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Q2LW66 (Q2LW66_SYNAS) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 51. Feed History...

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

Protein namesRecommended name:
Acetylornithine aminotransferase HAMAP-Rule MF_01107
Short name=ACOAT HAMAP-Rule MF_01107
EC=2.6.1.11 HAMAP-Rule MF_01107
Gene names
Name:argD HAMAP-Rule MF_01107
Ordered Locus Names:SYNAS_24470
ORF Names:SYN_01215 EMBL ABC78326.1
OrganismSyntrophus aciditrophicus (strain SB) [Complete proteome] [HAMAP] EMBL ABC78326.1
Taxonomic identifier56780 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Syntrophobacterales › Syntrophaceae › Syntrophus ›

Protein attributes

Sequence length447 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-Rule MF_01107

Cofactor

Binds 1 pyridoxal phosphate per subunit By similarity. HAMAP-Rule MF_01107

Pathway

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

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01107

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01107.

Miscellaneous

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

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. HAMAP-Rule MF_01107

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region263 – 2664Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01107

Sites

Binding site1551Pyridoxal phosphate; via carbonyl oxygen By similarity HAMAP-Rule MF_01107
Binding site1581N2-acetyl-L-ornithine By similarity HAMAP-Rule MF_01107
Binding site3201N2-acetyl-L-ornithine By similarity HAMAP-Rule MF_01107
Binding site3211Pyridoxal phosphate By similarity HAMAP-Rule MF_01107

Amino acid modifications

Modified residue2921N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01107

Sequences

Sequence LengthMass (Da)Tools
Q2LW66 [UniParc].

Last modified February 21, 2006. Version 1.
Checksum: 6C12244006FB7173

FASTA44749,113
        10         20         30         40         50         60 
MIMKENGNSC SGTRMSKEGE TMREDLVTRT QRLLAPSLVI HSDIVVKRGH GVYLESVDGK 

        70         80         90        100        110        120 
RYLDFTSGLA VANVGHSHPK IVEAIKKQAE ELVHAGCMFY YEPLAEYPER LKEVTPPGLD 

       130        140        150        160        170        180 
RFFFSNSGAE AIEGALKLAR YFTGRQGILA FSGAFHGRTY GALSLTASNA KYRNRYAPLL 

       190        200        210        220        230        240 
PSVYHAPYPY CYRCDIGREP ETCSLECFGH VETLLNRLIA PEEIACAVIE PMLGEGGYVV 

       250        260        270        280        290        300 
PPARYLKKLR KLCDREGILL IFDEVQSGMG RTGRWFASEH FGIVPDIMTL AKGIANGMPL 

       310        320        330        340        350        360 
SAVVSSGRIM DGWAPGTHGT TFGGNPVSLC AAAATLRVIE EERLLENAAV VGSKALERLE 

       370        380        390        400        410        420 
SMKDRHPVIG DVRGRGLMIG VEFVREGKEP DRATVEKIMK TCLDRGLLLV ECGGDKNILR 

       430        440 
LIPPLVITRE EMDHGLDILE EAIVKSA

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References

[1]"The genome of the syntrophic bacterium Syntrophus aciditrophicus: Life dependent on negative change in electrical potential."
Gunsalus R., Rohlin L., Kim U., Krupp R., Bhattacharyya A., Campbell J., McInerney M., Moutakki H., Rio-Hernandez L.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SB EMBL ABC78326.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000252 Genomic DNA. Translation: ABC78326.1.
RefSeqYP_462494.1. NC_007759.1.

3D structure databases

ProteinModelPortalQ2LW66.
ModBaseSearch...

Protein-protein interaction databases

STRING56780.SYN_01215.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3883321.
KEGGsat:SYN_01215.
PATRIC23865726. VBISynAci70500_2644.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0160.
HOGENOMHOG000020206.
KOK00823.
OMAPEEIACA.
ProtClustDBPRK08117.

Enzyme and pathway databases

BioCycSACI56780:GHXT-2498-MONOMER.
UniPathwayUPA00068; UER00109.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPMF_01107. ArgD_aminotrans_3.
InterProIPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR004636. Trfase_AcOrn/SuccOrn_fam.
[Graphical view]
PANTHERPTHR11986. PTHR11986. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ2LW66_SYNAS
AccessionPrimary (citable) accession number: Q2LW66
Entry history
Integrated into UniProtKB/TrEMBL: February 21, 2006
Last sequence update: February 21, 2006
Last modified: May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info