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Q6FXA4 (ARGD_CANGA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acetylornithine aminotransferase, mitochondrial
Short name=ACOAT
EC=2.6.1.11
Gene names
Name:ARG8
Ordered Locus Names:CAGL0B01507g
OrganismCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]
Taxonomic identifier284593 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate.

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processarginine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionN2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity

Inferred from electronic annotation. Source: EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 427Acetylornithine aminotransferase, mitochondrialPRO_0000002077

Amino acid modifications

Modified residue2791N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6FXA4 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: BF964B26B2221362

FASTA42746,824
        10         20         30         40         50         60 
MYKRYFSTSL KTNQQALKKI LEEKTYQVTT YARPSDLCIT RGLNAKLFDD FNNKEYIDFT 

        70         80         90        100        110        120 
AGIAVTALGH ANPKVAEILQ TQATKLVHSS NLYFTKECLD LSEKLIEKTK KFGGQHDASK 

       130        140        150        160        170        180 
VFLCNSGTEA NEAALKFAKK HGITKNPKKQ GIIAFENSFH GRTMGALSVT WNKKYRTPFG 

       190        200        210        220        230        240 
DLVPHVSFLN INDELSKIKD FINTKKDEIA GLIIEPIQGE GGIFPIPIEK LVALKEICQK 

       250        260        270        280        290        300 
NDIIVIYDEI QCGLGRTGNL WAHAALPKAA HPDIFTSAKA LGNGFPIAAT VVNEKVNNAL 

       310        320        330        340        350        360 
QVGDHGTTYG GNPLGCAVSN YVLDVIGDQA FLDSVTKKGE LLKKGLLKIK EQHPDKISDV 

       370        380        390        400        410        420 
RGSGLIWGVE FKDAPGAIVQ KARELGLLVI TAGKTTVRFV PSLTIEDEVV EEGLTIFNKA 


VNDVFSK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR380948 Genomic DNA. Translation: CAG57935.1.
RefSeqXP_445035.1. XM_445035.1.

3D structure databases

ProteinModelPortalQ6FXA4.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2886668.
GenomeReviewsGene locus CAGL0B01507g in contig CR380948_GR.
KEGGcgr:CAGL0B01507g.

Phylogenomic databases

eggNOGfuNOG06187.
HOGENOMHBG725944.
OMAGTYNDIA.
OrthoDBEOG4HMNJM.

Family and domain databases

InterProIPR004636. AcOrn/SuccinylOrn_aminoTrfase.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
KOK00818.
PANTHERPTHR11986. Aminotrans_3. 1 hit.
PTHR11986:SF19. ArgD_aminotrans. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR00707. ArgD. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARGD_CANGA
AccessionPrimary (citable) accession number: Q6FXA4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: July 19, 2004
Last modified: December 14, 2011
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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