Q6FK92 (Q6FK92_CANGA) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Branched-chain-amino-acid aminotransferase RuleBase RU004517
EC=2.6.1.42 RuleBase RU004517

Gene names

Ordered Locus Names:

CAGL0M00176g

Organism

Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

284593 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces › Candida glabrata

Protein attributes

Sequence length	371 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	L-isoleucine + 2-oxoglutarate = (S)-3-methyl-2-oxopentanoate + L-glutamate. RuleBase RU004517 L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate. L-valine + 2-oxoglutarate = 3-methyl-2-oxobutanoate + L-glutamate. RuleBase RU004517
Cofactor	Pyridoxal phosphate By similarity. RuleBase RU004516
Sequence similarities	Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. RuleBase RU004106

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis RuleBase RU004518
Ligand	Pyridoxal phosphate RuleBase RU004516
Molecular function	Aminotransferase RuleBase RU004517 Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	branched-chain amino acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	L-isoleucine transaminase activity Inferred from electronic annotation. Source: EC L-leucine transaminase activity Inferred from electronic annotation. Source: EC L-valine transaminase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Amino acid modifications
	Modified residue	197	1	N6-(pyridoxal phosphate)lysine By similarity PIRSR PIRSR006468-1

Sequences

	Sequence		Length	Mass (Da)
	Q6FK92 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 31440A536670222C	FASTA	371	41,577
	10 20 30 40 50 60 MDASRLKITK VSTPSERKPN DQLVFGKTFT DHMLTIEWTS ENGWDAPEIK PYGKLCLDPS 70 80 90 100 110 120 SIVFHYAFEL FEGMKAYRTK DGKIAMFRPE KNMERMNKSA ARICLPTFDG EELIKLIGKL 130 140 150 160 170 180 IELDKHLIPE GEGYSLYIRP TLIGTSEGLG VKEPDRALLF VICSPVGPYY KTGFKAVRLD 190 200 210 220 230 240 ATDYATRAWP GGVGDKKLGA NYAPCVLPQT QAAAKGFQQN LWLFGPEHYV TEVGTMNAFF 250 260 270 280 290 300 AFNCKETGKK ELVTAPLDGT ILEGVTRDSI LTLARKYLDP NEWEINERYF TIHEVQEKAH 310 320 330 340 350 360 KGELLEAFGS GTAAIVSPIK EIGWKDTIIN VPLIPGEQSG PLTKQIASWM MDIQYGKVEL 370 DNWLRIVADI N

References

[1]

"Genome evolution in yeasts." Genolevures Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR380959 Genomic DNA. Translation: CAG62328.1.
RefSeq	XP_449352.1. XM_449352.1.
3D structure databases
ProteinModelPortal	Q6FK92.
ModBase	Search...
Proteomic databases
PRIDE	Q6FK92.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2891150.
KEGG	cgr:CAGL0M00176g.
Phylogenomic databases
HOGENOM	HOG000276704.
KO	K00826.
OMA	SPIGGVQ.
OrthoDB	EOG4N07PZ.
Family and domain databases
InterPro	IPR001544. Aminotrans_IV. IPR018300. Aminotrans_IV_CS. IPR005786. B_amino_transII. [Graphical view]
PANTHER	PTHR11825. PTHR11825. 1 hit. PTHR11825:SF2. PTHR11825:SF2. 1 hit.
Pfam	PF01063. Aminotran_4. 1 hit. [Graphical view]
PIRSF	PIRSF006468. BCAT1. 1 hit.
SUPFAM	SSF56752. Aminotrans_IV. 1 hit.
TIGRFAMs	TIGR01123. ilvE_II. 1 hit.
PROSITE	PS00770. AA_TRANSFER_CLASS_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q6FK92_CANGA

Accession

Primary (citable) accession number: Q6FK92

Entry history

Integrated into UniProtKB/TrEMBL:	July 19, 2004
Last sequence update:	July 19, 2004
Last modified:	May 1, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)