P59316 (ARGD_CHLTE) 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:	CT0367

Organism

Chlorobium tepidum

Taxonomic identifier

1097 [NCBI]

Taxonomic lineage

Bacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobaculum

Protein attributes

Sequence length	400 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 Reference 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 – 400	400	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112738
Regions
	Region	106 – 107	2	Pyridoxal phosphate binding By similarity
	Region	224 – 227	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	139	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	142	1	N2-acetyl-L-ornithine By similarity
	Binding site	281	1	N2-acetyl-L-ornithine By similarity
	Binding site	282	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	253	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P59316 [UniParc]. Last modified February 12, 2003. Version 1. Checksum: 210092F514307CBF	FASTA	400	43,548
	10 20 30 40 50 60 MNTPAINLET EKQLFFHNYA RLPLDIASGK GSFLYTASGE RYLDMIAGVG VNAIGYGDKR 70 80 90 100 110 120 LEQAITEQAS KYIHVSNLFM QKPQFDLAAK LLEISRMSKV FFCNSGTEAI EAAIKLARRF 130 140 150 160 170 180 AARNGDTDKT QVLSLTNCFH GRTYGALSLT AKPKYVDGFE PLVPETGMID FNDVEDLERK 190 200 210 220 230 240 VSNRTAAVFV EFVQGEGGIH KVSEAFIAKL KELAKEHDFL IVADEIQAGC GRTGAFFSYM 250 260 270 280 290 300 PFDIQPDLVC VAKPLGGGLP LGAIIGSEKV AEVFTPGSHG TTFGGNPVAC AAGLAMIEAI 310 320 330 340 350 360 LADGLMQNAL EVGSMMRTAF EKMAEKHAQI LEIRQYGLMI GVTVHREAKY YVEEALKRGV 370 380 390 400 LVNATSNNVI RLLPPLSISK EEAQLCLDTL DAIFTEEAKA

References

[1]

"The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium." Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M. , Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002) [PubMed: 12093901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49652 / DSM 12025 / TLS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE006470 Genomic DNA. Translation: AAM71613.1.
RefSeq	NP_661271.1. NC_002932.3.
3D structure databases
ProteinModelPortal	P59316.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1008029.
GenomeReviews	Gene locus CT0367 in contig AE006470_GR.
KEGG	cte:CT0367.
NMPDR	fig|194439.1.peg.365.
PATRIC	21398843. VBIChlTep116050_0353.
TIGR	CT0367.
Phylogenomic databases
HOGENOM	HBG725944.
OMA	EFVQGEG.
ProtClustDB	PRK02627.
Enzyme and pathway databases
BioCyc	CTEP194439:CT_0367-MONOMER.
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	K00818.
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_CHLTE

Accession

Primary (citable) accession number: P59316

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	February 12, 2003
Last modified:	January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program