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Q1QAW9 (Q1QAW9_PSYCK) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 60. 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:Pcryo_1405
OrganismPsychrobacter cryohalolentis (strain K5) [Complete proteome] [HAMAP] EMBL ABE75184.1
Taxonomic identifier335284 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Psychrobacter ›

Protein attributes

Sequence length393 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

Region218 – 2214Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01107

Sites

Binding site1291Pyridoxal phosphate; via carbonyl oxygen By similarity HAMAP-Rule MF_01107
Binding site1321N2-acetyl-L-ornithine By similarity HAMAP-Rule MF_01107
Binding site2751N2-acetyl-L-ornithine By similarity HAMAP-Rule MF_01107
Binding site2761Pyridoxal phosphate By similarity HAMAP-Rule MF_01107

Amino acid modifications

Modified residue2471N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01107

Sequences

Sequence LengthMass (Da)Tools
Q1QAW9 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 6E2E0E28579150BB

FASTA39342,671
        10         20         30         40         50         60 
MSATYLMPTY LRQPISFTRG SGSWLYTQDE TPYLDALTGI AVCGLGHCHP QVTEAIQQQA 

        70         80         90        100        110        120 
ATLVHTSNLF GIDWQERAGE ALCNAAQMDS VFFANSGAEA NEAALKLARL YAHQQGFKRP 

       130        140        150        160        170        180 
KVIVMEQSFH GRTLLSLSAT ANPKAREGFY TLDNDFIRVP FGDIAAIKQA AHDYEDICAV 

       190        200        210        220        230        240 
FVEPIQGEGG LNTAANGFTY LEQIQAVCDT HNWLFMLDEV QTGNGRTGKY FAYQHSSARP 

       250        260        270        280        290        300 
DVLTTAKGLG NGFPVGACMV RGRANGLFGA GSHGSTYGGT PLASRVVHSV YDVLANSDIM 

       310        320        330        340        350        360 
QNAVNEGQFI RDSMVDAFGQ YGVSSRGAGM MIGIALPEDM DCSKLVDRAR DEQKLIINVT 

       370        380        390 
GGHVIRLLPP LNMSRNESSQ VVERLVNLLK PSF

« Hide

References

[1]"Complete sequence of chromosome of Psychrobacter cryohalolentis K5."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000323 Genomic DNA. Translation: ABE75184.1.
RefSeqYP_580668.1. NC_007969.1.

3D structure databases

ProteinModelPortalQ1QAW9.
ModBaseSearch...

Protein-protein interaction databases

STRING335284.Pcryo_1405.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE75184; ABE75184; Pcryo_1405.
GeneID4035800.
KEGGpcr:Pcryo_1405.
PATRIC23062349. VBIPsyCry128170_1499.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4992.
HOGENOMHOG000020206.
KOK00818.
OMAPKVIVME.
ProtClustDBPRK02627.

Enzyme and pathway databases

BioCycPCRY335284:GHE9-1468-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.
PTHR11986:SF19. PTHR11986:SF19. 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 nameQ1QAW9_PSYCK
AccessionPrimary (citable) accession number: Q1QAW9
Entry history
Integrated into UniProtKB/TrEMBL: May 16, 2006
Last sequence update: May 16, 2006
Last modified: May 1, 2013
This is version 60 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