ID   ARGD_NEIMA              Reviewed;         397 AA.
AC   Q9JTX9; A1ISH2;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   16-JUN-2009, entry version 58.
DE   RecName: Full=Acetylornithine aminotransferase;
DE            Short=ACOAT;
DE            EC=2.6.1.11;
GN   Name=argD; OrderedLocusNames=NMA1584;
OS   Neisseria meningitidis serogroup A.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=65699;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z2491 / Serogroup A / Serotype 4A;
RX   MEDLINE=20222556; PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T.,
RA   Davies R.M., Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S.,
RA   Jagels K., Leather S., Moule S., Mungall K.L., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA   Whitehead S., Spratt B.G., Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria
RT   meningitidis Z2491.";
RL   Nature 404:502-506(2000).
CC   -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-
CC       acetyl-L-glutamate 5-semialdehyde + L-glutamate.
CC   -!- COFACTOR: Binds 1 pyridoxal phosphate per subunit (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-L-ornithine from L-glutamate: step 4/4.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- MISCELLANEOUS: May also have succinyldiaminopimelate
CC       aminotransferase activity, thus carrying out the corresponding
CC       step in lysine biosynthesis.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. ArgD subfamily.
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DR   EMBL; AL157959; CAM08728.1; -; Genomic_DNA.
DR   PIR; C81851; C81851.
DR   RefSeq; YP_002342900.1; -.
DR   HSSP; P12995; 1QJ3.
DR   GeneID; 907972; -.
DR   GenomeReviews; AL157959_GR; NMA1584.
DR   KEGG; nma:NMA1584; -.
DR   HOGENOM; Q9JTX9; -.
DR   OMA; Q9JTX9; NAISARY.
DR   BioCyc; NMEN122587:NMA1584-MON; -.
DR   BRENDA; 2.6.1.11; 292829.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-amin...; IEA:HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01107; -; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR004636; ArgD_aminotrans.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR017652; SuccinylOrn_transaminase.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   PANTHER; PTHR11986; Aminotrans_3; 1.
DR   PANTHER; PTHR11986:SF19; ArgD_aminotrans; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   TIGRFAMs; TIGR03246; arg_catab_astC; 1.
DR   TIGRFAMs; TIGR00707; argD; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Arginine biosynthesis;
KW   Complete proteome; Cytoplasm; Pyridoxal phosphate; Transferase.
FT   CHAIN         1    397       Acetylornithine aminotransferase.
FT                                /FTId=PRO_0000112759.
FT   REGION      214    217       Pyridoxal phosphate binding (By
FT                                similarity).
FT   BINDING     129    129       Pyridoxal phosphate; via carbonyl oxygen
FT                                (By similarity).
FT   BINDING     132    132       N(2)-acetyl-L-ornithine (By similarity).
FT   BINDING     271    271       N(2)-acetyl-L-ornithine (By similarity).
FT   BINDING     272    272       Pyridoxal phosphate (By similarity).
FT   MOD_RES     243    243       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   397 AA;  42547 MW;  BE4DB264C16144D8 CRC64;
     MQNYLTPNFA FAPMIPERAS GSRVWDTEGR EYIDFSGGIA VNALGHCHPA LVDALNAQMH
     KLWHISNIYT TRPAQELAQK LVANSFADKV FFCNSGSEAN EAALKLARKY ARDRFGGGKS
     EIVACINSFH GRTLFTVSVG GQPKYSKDYA PLPQGITHVP FNDIAALEAA VGEQTCAVII
     EPIQGESGIL PATAEYLQTA RRLCDRHNAL LILDEVQTGM GHTGRLFAYE HYGVVPDILS
     SAKALGCGFP IGAMLATETI AAAFQPGTHG STFGGNPMAC AVGSRAFDII NAPETLHNVR
     SQGQKLQTAL LDLGRKTGLF SQVRGMGLLL GCVLDAPYRG RASEITAAAL KHGVMILVAG
     ADVLRFAPSL LLNDEDTAEG LRRLEHVLTE FAAANRP
//