ID A0A0N8NTZ5_9CLOT Unreviewed; 423 AA.
AC A0A0N8NTZ5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Acetylornithine/acetyl-lysine aminotransferase {ECO:0000313|EMBL:KPU46208.1};
DE EC=2.6.1.- {ECO:0000313|EMBL:KPU46208.1};
DE EC=2.6.1.11 {ECO:0000313|EMBL:KPU46208.1};
GN Name=argD_1 {ECO:0000313|EMBL:KPU46208.1};
GN ORFNames=OXPF_03180 {ECO:0000313|EMBL:KPU46208.1};
OS Oxobacter pfennigii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Oxobacter.
OX NCBI_TaxID=36849 {ECO:0000313|EMBL:KPU46208.1, ECO:0000313|Proteomes:UP000050326};
RN [1] {ECO:0000313|EMBL:KPU46208.1, ECO:0000313|Proteomes:UP000050326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3222 {ECO:0000313|EMBL:KPU46208.1,
RC ECO:0000313|Proteomes:UP000050326};
RA Poehlein A., Bengelsdorf F.R., Schiel-Bengelsdorf B., Duerre P., Daniel R.;
RT "Genome sequence of Oxobacter pfennigii DSM 3222.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC 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:KPU46208.1}.
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DR EMBL; LKET01000014; KPU46208.1; -; Genomic_DNA.
DR RefSeq; WP_054873462.1; NZ_LKET01000014.1.
DR AlphaFoldDB; A0A0N8NTZ5; -.
DR STRING; 36849.OXPF_03180; -.
DR PATRIC; fig|36849.3.peg.345; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000050326; Unassembled WGS sequence.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IEA:RHEA.
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 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; 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 PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 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:0000313|EMBL:KPU46208.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000050326};
KW Transferase {ECO:0000313|EMBL:KPU46208.1}.
FT COILED 181..208
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 423 AA; 47129 MW; 4441E84C3B410807 CRC64;
MSYIGPENIL SIRQQYFFPA TSHFYKNPPQ IVKGFMQYLY DQDNKKYTDF YGGVSVMNCG
HSNPEIINET AEQLKDLQHT TTLFFTQPMA LLAEELAKIL PGDIKRTFFC VTGSEANEGA
MALARLHTKK NGFIALNGGL HGRTHLTLSV TGIPMWRLDD NLMKDNIFFI DRPYSPDESY
EKAMEKSLEQ LKKVLEEHGN NIAAMILEPI QGNGGIIMYP LNYLKEVKRL LEKHGVLLII
DEVQTGYGRT GKMFCIEHYD VVPDIIVTAK ALGNGIPIST FSTTDEIAQS FNKPSASTFG
GNPVAATTAL NVLKYIKSHD LISRAEKLGK ILKQQLEEIP SPYIQEVRGI GLMIGVQIHA
VDENQPSHAI TDVILEEMKD LGFLIGKNGL DRDVLAFQPP LVVTEEDINE VVAALKKVLA
KLS
//
