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ARGD_RALSO
ID   ARGD_RALSO              Reviewed;         399 AA.
AC   Q8XWN8;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Acetylornithine aminotransferase {ECO:0000255|HAMAP-Rule:MF_01107};
DE            Short=ACOAT {ECO:0000255|HAMAP-Rule:MF_01107};
DE            EC=2.6.1.11 {ECO:0000255|HAMAP-Rule:MF_01107};
GN   Name=argD {ECO:0000255|HAMAP-Rule:MF_01107}; OrderedLocusNames=RSc2435;
GN   ORFNames=RS02668;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-
CC         acetyl-L-glutamate 5-semialdehyde; Xref=Rhea:RHEA:18049,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29123, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57805; EC=2.6.1.11; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01107};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01107};
CC       Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01107};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 4/4. {ECO:0000255|HAMAP-
CC       Rule:MF_01107}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01107}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01107}.
CC   -!- MISCELLANEOUS: May also have succinyldiaminopimelate aminotransferase
CC       activity, thus carrying out the corresponding step in lysine
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01107}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. ArgD subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01107}.
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DR   EMBL; AL646052; CAD16142.1; -; Genomic_DNA.
DR   RefSeq; WP_011002354.1; NC_003295.1.
DR   AlphaFoldDB; Q8XWN8; -.
DR   SMR; Q8XWN8; -.
DR   STRING; 267608.RSc2435; -.
DR   EnsemblBacteria; CAD16142; CAD16142; RSc2435.
DR   GeneID; 60501944; -.
DR   KEGG; rso:RSc2435; -.
DR   PATRIC; fig|267608.8.peg.2478; -.
DR   eggNOG; COG4992; Bacteria.
DR   HOGENOM; CLU_016922_10_1_4; -.
DR   OMA; FWGWQAH; -.
DR   UniPathway; UPA00068; UER00109.
DR   Proteomes; UP000001436; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01107; ArgD_aminotrans_3; 1.
DR   InterPro; IPR004636; AcOrn/SuccOrn_fam.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; SSF53383; 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; Reference proteome; Transferase.
FT   CHAIN           1..399
FT                   /note="Acetylornithine aminotransferase"
FT                   /id="PRO_0000112772"
FT   BINDING         102..103
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   BINDING         138
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   BINDING         141
FT                   /ligand="N(2)-acetyl-L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:57805"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   BINDING         223..226
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   BINDING         280
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   MOD_RES         252
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
SQ   SEQUENCE   399 AA;  42778 MW;  D1D6C190E8351FAC CRC64;
     MAFADYPVQS LMYITNRPEI VFTEGKGSWL TDHNGKRYLD FVQGWAVNCL GHSNDGMIEA
     LNAQAKKLIN PSPAFYNEPM AKLAGLLSAH SCFDKVFFAN SGAEANEGAI KLARKWGKKH
     KSGAGKNRFE IITFDHSFHG RTLATMSASG KAGWDTIFAP QVPGFPKAIL NDIASVEALI
     TDETVGVMLE PVQGEGGVLP ATQEFMQQLR ALTRKHKLLL IVDEVQAGCG RCGTLFAYQL
     SNIEPDIMTL GKGIGGGVPL SALLCTDEVA SFEAGDQGGT YNGNPLMTAV GCSVIEQLLA
     PGFLAGVQER GAYLRAQLLE LSEAFGLAGE RGEGLLRALL LGKDIGGQLV EAAREMNPTG
     LLLNAPRPNI LRFMPALNVT TDEIDTMIGM LRTLLKAHG
 
 
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