ID A0A059BYR3_EUCGR Unreviewed; 471 AA.
AC A0A059BYR3;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=acetylornithine transaminase {ECO:0000256|ARBA:ARBA00012919};
DE EC=2.6.1.11 {ECO:0000256|ARBA:ARBA00012919};
GN ORFNames=EUGRSUZ_F04428 {ECO:0000313|EMBL:KCW71348.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW71348.1};
RN [1] {ECO:0000313|EMBL:KCW71348.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW71348.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) 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; 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; KK198758; KCW71348.1; -; Genomic_DNA.
DR RefSeq; XP_010064050.1; XM_010065748.2.
DR AlphaFoldDB; A0A059BYR3; -.
DR STRING; 71139.A0A059BYR3; -.
DR EnsemblPlants; KCW71348; KCW71348; EUGRSUZ_F04428.
DR GeneID; 104451004; -.
DR Gramene; KCW71348; KCW71348; EUGRSUZ_F04428.
DR KEGG; egr:104451004; -.
DR eggNOG; KOG1401; Eukaryota.
DR InParanoid; A0A059BYR3; -.
DR OMA; IDHAEYN; -.
DR OrthoDB; 5487467at2759; -.
DR UniPathway; UPA00068; UER00109.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
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; IBA:GO_Central.
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:SF116; ACETYLORNITHINE TRANSAMINASE; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}.
SQ SEQUENCE 471 AA; 50712 MW; C9133FDB6683425F CRC64;
MTFARASLDR SILQSPDLLR RRNPVWERPP SSLVKLPRGG AGIAAGLNLE VKEPRAPPRN
VGFGDNSKGV MAAEGEVLVG TYARAPVVLA SGRGCKLYDV EGREYLDLSS GIAVNALGHG
DPDWVNAVVE QANTLTHVSN VYYSVPQVEL AKHLVASSFA DRVFFTNSGT EANEAAIKFA
RKFQRHTHPD EKEPATEFIS FTNSFHGRTM GALALTSKEN YRTPFQPVMP GVTFVEYGNI
EATKEKIKRG KTAAVFVEPI QGEGGIYSAT REFLQYLRSA CDDAGALLVF DEIQCGLGRS
GYLWAYEAYG VYPDIMTLAK PLAGGLPIGA VLVTEEVASA MKYGDHGSTF AGSPLVCKAA
QAVLDKISKP DFLASVRKNG EYFKQKLVQK LGGNSHVKEV RGLGLIIGIE LDVSASPLVD
ACRNSGLLIL TAGKGNVVRL VPPLIITVEE LDEAVEILFN ALPALDENSS N
//
