ID A0A2I0VTW6_9ASPA Unreviewed; 470 AA.
AC A0A2I0VTW6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=acetylornithine transaminase {ECO:0000256|ARBA:ARBA00012919};
DE EC=2.6.1.11 {ECO:0000256|ARBA:ARBA00012919};
GN Name=AG118 {ECO:0000313|EMBL:PKU66843.1};
GN ORFNames=MA16_Dca014450 {ECO:0000313|EMBL:PKU66843.1};
OS Dendrobium catenatum.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC Epidendroideae; Malaxideae; Dendrobiinae; Dendrobium.
OX NCBI_TaxID=906689 {ECO:0000313|EMBL:PKU66843.1, ECO:0000313|Proteomes:UP000233837};
RN [1] {ECO:0000313|EMBL:PKU66843.1, ECO:0000313|Proteomes:UP000233837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=The whole plant {ECO:0000313|EMBL:PKU66843.1};
RX PubMed=26754549; DOI=10.1038/srep19029;
RA Zhang G.Q., Xu Q., Bian C., Tsai W.C., Yeh C.M., Liu K.W., Yoshida K.,
RA Zhang L.S., Chang S.B., Chen F., Shi Y., Su Y.Y., Zhang Y.Q., Chen L.J.,
RA Yin Y., Lin M., Huang H., Deng H., Wang Z.W., Zhu S.L., Zhao X., Deng C.,
RA Niu S.C., Huang J., Wang M., Liu G.H., Yang H.J., Xiao X.J., Hsiao Y.Y.,
RA Wu W.L., Chen Y.Y., Mitsuda N., Ohme-Takagi M., Luo Y.B., Van de Peer Y.,
RA Liu Z.J.;
RT "The Dendrobium catenatum Lindl. genome sequence provides insights into
RT polysaccharide synthase, floral development and adaptive evolution.";
RL Sci. Rep. 6:19029-19029(2016).
RN [2] {ECO:0000313|EMBL:PKU66843.1, ECO:0000313|Proteomes:UP000233837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=The whole plant {ECO:0000313|EMBL:PKU66843.1};
RX PubMed=28902843; DOI=10.1038/nature23897;
RA Zhang G.Q., Liu K.W., Li Z., Lohaus R., Hsiao Y.Y., Niu S.C., Wang J.Y.,
RA Lin Y.C., Xu Q., Chen L.J., Yoshida K., Fujiwara S., Wang Z.W., Zhang Y.Q.,
RA Mitsuda N., Wang M., Liu G.H., Pecoraro L., Huang H.X., Xiao X.J., Lin M.,
RA Wu X.Y., Wu W.L., Chen Y.Y., Chang S.B., Sakamoto S., Ohme-Takagi M.,
RA Yagi M., Zeng S.J., Shen C.Y., Yeh C.M., Luo Y.B., Tsai W.C.,
RA Van de Peer Y., Liu Z.J.;
RT "The Apostasia genome and the evolution of orchids.";
RL Nature 549:379-383(2017).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 4/4.
CC {ECO:0000256|ARBA:ARBA00005024}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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DR EMBL; KZ503238; PKU66843.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0VTW6; -.
DR STRING; 906689.A0A2I0VTW6; -.
DR OrthoDB; 5487467at2759; -.
DR UniPathway; UPA00068; UER00109.
DR Proteomes; UP000233837; 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:UniProtKB-UniPathway.
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 HAMAP; MF_01107; ArgD_aminotrans_3; 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; 2.
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:PKU66843.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000233837};
KW Transferase {ECO:0000313|EMBL:PKU66843.1}.
SQ SEQUENCE 470 AA; 50371 MW; E5EDBB370D9ECB29 CRC64;
MSSLQSFVAV STSSANDLRH LFRLNSQKAP PGTQPYLPRI SCCFVSEDTQ KSAPSISTGN
RLLSAKSEDL IEREKRVLVG TYARAPVVLV RGKGCKLYDV DGMEYVDMTA GIAVNSLGYG
DGEWVKAVAE QAKSLAHVSN VYYSEPQVIL AEHLVECSFA DRVFFTNSGT EANEAAIKFA
RKFQRVSCDS DTHATEFVSF SNSFHGRTMG ALALTSKENY RLPFEPVMPG VKFVKYGDID
GAKKAIVSGK TAAVFVEPIQ GEGGIHSATK EFLQTLRIAC DDAGALLIFD EVQCGLGRTG
YLWAHEPYGI VPDIMTLAKP LAGGLPIGVA LTTEKVASAI NYGDHGSTFA GSPLVCHAAL
TVLKRIKDPG FLSAVTKKGL YFKELLTHKL GANSHVKEVR GLGLIVGIDL DVLASPLVDA
CRALGLLVLT AGKGNVVRLV PPLIISEEEL KQAADIIERC LPALDADGVH
//