ID A0A3M8A1U9_9MICO Unreviewed; 396 AA.
AC A0A3M8A1U9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Acetylornithine transaminase {ECO:0000313|EMBL:RNB45218.1};
DE EC=2.6.1.11 {ECO:0000313|EMBL:RNB45218.1};
GN ORFNames=EDM22_16585 {ECO:0000313|EMBL:RNB45218.1};
OS Agromyces tardus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agromyces.
OX NCBI_TaxID=2583849 {ECO:0000313|EMBL:RNB45218.1, ECO:0000313|Proteomes:UP000275048};
RN [1] {ECO:0000313|EMBL:RNB45218.1, ECO:0000313|Proteomes:UP000275048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJ-23 {ECO:0000313|EMBL:RNB45218.1,
RC ECO:0000313|Proteomes:UP000275048};
RA Sun T.;
RT "Isolation, diversity and antibacterial activity of antinobacteria from the
RT wheat rhizosphere soil.";
RL Submitted (OCT-2018) 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}.
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:RNB45218.1}.
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DR EMBL; RHHB01000052; RNB45218.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8A1U9; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000275048; 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: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; 3.
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:RNB45218.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000275048};
KW Transferase {ECO:0000313|EMBL:RNB45218.1}.
SQ SEQUENCE 396 AA; 41552 MW; 8489D631096BAE1B CRC64;
MSDWQQRFDR RIMRSMGMPL AKLVRGEGAR VWDDAGNEYL DFLAGIAVNS LGHAHPVFVE
AVSRQAATLA HVSNYFMTEP ALELAERLVR LAGAGDQGRV WFGNSGAEAN EAAFKLARLN
NSGGARTRVL ALVDAFHGRT MGSLALTGKP HMRQAFEPLP GGVEHLPSTI QALEANLDDA
VAALFVEPIK GEAGVVELPE GYLEAARELT HRHGALLIVD EVQTGAGRTG EWFAYQHAGI
TPDAIAVAKG IGGGFPIGGI VTFGHASELY SKGQHGSTFG GNPLATAVAN AVLGEIERAG
LVDNAAVRGA QLRDRVLGLG SPLVTGVRGR GLLLGVALAE PVAQQVSDAA LANGLIVNAA
NDATIRMAPP LIIGDAELDE FDERFARALD SVAATL
//
