ID A0A0Q4CIC5_9SPHN Unreviewed; 398 AA.
AC A0A0Q4CIC5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Acetylornithine aminotransferase {ECO:0000313|EMBL:KQM24699.1};
DE EC=2.6.1.11 {ECO:0000313|EMBL:KQM24699.1};
GN ORFNames=ASE58_14925 {ECO:0000313|EMBL:KQM24699.1};
OS Sphingomonas sp. Leaf9.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1735674 {ECO:0000313|EMBL:KQM24699.1, ECO:0000313|Proteomes:UP000051210};
RN [1] {ECO:0000313|EMBL:KQM24699.1, ECO:0000313|Proteomes:UP000051210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf9 {ECO:0000313|EMBL:KQM24699.1,
RC ECO:0000313|Proteomes:UP000051210};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM24699.1, ECO:0000313|Proteomes:UP000051210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf9 {ECO:0000313|EMBL:KQM24699.1,
RC ECO:0000313|Proteomes:UP000051210};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQM24699.1}.
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DR EMBL; LMKC01000005; KQM24699.1; -; Genomic_DNA.
DR RefSeq; WP_055822975.1; NZ_LMKC01000005.1.
DR AlphaFoldDB; A0A0Q4CIC5; -.
DR Proteomes; UP000051210; Unassembled WGS sequence.
DR GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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:SF113; ACETYLORNITHINE_SUCCINYLDIAMINOPIMELATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:KQM24699.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:KQM24699.1}.
SQ SEQUENCE 398 AA; 41897 MW; 032E3907E3E5A878 CRC64;
MTDPLMNLYN RAPIAVDRGE GVWLIDTEGR RYIDCVAGIA TDALGHAHPA LVAALTQQAG
KLWHVSNIFR IPGQEALAQR LVDASFADCV FFANTGTEAV ECAIKTARRY HHVNGQPERI
DIVGFAGSFH GRTYAAINAS GNAGYMEGCG PRLPGFVQLS IDDAAAIEAA IASPTTAAVI
VEPVQGEGGA RALSGEWLLR LRELTRRHGV LLIHDEVQSG MGRTGRLFAH QWFDGAAPDI
MALAKALGSG FPVGACLATT EAAKGMTPGV HGTTFGGNPL AMAVGIAAFD TIANEDTLAH
ARAASADFFD RLEGLRSRFP DVIAEVRGKG LLIGLKMIPN NREFMGIARD HGILVAGGGE
NCVRLLPSLL ISAEEVAEAV TRLEAACVAA RGLMAEAA
//
