ID A0A0K1P8D3_9DELT Unreviewed; 398 AA. AC A0A0K1P8D3; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 08-JUN-2016, entry version 7. DE RecName: Full=Acetylornithine aminotransferase {ECO:0000256|HAMAP-Rule:MF_01107}; DE Short=ACOAT {ECO:0000256|HAMAP-Rule:MF_01107}; DE EC=2.6.1.11 {ECO:0000256|HAMAP-Rule:MF_01107}; GN Name=argD {ECO:0000256|HAMAP-Rule:MF_01107}; GN ORFNames=AKJ08_0162 {ECO:0000313|EMBL:AKU89775.1}; OS Vulgatibacter incomptus. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Vulgatibacteraceae; Vulgatibacter. OX NCBI_TaxID=1391653 {ECO:0000313|EMBL:AKU89775.1}; RN [1] {ECO:0000313|EMBL:AKU89775.1, ECO:0000313|Proteomes:UP000055590} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 27710 {ECO:0000313|EMBL:AKU89775.1, RC ECO:0000313|Proteomes:UP000055590}; RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V., RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., RA Henderson B.A., Jones I.B., McGettigan J.A., Micheletti S.J., RA Nasrallah M.E., Ortiz D., Piller C.R., Privatt S.R., Schneider S.L., RA Sharp S., Smith T.C., Stanton J.D., Ullery H.E., Wilson R.J., RA Serrano M.G., Buck G., Lee V., Wang Y., Carvalho R., Voegtly L., RA Shi R., Duckworth R., Johnson A., Loviza R., Walstead R., Shah Z., RA Kiflezghi M., Wade K., Ball S.L., Bradley K.W., Asai D.J., RA Bowman C.A., Russell D.A., Pope W.H., Jacobs-Sera D., Hendrix R.W., RA Hatfull G.F.; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + 2-oxoglutarate = N- CC acetyl-L-glutamate 5-semialdehyde + L-glutamate. CC {ECO:0000256|HAMAP-Rule:MF_01107}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01107}; CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01107}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)- CC acetyl-L-ornithine from L-glutamate: step 4/4. {ECO:0000256|HAMAP- CC Rule:MF_01107}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01107}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01107}. CC -!- MISCELLANEOUS: May also have succinyldiaminopimelate CC aminotransferase activity, thus carrying out the corresponding CC step in lysine biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01107}. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000256|SAAS:SAAS00571336}. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. ArgD subfamily. {ECO:0000256|HAMAP- CC Rule:MF_01107}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP012332; AKU89775.1; -; Genomic_DNA. DR KEGG; vin:AKJ08_0162; -. DR KO; K00821; -. DR Proteomes; UP000055590; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 2. DR HAMAP; MF_01107; ArgD_aminotrans_3; 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_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR PANTHER; PTHR11986; PTHR11986; 1. DR Pfam; PF00202; Aminotran_3; 1. DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR00707; argD; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01107}; KW Aminotransferase {ECO:0000256|HAMAP-Rule:MF_01107, KW ECO:0000256|SAAS:SAAS00461222, ECO:0000313|EMBL:AKU89775.1}; KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01107}; KW Complete proteome {ECO:0000313|Proteomes:UP000055590}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01107}; KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01107, KW ECO:0000256|RuleBase:RU003560, ECO:0000256|SAAS:SAAS00461208}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01107, KW ECO:0000256|SAAS:SAAS00461217, ECO:0000313|EMBL:AKU89775.1}. FT REGION 223 226 Pyridoxal phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_01107}. FT BINDING 138 138 Pyridoxal phosphate; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01107}. FT BINDING 141 141 N2-acetyl-L-ornithine. FT {ECO:0000256|HAMAP-Rule:MF_01107}. FT BINDING 280 280 N2-acetyl-L-ornithine. FT {ECO:0000256|HAMAP-Rule:MF_01107}. FT BINDING 281 281 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_01107}. FT MOD_RES 252 252 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|HAMAP-Rule:MF_01107}. SQ SEQUENCE 398 AA; 42912 MW; E11768BA2B12A3FF CRC64; MGRNEELADR ARNVLVGNYK QQPIAIERGE GCYLYDAEGR RYLDMIAGIA TVSLGHCHPK VVAALEAQSK QLWHASNVVY TLPQIELAER ICSSSFAERV FFCNSGAEAN EAALKLARRW QRDRGQDRFE IIAFQSSFHG RTLFTVTATG QPKYWEGFEP MVPGVHHAKY GDLASVEALI GPKTAAIIVE PVQGEGGVRP APKGFLAGLR KLADEHGLVL IFDEVQTGMG RTGPLFAYQR HGVEPDVMTL AKALGNGIPI GAMCTREELA RSLVPGTHAS TFGGNPLAAA CASAVFDELL DGGVLERGQI AGEYLAARLG DMARRLGPEK VVEARGQGLL HGVELLGPAA PVISRCRELG VIVNAAGEKV VRLAPPLIIE HVQIDEAVDV LERAIRES //