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 01-MAY-2013, entry version 91.
DE RecName: Full=Acetylornithine aminotransferase;
DE Short=ACOAT;
DE EC=2.6.1.11;
GN Name=argD; OrderedLocusNames=NMA1584;
OS Neisseria meningitidis serogroup A / serotype 4A (strain Z2491).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Neisseriaceae; Neisseria.
OX NCBI_TaxID=122587;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z2491;
RX 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 (By similarity).
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; NC_003116.1.
DR ProteinModelPortal; Q9JTX9; -.
DR SMR; Q9JTX9; 2-393.
DR STRING; 122587.NMA1584; -.
DR EnsemblBacteria; CAM08728; CAM08728; NMA1584.
DR GeneID; 907972; -.
DR KEGG; nma:NMA1584; -.
DR PATRIC; 20364272; VBINeiMen132687_1840.
DR eggNOG; COG4992; -.
DR HOGENOM; HOG000020206; -.
DR KO; K00821; -.
DR OMA; LDDVFCE; -.
DR ProtClustDB; PRK05093; -.
DR BioCyc; NMEN122587:GI3Q-1400-MONOMER; -.
DR UniPathway; UPA00068; UER00109.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IEA:HAMAP.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 2.
DR HAMAP; MF_01107; ArgD_aminotrans_3; 1; -.
DR InterPro; IPR017652; Ac/SucOrn_transaminase_bac.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR InterPro; IPR004636; Trfase_AcOrn/SuccOrn_fam.
DR PANTHER; PTHR11986; PTHR11986; 1.
DR PANTHER; PTHR11986:SF19; PTHR11986:SF19; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 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 N2-acetyl-L-ornithine (By similarity).
FT BINDING 271 271 N2-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
//
