ID A0A0Q7SYP1_9CAUL Unreviewed; 391 AA.
AC A0A0Q7SYP1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Acetylornithine aminotransferase {ECO:0000313|EMBL:KQY89488.1};
DE EC=2.6.1.11 {ECO:0000313|EMBL:KQY89488.1};
GN ORFNames=ASD25_02555 {ECO:0000313|EMBL:KQY89488.1};
OS Brevundimonas sp. Root1423.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=1736462 {ECO:0000313|EMBL:KQY89488.1, ECO:0000313|Proteomes:UP000051815};
RN [1] {ECO:0000313|Proteomes:UP000051815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1423 {ECO:0000313|Proteomes:UP000051815};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY89488.1, ECO:0000313|Proteomes:UP000051815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1423 {ECO:0000313|EMBL:KQY89488.1,
RC ECO:0000313|Proteomes:UP000051815};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {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:KQY89488.1}.
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DR EMBL; LMFL01000012; KQY89488.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q7SYP1; -.
DR Proteomes; UP000051815; 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 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 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 PANTHER; PTHR11986:SF113; ACETYLORNITHINE_SUCCINYLDIAMINOPIMELATE AMINOTRANSFERASE; 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 Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:KQY89488.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000051815};
KW Transferase {ECO:0000313|EMBL:KQY89488.1}.
SQ SEQUENCE 391 AA; 42194 MW; CC13B4A7427443CA CRC64;
MGVYNRAPLE VDRGQGARLW GKDGTEYLDC VMGISTNALG HANPVLVQAV KDQAEKLWHV
SNIFKIPGQE ALADALCEKS FADVVFFTNS GTEAVECALK TARRHHVANG HPERIDIYGF
DGSFHGRTYG AINAAANPSY TEGFGPKMEG FHQLVWGDKE ALEAAFRNPT TCAIILEPVQ
GEGGCRATPD EDLRWMRQMA DENGVLIIFD EVQCGMGRTG KLWAHEWAGM TPDIMAIAKA
LGGGFPIGAC LATADAAKGM TVGVHGSTFG GNPLAMAVGQ AAFGEISKAE TLAHVNEIAG
YLKQQLHGLA QRFPDVIVDV RGKGLLLGVK LVPNNREFMG WARDEQHLLV AGGGDNCCRI
LPPLNLTLEE AREAVERFER TCEFARSKMA A
//
