ID   F7YU15_9THEM            Unreviewed;       397 AA.
AC   F7YU15;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   01-MAY-2013, entry version 15.
DE   RecName: Full=Acetylornithine aminotransferase;
DE            Short=ACOAT;
DE            EC=2.6.1.11;
GN   Name=argD; ORFNames=Theth_1544;
OS   Thermotoga thermarum DSM 5069.
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=688269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 5069;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Zeytun A., Brettin T.,
RA   Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Thermotoga thermarum DSM 5069.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. ArgD subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002351; AEH51597.1; -; Genomic_DNA.
DR   RefSeq; YP_004660693.1; NC_015707.1.
DR   EnsemblBacteria; AEH51597; AEH51597; Theth_1544.
DR   GeneID; 10886317; -.
DR   KEGG; tta:Theth_1544; -.
DR   KO; K00821; -.
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; 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; TIGR00707; argD; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Arginine biosynthesis;
KW   Cytoplasm; Pyridoxal phosphate; Transferase.
FT   REGION       97     98       Pyridoxal phosphate binding (By
FT                                similarity).
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     270    270       N2-acetyl-L-ornithine (By similarity).
FT   BINDING     271    271       Pyridoxal phosphate (By similarity).
FT   MOD_RES     243    243       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   397 AA;  43883 MW;  3EAB44E273522DE9 CRC64;
     MNEYLMNTYS RYPIVLDHGK GSWVWDENGN KYLDFAAGIA VNSLGHANRK LLKALKTQAE
     KLIHCSNLYW TRPQMELAKL LIEKSFGKGK VFFANSGTEA NEAAIKIARK YGKKFSQTKF
     KILSATNSFH GRTYGSLSAT AQEKYQKPFT PLVDGFEYFE FNNIEDLKKK MSEDICAVIL
     EPIQGESGIV PAKKEFLQQV RNLCDSYNAL LIFDEVQCGV GRTGKLFAYQ LYDVQPDVLT
     LAKGLGGGLP IGAVLVNEKA DILEPGDHGS TFGGNPLVCS VAISVLQEIS KPEFLSKVEK
     AGKRLKNGLL RLKKKYPELI KDVRGIGLMI GVELNKISAK EFSSTCVKEG LLLAPAGNNT
     LRFLPPLTIS FKEISYGLNI FESCLQKVMQ SNLQAAG
//