ID S8C1M9_9LAMI Unreviewed; 417 AA.
AC S8C1M9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=acetylornithine transaminase {ECO:0000256|ARBA:ARBA00012919};
DE EC=2.6.1.11 {ECO:0000256|ARBA:ARBA00012919};
DE Flags: Fragment;
GN ORFNames=M569_14125 {ECO:0000313|EMBL:EPS60675.1};
OS Genlisea aurea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS60675.1, ECO:0000313|Proteomes:UP000015453};
RN [1] {ECO:0000313|EMBL:EPS60675.1, ECO:0000313|Proteomes:UP000015453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23855885;
RA Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA Logacheva M.D.;
RT "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT number of genes and short non-coding sequences.";
RL BMC Genomics 14:476-476(2013).
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}.
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:EPS60675.1}.
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DR EMBL; AUSU01007376; EPS60675.1; -; Genomic_DNA.
DR AlphaFoldDB; S8C1M9; -.
DR OrthoDB; 5487467at2759; -.
DR UniPathway; UPA00068; UER00109.
DR Proteomes; UP000015453; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000015453}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EPS60675.1"
FT NON_TER 417
FT /evidence="ECO:0000313|EMBL:EPS60675.1"
SQ SEQUENCE 417 AA; 44457 MW; 42F62445A9DFD48C CRC64;
GVGVGVRVPD SNSEIREKSS ADVIADENKF VVGTYARAPV VFSSGIGCTL YDVEGREYLD
LTSGIAVNAL GHGDPDFVRA VSEQVEVLTH VSNVYYSIPQ VELAKRLVST SFADRVFFCN
SGTEANEAAI KFSRKFQRVK KPQDPPVEFI AFSNCFHGRT MGALALTSKE HYRSPFEPVM
PGVHFLEYGD SESAVGLIRS GKIAAVFVEP IQGEGGIYGA PPQFLEALRV ACDDAGCVLV
FDEVQCGLGR TGYLWAHEAY GIFPDVMTLA KPLAGGLPIG AVLVTESIAS AIDRGDHGST
FAGNPLVCKA GIAVLDKISD RSFLAGVSEK GGYFKRLLEE KLSENPHVKG VRGFGLIVGV
ELDVSGSALV EACRESGLLV LTAGKGNVIR MVPPLIISKE ELERAADILV SCLPALE
//
