P30900 (ARGD_RHOCB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetylornithine aminotransferase
Short name=ACOAT
EC=2.6.1.11

Gene names

Name:	argD
Ordered Locus Names:	RCAP_rcc03135

Organism

Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003) [Complete proteome] [HAMAP]

Taxonomic identifier

272942 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	N2-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 393	393	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112775
Regions
	Region	214 – 217	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	129	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	132	1	N2-acetyl-L-ornithine By similarity
	Binding site	271	1	N2-acetyl-L-ornithine By similarity
	Binding site	272	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	243	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P30900 [UniParc]. Last modified May 31, 2011. Version 2. Checksum: AABAC88D4ED3B0A3	FASTA	393	41,517
	10 20 30 40 50 60 MIASVLPTYT RAPLAFVRGE GSWLWTADGS RYLDLGAGIA VNALGHAAPD LVATLTEQAG 70 80 90 100 110 120 KLWHVSNLYR IPEQERLADM LVAKTFADTV FFTNSGTEAC ELAVKMVRKH FYDKGQPERT 130 140 150 160 170 180 EILTFSGAFH GRSSAAIAAA GTEKMVKGFG PLLPGFVHLP WGDLDAVKAA VTETTAAILI 190 200 210 220 230 240 EPIQGEGGIR PAPEGFLRAL REICDETGTL LVFDEVQCGV ARTGKLFAHE WAGVTPDVMM 250 260 270 280 290 300 VAKGIGGGFP LGAVLATEDA ASGMIAGTHG STYGGNPLGC AIGAKMIEIV TAPGFLDEVS 310 320 330 340 350 360 RKAGFLRQWL EGLVAAHPDI FEEVRGQGLM LGLRLKLPPG DVVKAAYAQN LLTVPAADNV 370 380 390 LRLLPALTIS EDDMAEAVRR LDAAAASLET QPA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of the photosynthetic purple nonsulfur bacterium Rhodobacter capsulatus SB 1003." Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V., Haselkorn R. J. Bacteriol. 192:3545-3546(2010) [PubMed: 20418398] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-309 / NBRC 16581 / SB1003.
[2]	"Bacterial cytochromes c biogenesis." Beckman D.L., Trawick D.R., Kranz R.G. Genes Dev. 6:268-283(1992) [PubMed: 1310666] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71. Strain: ATCC BAA-309 / NBRC 16581 / SB1003.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001312 Genomic DNA. Translation: ADE86859.1. X63461 Genomic DNA. No translation available.
PIR	S29255.
RefSeq	YP_003579266.1. NC_014034.1.
3D structure databases
ProteinModelPortal	P30900.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	9005951.
GenomeReviews	Gene locus RCAP_rcc03135 in contig CP001312_GR.
KEGG	rcp:RCAP_rcc03135.
PATRIC	35506474. VBIRhoCap134200_3172.
Organism-specific databases
CMR	Search...
Family and domain databases
HAMAP	MF_01107. ArgD_aminotrans_3. [Tree]
InterPro	IPR004636. 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]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
KO	K00821.
PANTHER	PTHR11986. Aminotrans_3. 1 hit. PTHR11986:SF19. ArgD_aminotrans. 1 hit.
Pfam	PF00202. Aminotran_3. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR00707. ArgD. 1 hit.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGD_RHOCB

Accession

Primary (citable) accession number: P30900
Secondary accession number(s): D5AR54

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	May 31, 2011
Last modified:	January 25, 2012
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program