ID   ARGD_METKA              Reviewed;         389 AA.
AC   Q8TUZ5;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   16-JUN-2009, entry version 49.
DE   RecName: Full=Acetylornithine aminotransferase;
DE            Short=ACOAT;
DE            EC=2.6.1.11;
GN   Name=argD; OrderedLocusNames=MK1606;
OS   Methanopyrus kandleri.
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=2320;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   MEDLINE=21927647; PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L.,
RA   Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O.,
RA   Malykh A.G., Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19
RT   and monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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; AE010450; AAM02819.1; -; Genomic_DNA.
DR   RefSeq; NP_614889.1; -.
DR   HSSP; P12995; 1QJ3.
DR   GeneID; 1478201; -.
DR   GenomeReviews; AE009439_GR; MK1606.
DR   KEGG; mka:MK1606; -.
DR   NMPDR; fig|190192.1.peg.1602; -.
DR   HOGENOM; Q8TUZ5; -.
DR   OMA; Q8TUZ5; IDCVAGI.
DR   BioCyc; MKAN190192:MK1606-MON; -.
DR   BRENDA; 2.6.1.11; 7577.
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    389       Acetylornithine aminotransferase.
FT                                /FTId=PRO_0000112822.
FT   REGION      104    105       Pyridoxal phosphate binding (By
FT                                similarity).
FT   REGION      216    219       Pyridoxal phosphate binding (By
FT                                similarity).
FT   BINDING     131    131       Pyridoxal phosphate; via carbonyl oxygen
FT                                (By similarity).
FT   BINDING     134    134       N(2)-acetyl-L-ornithine (By similarity).
FT   BINDING     273    273       N(2)-acetyl-L-ornithine (By similarity).
FT   BINDING     274    274       Pyridoxal phosphate (By similarity).
FT   MOD_RES     245    245       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   389 AA;  42025 MW;  AD72B13CCFE962F9 CRC64;
     MDARELIDKY HMNTYSRFPV TLVPGEGARV WDDEGNEYID LVAGIAVNVL GHCHPAVVEA
     VKEQVERLIH CSNLYYNEPQ AEAARLLAEA APKDLNKVFF CNSGTESVEC AIKLARKFTG
     CTKFIAFEGG FHGRTMGALS ATWKPEFREP FEPLVPEFEH VPYGDVNAVE KAIDDDTAAV
     IVEPVQGEAG VRIPPEGFLR ELRELCDEHG LLLIVDEVQS GMGRTGQFFA FEHEDVLPDI
     VCLAKGLGGG VPVGATIARE EVAEAFEPGD HGSTFGGNPL ACAAVCAAVS TVLEENLPEA
     AERKGKLAMR ILSEAEDVVE EVRGRGLMMG VEVGDDERAK DVAREMLDRG ALVNVTSGDV
     IRLVPPLVIG EDELEKALAE LADALRASG
//