ID   ARGD_ANASP              Reviewed;         427 AA.
AC   P54752;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 65.
DE   RecName: Full=Acetylornithine aminotransferase;
DE            Short=ACOAT;
DE            EC=2.6.1.11;
GN   Name=argD; OrderedLocusNames=alr1080;
OS   Anabaena sp. (strain PCC 7120).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=95014086; PubMed=7929012;
RA   Floriano B., Herrero A., Flores E.;
RT   "Analysis of expression of the argC and argD genes in the
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   J. Bacteriol. 176:6397-6401(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=21595285; PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T.,
RA   Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M.,
RA   Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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; X78854; CAA55410.1; -; Genomic_DNA.
DR   EMBL; BA000019; BAB73037.1; -; Genomic_DNA.
DR   PIR; AE1941; AE1941.
DR   RefSeq; NP_485123.1; -.
DR   HSSP; P12995; 1QJ3.
DR   GeneID; 1104674; -.
DR   GenomeReviews; BA000019_GR; alr1080.
DR   KEGG; ana:alr1080; -.
DR   NMPDR; fig|103690.1.peg.1390; -.
DR   HOGENOM; P54752; -.
DR   OMA; P54752; EHNALLV.
DR   BioCyc; NSP103690:ALR1080-MON; -.
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   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; 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    427       Acetylornithine aminotransferase.
FT                                /FTId=PRO_0000112714.
FT   REGION      248    251       Pyridoxal phosphate binding (By
FT                                similarity).
FT   BINDING     157    157       Pyridoxal phosphate; via carbonyl oxygen
FT                                (By similarity).
FT   BINDING     160    160       N(2)-acetyl-L-ornithine (By similarity).
FT   BINDING     304    304       N(2)-acetyl-L-ornithine (By similarity).
FT   BINDING     305    305       Pyridoxal phosphate (By similarity).
FT   MOD_RES     277    277       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   427 AA;  46140 MW;  6AF594BB4B3B134E CRC64;
     MSLQTLIEQA TNPPESGSAA SSPFSTDSFD ASVMSTYGRF PLALERGAGC RVWDTQGKEY
     LDFVAGIATC TLGHAHPAMV EAVTRQIQKL HHVSNLYYIP EQGELAQWII QHSCADRVFF
     CNSGAEANEA AIKLARKYAH TVLDIEKPII LTANASFHGR TLATITATGQ AKYQKYFDPL
     VPGFHYVNYN DISAVEAAIS ELDEGDYRVA AILIEPLQGE GGVRPGDVEY FQKLRQICDD
     TGILLMFDEV QVGMGRSGKL WGYEYLGVEP DIFTSAKGLG GGIPIGAMMS KKFCDVFQPG
     EHASTFGGNP FACGVALAVC QTLERENILQ NVQDRGEQLR SGLRAIAAKY PHHLTEVRGW
     GLINGLELAA DIPLTAADVV KAAINEGLLL VPAGPKVVRF VPPLIVTEAE INTALKLLEK
     ALATVTA
//