Reviewed, UniProtKB/Swiss-Prot Q72RH8 (ARGD_LEPIC)

Names and origin

Protein names

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

Gene names

Name:	argD
Ordered Locus Names:	LIC_11767

Organism

Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni [Complete proteome] [HAMAP]

Taxonomic identifier

44275 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Leptospiraceae › Leptospira

Protein attributes

Sequence length	406 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
Subcellular location	Cytoplasm Probable.
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: HAMAP
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: HAMAP 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 – 406	406	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112750
Regions
	Region	113 – 114	2	Pyridoxal phosphate binding By similarity
	Region	233 – 236	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	145	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	148	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	290	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	291	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	262	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q72RH8-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 5AB51966B5062614	FASTA	406	44,866
	10 20 30 40 50 60 MNDADIHKEL FQHTKELADH YLLNTYARYD VAFRYGVNEL LFDFDNKQYI DFHCGVAVTN 70 80 90 100 110 120 LGHADPDIIE VVRSQADKLF HTSNLFYSEE ASKLAELLIL NSFPGKVFLT NSGTEAIEGA 130 140 150 160 170 180 FKLARKYAYS KSIVDPIILS LEKSFHGRSV SGMSLTGQDK IRKGYGELLK GIEFIEPNND 190 200 210 220 230 240 EALVAAFERY QGRIVALIEE PILGESGIIP LSRNFLTLSR ELTEENEALL IFDEIQTGMG 250 260 270 280 290 300 RTGTLFAFET MGFSPDAMTL AKGLGSGFPI GALIVGEKYQ DLFTQGSHGS TFGGNHLAAA 310 320 330 340 350 360 VAYETIRIIQ TREILNNVNI CSDIAFTRLR EMQEKYPVIS EVRGKGLHIG LELKVPSKPI 370 380 390 400 AEACLSAGLV VNATADNVVR IMPPLTISTD FLNQGLDILE SVLKQN

References

[1]

"Comparative genomics of two Leptospira interrogans serovars reveals novel insights into physiology and pathogenesis." Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B., Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V., Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L., Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S. , Ferro M.I.T., Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H., Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M., Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L., Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A., Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A., Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A. J. Bacteriol. 186:2164-2172(2004) [PubMed: 15028702] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Fiocruz L1-130.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016823 Genomic DNA. Translation: AAS70356.1.
RefSeq	YP_001719.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2771509.
GenomeReviews	Gene locus LIC_11767 in contig AE016823_GR.
KEGG	lic:LIC11767.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q72RH8.
OMA	EHIDEMS.
Enzyme and pathway databases
BioCyc	LINT267671:LIC_11767-MON.
Family and domain databases
HAMAP	MF_01107. [Tree]
InterPro	IPR004636. AcOrn/succinylOrn_aminoTrfase. IPR005814. Aminotrans_3. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHER	PTHR11986. Aminotrans_3. 1 hit. PTHR11986:SF19. ArgD_aminotrans. 1 hit.
Pfam	PF00202. Aminotran_3. 1 hit. [Graphical view]
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGD_LEPIC

Accession

Primary (citable) accession number: Q72RH8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	July 5, 2004
Last modified:	November 3, 2009
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)