Q97GH9 (ARGD_CLOAB) 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:	CA_C2388

Organism

Clostridium acetobutylicum

Taxonomic identifier

1488 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	387 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 – 387	387	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112739
Regions
	Region	97 – 98	2	Pyridoxal phosphate binding By similarity
	Region	215 – 218	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	130	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	133	1	N2-acetyl-L-ornithine By similarity
	Binding site	273	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	244	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q97GH9 [UniParc]. Last modified October 1, 2001. Version 1. Checksum: 51DE3C9ACE13AC3E	FASTA	387	42,714
	10 20 30 40 50 60 MSKSYLMNTY GRFNVTFDKG EGTKLYDKDG NEYIDFVSGV AVNCLGHCNP SIVKAIEEQS 70 80 90 100 110 120 SKLMHVSNYY WNENAMELTE ILCKNSEFDK VFMCNSGTEA IEAGLKLARK YALLHGDENK 130 140 150 160 170 180 KEIIYMDNSF HGRTMGALSV TGQPKYQESF KPLIGAVKSV KFNDLDDIKQ KISSKTAAVI 190 200 210 220 230 240 VEPIQGEGGI IPAKKEYLKL LRDLCDENNA LLIFDEVQCG MGRVGSLFAY QKFEVVPDIV 250 260 270 280 290 300 CIAKALGGGF PIGAMLAKES VASSFVPGDH GNTYGGNPLA CAVAIAVLKE LVDKKVVEIN 310 320 330 340 350 360 VNEKSKYLFD KLMTLKEKYK VINDVRGMGL LIGVEVACDV KKIINKCFES KLLLITAGKN 370 380 VVRFLPPLNV SFEEIDKALG IFEESIK

References

[1]

"Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum." Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., Smith D.R. J. Bacteriol. 183:4823-4838(2001) [PubMed: 11466286] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE001437 Genomic DNA. Translation: AAK80343.1.
PIR	D97194.
RefSeq	NP_349003.1. NC_003030.1.
3D structure databases
ProteinModelPortal	Q97GH9.
SMR	Q97GH9. Positions 5-387.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1118571.
GenomeReviews	Gene locus CA_C2388 in contig AE001437_GR.
KEGG	cac:CA_C2388.
NMPDR	fig|272562.1.peg.2532.
PATRIC	32039155. VBICloAce74127_2585.
Phylogenomic databases
HOGENOM	HBG725944.
OMA	TTYARPN.
PhylomeDB	Q97GH9.
ProtClustDB	PRK02627.
Enzyme and pathway databases
BioCyc	CACE272562:CAC2388-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	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_CLOAB

Accession

Primary (citable) accession number: Q97GH9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	October 1, 2001
Last modified:	January 25, 2012
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program