Q59928 (ARGD_STRMU) 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:	SMU_666

Organism

Streptococcus mutans [Complete proteome] [HAMAP]

Taxonomic identifier

1309 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length	379 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 – 379	379	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112801
Regions
	Region	205 – 208	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	120	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	123	1	N2-acetyl-L-ornithine By similarity
	Binding site	262	1	N2-acetyl-L-ornithine By similarity
	Binding site	263	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	234	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	148	1	H → N in AAC44504. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q59928 [UniParc]. Last modified November 28, 2002. Version 2. Checksum: 84CA88267A4C770A	FASTA	379	41,142
	10 20 30 40 50 60 MSNLFQNYTR ADLEFIKAEG NYLFDTQGKK YLDFSTGIGV TNLGFHPQVQ VALQKQAEQI 70 80 90 100 110 120 WHTPNLYQNS LQEEVAAKLM AGKDYLAFFC NSGAEANEAA IKIARKATGK QEIITFQNSF 130 140 150 160 170 180 HGRTFGSMSA TGQDKIKVGF GDAVPHFHYA VFNDLNSVKA LVTENTAAVM LELVQGESGV 190 200 210 220 230 240 LPAEQDFVTA LADYCQKNGL LLIIDEVQTG MGRTGKLYAF QHYGIEPDIF TLAKGLANGV 250 260 270 280 290 300 PVGAMLAKKQ FGSAFGPGSH GSTFGGNKLA MAASSAVLDI MTKAGFLEQA WENAHYLQEQ 310 320 330 340 350 360 LTSALQVADT VTQVRGLGYM IGIETTADLG QLVKATRDRG LIVLTAGTNV IRLLPPLTLT 370 KDEIDQGIMI LQEVFEQHN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen." Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J. Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002) [PubMed: 12397186] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700610 / UA159 / Serotype c.
[2]	"Insertional mutagenesis and recovery of interrupted genes of Streptococcus mutans by using transposon Tn917: preliminary characterization of mutants displaying acid sensitivity and nutritional requirements." Gutierrez J.A., Crowley P.J., Brown D.P., Hillman J.D., Youngman P., Bleiweis A.S. J. Bacteriol. 178:4166-4175(1996) [PubMed: 8763945] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: JH1005.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014133 Genomic DNA. Translation: AAN58400.1. U48887 Genomic DNA. Translation: AAC44504.1.
RefSeq	NP_721094.1. NC_004350.2.
3D structure databases
ProteinModelPortal	Q59928.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTRT00000013184; EBSTRP00000012666; EBSTRG00000013184.
GeneID	1028085.
GenomeReviews	Gene locus SMU_666 in contig AE014133_GR.
KEGG	smu:SMU_666.
NMPDR	fig|210007.1.peg.607.
PATRIC	19663517. VBIStrMut61772_0591.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000029271.
HOGENOM	HBG725944.
OMA	QEIITFQ.
ProtClustDB	PRK04260.
Enzyme and pathway databases
BioCyc	SMUT210007:SMU_666-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_STRMU

Accession

Primary (citable) accession number: Q59928

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 28, 2002
Last modified:	January 25, 2012
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program