Q9JYY4 (ARGD_NEIMB) 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:	NMB1371

Organism

Neisseria meningitidis serogroup B

Taxonomic identifier

491 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length	398 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 – 398	398	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112760
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)
	Q9JYY4 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 41C4592BFD1DA04D	FASTA	398	42,815
	10 20 30 40 50 60 MQNYLTPNFA FAPMIPERAS GSRVWDTKGR EYIDFSGGIA VNALGHCHPA LVDALNAQMH 70 80 90 100 110 120 KLWHISNIYT TRPAQELAQK LVANSFADKV FFCNSGSEAN EAALKLARKY ARDRFGGGKS 130 140 150 160 170 180 EIVACINSFH GRTLFTVSVG GQPKYSKDYA PLPQGITHVP FNDIAALEAA VGEQTCAVII 190 200 210 220 230 240 EPIQGESGIL PATAEYLQTA RRLCDRHNAL LILDEVQTGM GHTGRLFAYE HYGIVPDILS 250 260 270 280 290 300 SAKALGCGFP IGAMLATEKI AAAFQPGTHG STFGGNPMAC AVGSRAFDII NTPETLNHVR 310 320 330 340 350 360 EQGQKLQTAL LDLCRKTGLF SQVRGMGLLL GCVLDEAYRG RASEITAAAL KHGVMILVAG 370 380 390 ADVLRFAPSL LLNDEDMAEG LRRLEHALTE FAATSDNP

References

[1]

"Complete genome sequence of Neisseria meningitidis serogroup B strain MC58." Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L., White O. , Fleischmann R.D., Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C. Science 287:1809-1815(2000) [PubMed: 10710307] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MC58 / Serogroup B.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE002098 Genomic DNA. Translation: AAF41745.1.
PIR	H81090.
RefSeq	NP_274389.1. NC_003112.2.
3D structure databases
ProteinModelPortal	Q9JYY4.
SMR	Q9JYY4. Positions 2-393.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBNEIT00000009216; EBNEIP00000008836; EBNEIG00000009216.
GeneID	903793.
GenomeReviews	Gene locus NMB1371 in contig AE002098_GR.
KEGG	nme:NMB1371.
NMPDR	fig|122586.1.peg.1323.
PATRIC	20358413. VBINeiMen85645_1718.
TIGR	NMB1371.
Phylogenomic databases
GeneTree	EBGT00050000020132.
HOGENOM	HBG725944.
OMA	TTYARPN.
ProtClustDB	PRK05093.
Enzyme and pathway databases
BioCyc	NMEN122586:NMB_1371-MONOMER.
Family and domain databases
HAMAP	MF_01107. ArgD_aminotrans_3. [Tree]
InterPro	IPR017652. Ac/SuccinylOrn_transaminase. 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	TIGR03246. Arg_catab_astC. 1 hit. TIGR00707. ArgD. 1 hit.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGD_NEIMB

Accession

Primary (citable) accession number: Q9JYY4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program