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I0I3V7 (I0I3V7_CALAS) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 14. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

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:gabT EMBL BAL99944.1
Synonyms:argD HAMAP-Rule MF_01107
Ordered Locus Names:CLDAP_19050 EMBL BAL99944.1
OrganismCaldilinea aerophila (strain DSM 14535 / JCM 11387 / NBRC 104270 / STL-6-O1) [Complete proteome] [HAMAP] EMBL BAL99944.1
Taxonomic identifier926550 [NCBI]
Taxonomic lineageBacteriaChloroflexiCaldilineaeCaldilinealesCaldilineaceaeCaldilinea

Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

Region126 – 1272Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01107
Region263 – 2664Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01107

Sites

Binding site1531Pyridoxal phosphate; via carbonyl oxygen By similarity HAMAP-Rule MF_01107
Binding site1561N2-acetyl-L-ornithine By similarity HAMAP-Rule MF_01107
Binding site3201Pyridoxal 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
I0I3V7 [UniParc].

Last modified June 13, 2012. Version 1.
Checksum: 9F9049CDA32C8B7F

FASTA45049,486
        10         20         30         40         50         60 
MLATHLTRTI PRLNTPGPKA RAILERDRAV VSRAYGRVAD FVMSHGLGSQ VWDVDGNRYL 

        70         80         90        100        110        120 
DFMSGIAVNA TGHSHPRVVR AIQEQAEKFL HISSDYYHES WVRLSERLNE IAPFAEPSSV 

       130        140        150        160        170        180 
FLGNSGTEAV EGAIKLARYH TGRPYFLGFI GGFHGRTLGS LGFTASKITQ RRGFLPQREV 

       190        200        210        220        230        240 
IHVPYPYEYR PLLAMQPGEA DYGETVVNYI ERVVFKNLVA PDEVAAVVVE PIQGEGGYVV 

       250        260        270        280        290        300 
PPASFFPRLR ELCDRHGILL IVDEVQSGMG RTGKWWAIEH WGVEPDIVCT AKGIASGVPL 

       310        320        330        340        350        360 
GGFIARQRIA TWPTGAHGNT YGGNPLAMVA ALATMEVLEN GGIQNAAEQG AYMLSRLNEM 

       370        380        390        400        410        420 
AARHPSIGDV RGKGLMIGVE FVQDKATRMP NARLRDRIVE LAFEHGLLIM GCGVSTMRII 

       430        440        450 
PPLIITRPEV DEGLEIFEYA VTLAEEELMG 

« Hide

References

[1]"Complete genome sequence of Caldilinea aerophila DSM 14535 (= NBRC 102666)."
Oguchi A., Hosoyama A., Sekine M., Fukai R., Kato Y., Nakamura S., Hanada S., Yamazaki S., Fujita N.
Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 14535 / JCM 11387 / NBRC 104270 / STL-6-O1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP012337 Genomic DNA. Translation: BAL99944.1.
RefSeqYP_005441842.1. NC_017079.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAL99944; BAL99944; CLDAP_19050.
GeneID12033791.
KEGGcap:CLDAP_19050.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00823.

Enzyme and pathway databases

BioCycCAER926550:GLA5-1942-MONOMER.
UniPathwayUPA00068; UER00109.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
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]
PIRSFPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameI0I3V7_CALAS
AccessionPrimary (citable) accession number: I0I3V7
Entry history
Integrated into UniProtKB/TrEMBL: June 13, 2012
Last sequence update: June 13, 2012
Last modified: July 9, 2014
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)