ID A0A067FDW0_CITSI Unreviewed; 465 AA.
AC A0A067FDW0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=acetylornithine transaminase {ECO:0000256|ARBA:ARBA00012919};
DE EC=2.6.1.11 {ECO:0000256|ARBA:ARBA00012919};
GN ORFNames=CISIN_1g012363mg {ECO:0000313|EMBL:KDO61627.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO61627.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO61627.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) 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; KK784924; KDO61626.1; -; Genomic_DNA.
DR EMBL; KK784924; KDO61627.1; -; Genomic_DNA.
DR RefSeq; XP_006475328.1; XM_006475265.2.
DR STRING; 2711.A0A067FDW0; -.
DR PaxDb; 2711-XP_006475328-1; -.
DR eggNOG; KOG1401; Eukaryota.
DR OrthoDB; 5487467at2759; -.
DR UniPathway; UPA00068; UER00109.
DR Proteomes; UP000027120; Unassembled WGS sequence.
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 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000027120}.
SQ SEQUENCE 465 AA; 50013 MW; F984B69076D129CF CRC64;
MQNAMSSTFQ APLQVPLSQS GNLRRQIKFN GVKRRPMVAA ASVNVEVNDA ARGSAGGLGR
NNKEVMEAEK KLLVGTYNRA PVVLASGKGC KLYDAEGREY LDLSSGIAVN ALGHGDADWI
KAVVDQANVL THVSNMYYSI PQIELAKRLV ACSFADRVFF SNTGTEANEA AIKFARKFQR
HSNPDSKEPA TEFVSFTNSF HGRTMGALAL TSKEHYRSPF EPVMPGVNFV EYGNIEATRK
LIQPGKTAAV FVEPIQGEGG IYSATKEFLQ FLRDACDDAG ALLVFDEVQC GLGRTGYLWA
HEHYGIFPDI MTLAKPLAGG LPIGAALVTE KVASAINYGD HGSTFAGSPL VCNAAIAVLD
KISNPAFLAS VSKKGHYFKE TLKQKLARNP HVKDVRGLGL IIGIEFDVSA TPVVDACRDS
GLLVLTAGKG NVVRLVPPLI ISEQELDQAV EILCKTLPVL DSNSN
//
