ID Q1MS82_LAWIP Unreviewed; 420 AA.
AC Q1MS82;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Ornithine/acetylornithine aminotransferase {ECO:0000313|EMBL:CAJ54143.1};
GN Name=argD {ECO:0000313|EMBL:CAJ54143.1};
GN OrderedLocusNames=LI0087 {ECO:0000313|EMBL:CAJ54143.1};
OS Lawsonia intracellularis (strain PHE/MN1-00).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Lawsonia.
OX NCBI_TaxID=363253 {ECO:0000313|EMBL:CAJ54143.1, ECO:0000313|Proteomes:UP000002430};
RN [1] {ECO:0000313|EMBL:CAJ54143.1, ECO:0000313|Proteomes:UP000002430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHE/MN1-00 {ECO:0000313|EMBL:CAJ54143.1,
RC ECO:0000313|Proteomes:UP000002430};
RA Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT "The complete genome sequence of Lawsonia intracellularis: the causative
RT agent of proliferative enteropathy.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR EMBL; AM180252; CAJ54143.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1MS82; -.
DR STRING; 363253.LI0087; -.
DR KEGG; lip:LI0087; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_1_7; -.
DR Proteomes; UP000002430; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProt.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004636; AcOrn/SuccOrn_fam.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00707; argD; 1.
DR PANTHER; PTHR11986:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aminotransferase {ECO:0000313|EMBL:CAJ54143.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000002430};
KW Transferase {ECO:0000313|EMBL:CAJ54143.1}.
SQ SEQUENCE 420 AA; 46835 MW; 728C917C7BC9D624 CRC64;
MVLDIQEKTN SSKGKVFMQL SYNESIMLHE KKLLCHTYGR YPIHVVEAHG SIILDANGNK
FIDLLSGLAV TSLGHCNEEI AEVIEKQARK LIHTSNLLYH DEQLELAERL LSMGHFTKVF
FSNSGAEANE TSFKLTRRYM QHIKKCNAFE IISLEGSFHG RTLTTVAATG QPSLKEGFAP
MPNGFKQVPW NDLVALEEAI TPSTAAVLIE IIQGEGGVRP MDSDYIIGIE KLCRKHDLLL
IVDEIQTGLC RTGQYWAFQH FPIKPDILSC AKALANGLPI SAILTTDEIA QAFVVGSHGT
TFGGGPLISA VATKTIEIMQ RDNLHKRAEK LGNIFIQRLK NIANRHPTKI QEVRGMGLMI
GIVLPCPGKP LWEKLLQKGF LLNLTQNNIL RLLPALTIDE HYLETFAQTL EDTLEKYIQE
//
