ID Q023W8_SOLUE Unreviewed; 406 AA.
AC Q023W8;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Acetylornithine aminotransferase {ECO:0000313|EMBL:ABJ83708.1};
DE EC=2.6.1.11 {ECO:0000313|EMBL:ABJ83708.1};
GN OrderedLocusNames=Acid_2719 {ECO:0000313|EMBL:ABJ83708.1};
OS Solibacter usitatus (strain Ellin6076).
OC Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC Solibacter.
OX NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ83708.1};
RN [1] {ECO:0000313|EMBL:ABJ83708.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ83708.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Janssen P.H., Kuske C.R., Richardson P.;
RT "Complete sequence of Solibacter usitatus Ellin6076.";
RL Submitted (OCT-2006) 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}.
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DR EMBL; CP000473; ABJ83708.1; -; Genomic_DNA.
DR AlphaFoldDB; Q023W8; -.
DR STRING; 234267.Acid_2719; -.
DR KEGG; sus:Acid_2719; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_1_0; -.
DR InParanoid; Q023W8; -.
DR OrthoDB; 9807885at2; -.
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; 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; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aminotransferase {ECO:0000313|EMBL:ABJ83708.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:ABJ83708.1}.
SQ SEQUENCE 406 AA; 44360 MW; D9DC7FC270AD48B9 CRC64;
MTTALPPVQD TLAQPIMDLE REYLLQNYAR YPLVLARGKG CYLYDLAGKR YLDLISGIGV
NALGHAHPRI TKVIRAQAAL LLHTSNLYYH EYQGALAKRL AQMSGLQRCF FSNTGTEAVE
GALKMAHSHG RAIHSDKYEV IALDNSFHGR TLGALSITGQ AKYRQDFEPL VPGARFVPAN
DIAALEGAFS ERTAAIVLEM IQGEGGINPL SPEYVVKARE LADRYNALLV LDETQCGVGR
PGTYFSYQRS SHITMPDVMV SAKPLACGIP LGVIMANERA AAAIKPGMHG STFGGGPLAC
RVALEFCDIL DELLPSIQRV GGYLHVELNE LARKHSFIKE VRGFGLMIGV ELAMPGKQLV
LDAMAQGLLI NCTHDTVLRF LPPYIITEKE VDLAVRTLGK IFSRVK
//
