Crystal Structure At 1.61a Resolution Of Human Mitochondrial Branched Chain Aminotransferase (bcatm) Complexed With A Biphenyl Pyrrolidine Ether Compound And An Internal Aldimine Linked Plp Cofactor. [Homo sapiens],5CR5_B X-ray Crystal Structure At 1.61a Resolution Of Human Mitochondrial Branched Chain Aminotransferase (bcatm) Complexed With A Biphenyl Pyrrolidine Ether Compound And An Internal Aldimine Linked Plp Cofactor. [Homo sapiens],5HNE_A X-ray Crystal Structure Of Human Mitochondrial Branched Chain Aminotransferase (bcatm) Complexed With A 2-aryl Benzimidazole Compound And An Internal Aldimine Linked Plp Cofactor [Homo sapiens],5HNE_B X-ray Crystal Structure Of Human Mitochondrial Branched Chain Aminotransferase (bcatm) Complexed With A 2-aryl Benzimidazole Compound And An Internal Aldimine Linked Plp Cofactor [Homo sapiens],5I5S_A X-ray Crystal Structure At 2.06a Resolution Of Human Mitochondrial Branched Chain Aminotransferase (bcatm) Complexed With A Benzisoxazole Compound And An Internal Aldimine Linked Plp Cofactor. [Homo sapiens],5I5S_B X-ray Crystal Structure At 2.06a Resolution Of Human Mitochondrial Branched Chain Aminotransferase (bcatm) Complexed With A Benzisoxazole Compound And An Internal Aldimine Linked Plp Cofactor. [Homo sapiens],5I5T_A X-ray Crystal Structure At 2.31a Resolution Of Human Mitochondrial Branched Chain Aminotransferase (bcatm) Complexed With A Tetrahydroquinoline Compound And An Internal Aldimine Linked Plp Cofactor. [Homo sapiens],5I5T_B X-ray Crystal Structure At 2.31a Resolution Of Human Mitochondrial Branched Chain Aminotransferase (bcatm) Complexed With A Tetrahydroquinoline Compound And An Internal Aldimine Linked Plp Cofactor. [Homo sapiens],5I5U_A X-ray Crystal Structure At 2.40a Resolution Of Human Mitochondrial Branched Chain Aminotransferase (bcatm) Complexed With A Tetrahydronaphthalenyl Compound And An Internal Aldimine Linked Plp Cofactor. [Homo sapiens],5I5U_B X-ray Crystal Structure At 2.40a Resolution Of Human Mitochondrial Branched Chain Aminotransferase (bcatm) Complexed With A Tetrahydronaphthalenyl Compound And An Internal Aldimine Linked Plp Cofactor. [Homo sapiens],5I5V_A X-ray Crystal Structure At 1.94a Resolution Of Human Mitochondrial Branched Chain Aminotransferase (bcatm) Complexed With A Thienopyrimidine Compound And An Internal Aldimine Linked Plp Cofactor. [Homo sapiens],5I5V_B X-ray Crystal Structure At 1.94a Resolution Of Human Mitochondrial Branched Chain Aminotransferase (bcatm) Complexed With A Thienopyrimidine Compound And An Internal Aldimine Linked Plp Cofactor. [Homo sapiens],5I5W_A X-ray Crystal Structure At 2.40a Resolution Of Human Mitochondrial Branched Chain Aminotransferase (bcatm) Complexed With A Biaryl Amide Compound And An Internal Aldimine Linked Plp Cofactor. [Homo sapiens],5I5W_B X-ray Crystal Structure At 2.40a Resolution Of Human Mitochondrial Branched Chain Aminotransferase (bcatm) Complexed With A Biaryl Amide Compound And An Internal Aldimine Linked Plp Cofactor. [Homo sapiens],5I5X_A X-ray Crystal Structure At 1.65a Resolution Of Human Mitochondrial Branched Chain Aminotransferase (bcatm) Complexed With A Thiazole Compound And Pmp Cofactor. [Homo sapiens],5I5X_B X-ray Crystal Structure At 1.65a Resolution Of Human Mitochondrial Branched Chain Aminotransferase (bcatm) Complexed With A Thiazole Compound And Pmp Cofactor. [Homo sapiens],5I5Y_A X-ray Crystal Structure At 1.81a Resolution Of Human Mitochondrial Branched Chain Aminotransferase (bcatm) Complexed With An Aryl Acetate Compound And An Internal Aldimine Linked Plp Cofactor. [Homo sapiens],5I5Y_B X-ray Crystal Structure At 1.81a Resolution Of Human Mitochondrial Branched Chain Aminotransferase (bcatm) Complexed With An Aryl Acetate Compound And An Internal Aldimine Linked Plp Cofactor. [Homo sapiens],5I60_A X-ray Crystal Structure At 2.12a Resolution Of Human Mitochondrial Branched Chain Aminotransferase (bcatm) Complexed With A Biarl Amide Compound And An Internal Aldimine Linked Plp Cofactor. [Homo sapiens],5I60_B X-ray Crystal Structure At 2.12a Resolution Of Human Mitochondrial Branched Chain Aminotransferase (bcatm) Complexed With A Biarl Amide Compound And An Internal Aldimine Linked Plp Cofactor. [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.85e-183 834 1204 1 372
Branched-chain-amino-acid aminotransferase, cytosolic OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=BAT2 PE=1 SV=1
4.72e-176 820 1205 5 390
Branched-chain-amino-acid aminotransferase, mitochondrial OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=BAT1 PE=1 SV=1
1.40e-134 27 664 26 637
ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=MNL1 PE=1 SV=1
9.85e-123 838 1201 59 422
Branched-chain-amino-acid aminotransferase, mitochondrial OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=eca39 PE=1 SV=3
1.17e-120 839 1205 29 390
Branched-chain-amino-acid aminotransferase OS=Monosiga brevicollis OX=81824 GN=37018 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000824 0.999167 CS pos: 19-20. Pr: 0.9698

TMHMM  Annotations      help

There is no transmembrane helices in QEO24085.1.