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Q8TUE8 (ARGD_METAC) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 72. 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
Short name=ACOAT
EC=2.6.1.11
Gene names
Name:argD
Ordered Locus Names:MA_0119
OrganismMethanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Taxonomic identifier188937 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

Protein attributes

Sequence length395 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate. HAMAP MF_01107

Cofactor

Binds 1 pyridoxal phosphate per subunit By similarity. HAMAP MF_01107

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4. HAMAP MF_01107

Subunit structure

Homodimer By similarity. HAMAP MF_01107

Subcellular location

Cytoplasm Probable HAMAP MF_01107.

Miscellaneous

May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the corresponding step in lysine biosynthesis. HAMAP MF_01107

Sequence similarities

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

Sequence caution

The sequence AAM03573.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

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

Chain1 – 395395Acetylornithine aminotransferase HAMAP MF_01107
PRO_0000112820

Regions

Region230 – 2334Pyridoxal phosphate binding By similarity

Sites

Binding site1441Pyridoxal phosphate; via carbonyl oxygen By similarity
Binding site1471N2-acetyl-L-ornithine By similarity
Binding site2851N2-acetyl-L-ornithine By similarity
Binding site2861Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2591N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8TUE8 [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: AC5724ABD9B46897

FASTA39542,692
        10         20         30         40         50         60 
MTENIIESGD PQARYDSVIE KDSKYVMQTY GRQPLVLSKG KGAVVQDIYG KEYIDCVAGI 

        70         80         90        100        110        120 
AVNNVGHCHP TVVKAIQAQA ENLIHVSNLY YTEIQAEFAE TLASITGMER VFFCNSGAES 

       130        140        150        160        170        180 
VEAAMKLARV ATGKSAFVAA EHSFHGRTIG ALSVTHKSMY RDPFMPPVSS ETTFVPYSDA 

       190        200        210        220        230        240 
EAIRQAISEN TAAVILEPIQ GEGGINIPDP GYLKEVREIC DETGALLIFD EVQTGFGRTG 

       250        260        270        280        290        300 
TWFCKEQFGV EPDIMSMSKA IGGGFPMGAI AAHNGINFGR GQHASTFGGG PLACAAALAS 

       310        320        330        340        350        360 
VKVIREEKLL ERSKEMGAYF MKKLAGMVRD DVVEVRGKGL MIGVEIKYPC GKFVDFAREQ 

       370        380        390 
GVLVNCTSDS VLRLVPPLVI TKEQIDTVVD VLEQA

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE010299 Genomic DNA. Translation: AAM03573.1. Different initiation.
RefSeqNP_615093.1. NC_003552.1.

3D structure databases

ProteinModelPortalQ8TUE8.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1472011.
GenomeReviewsGene locus MA_0119 in contig AE010299_GR.
KEGGmac:MA0119.
NMPDRfig|188937.1.peg.119.

Phylogenomic databases

HOGENOMHBG725944.
OMAVEKDSKY.
ProtClustDBPRK02627.

Enzyme and pathway databases

BioCycMACE188937:MA0119-MONOMER.

Family and domain databases

HAMAPMF_01107. ArgD_aminotrans_3.
[Tree]
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.
KOK00821.
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_METAC
AccessionPrimary (citable) accession number: Q8TUE8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: May 5, 2009
Last modified: November 16, 2011
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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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