ID G0L7H9_ZOBGA Unreviewed; 393 AA.
AC G0L7H9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Acetylornithine aminotransferase {ECO:0000313|EMBL:CAZ97810.1};
DE EC=2.6.1.11 {ECO:0000313|EMBL:CAZ97810.1};
GN OrderedLocusNames=zobellia_3672 {ECO:0000313|EMBL:CAZ97810.1};
OS Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 /
OS NCIMB 13871 / Dsij).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zobellia.
OX NCBI_TaxID=63186 {ECO:0000313|EMBL:CAZ97810.1, ECO:0000313|Proteomes:UP000008898};
RN [1] {ECO:0000313|Proteomes:UP000008898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC {ECO:0000313|Proteomes:UP000008898};
RG Genoscope - CEA;
RT "Complete genome sequence of Zobellia galactanivorans Dsij.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAZ97810.1, ECO:0000313|Proteomes:UP000008898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC {ECO:0000313|Proteomes:UP000008898};
RX PubMed=22513138; DOI=10.1111/j.1462-2920.2012.02751.x;
RA Thomas F., Barbeyron T., Tonon T., Genicot S., Czjzek M., Michel G.;
RT "Characterization of the first alginolytic operons in a marine bacterium:
RT from their emergence in marine Flavobacteriia to their independent
RT transfers to marine Proteobacteria and human gut Bacteroides.";
RL Environ. Microbiol. 14:2379-2394(2012).
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}.
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DR EMBL; FP476056; CAZ97810.1; -; Genomic_DNA.
DR RefSeq; WP_013995000.1; NZ_JAUOSS010000002.1.
DR AlphaFoldDB; G0L7H9; -.
DR STRING; 63186.ZOBELLIA_3672; -.
DR KEGG; zga:ZOBELLIA_3672; -.
DR PATRIC; fig|63186.3.peg.3588; -.
DR HOGENOM; CLU_016922_10_1_10; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000008898; Chromosome.
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: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; 3.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:CAZ97810.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000008898};
KW Transferase {ECO:0000313|EMBL:CAZ97810.1}.
SQ SEQUENCE 393 AA; 43080 MW; 81EBA45137C14774 CRC64;
MKEDFLKYQA QTSPYPLALP ISHAKGSYIY DTDGKAHLDF VAGVSACSLG HCHPKVVEAV
QKQAETYMHV MVYGEYIQEP AVAYTKLLAS LLPPSLETTY MVNSGTEAVE GAMKLARRAT
GRSRLLAARH AYHGNTMGSL SVMGYEERKS AFRPLIPDVG FIRFNNEDDL DKITDKTAAV
ILETIQGGAG FIEPTNGYLK KVRQRCNATG TMLILDEIQP GFGRTGKLFA FEHYDCVPDI
LVMGKGMASG LPVGAFTASK ELMSTLQDSP KLGHITTFGG NPVIASACLA TLKEITETQL
IADTLKKEAL VRKLLKHRLI KEIRGKGLML ALIMENAEIA NHVILNCAKR GLILFWLLFE
PRAVRISPPL TMSTEEIESG CGIILEVLEG YKQ
//
