ID D3PZD8_STANL Unreviewed; 417 AA.
AC D3PZD8;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Acetylornithine transaminase {ECO:0000313|EMBL:ADD41612.1};
DE EC=2.6.1.11 {ECO:0000313|EMBL:ADD41612.1};
GN OrderedLocusNames=Snas_1916 {ECO:0000313|EMBL:ADD41612.1};
OS Stackebrandtia nassauensis (strain DSM 44728 / CIP 108903 / NRRL B-16338 /
OS NBRC 102104 / LLR-40K-21).
OC Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC Stackebrandtia.
OX NCBI_TaxID=446470 {ECO:0000313|EMBL:ADD41612.1, ECO:0000313|Proteomes:UP000000844};
RN [1] {ECO:0000313|EMBL:ADD41612.1, ECO:0000313|Proteomes:UP000000844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44728 / CIP 108903 / NRRL B-16338 / NBRC 102104 /
RC LLR-40K-21 {ECO:0000313|Proteomes:UP000000844};
RX PubMed=21304662; DOI=10.4056/sigs.47643;
RA Munk C., Lapidus A., Copeland A., Jando M., Mayilraj S.,
RA Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F.,
RA Han C., Detter J.C., Bruce D., Goodwin L., Chain P., Pitluck S., Goker M.,
RA Ovchinikova G., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Stackebrandtia nassauensis type strain (LLR-
RT 40K-21).";
RL Stand. Genomic Sci. 1:292-299(2009).
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; CP001778; ADD41612.1; -; Genomic_DNA.
DR RefSeq; WP_013017183.1; NC_013947.1.
DR AlphaFoldDB; D3PZD8; -.
DR STRING; 446470.Snas_1916; -.
DR KEGG; sna:Snas_1916; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_11; -.
DR OrthoDB; 3204291at2; -.
DR Proteomes; UP000000844; 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; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 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:0000313|EMBL:ADD41612.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000000844};
KW Transferase {ECO:0000313|EMBL:ADD41612.1}.
SQ SEQUENCE 417 AA; 44169 MW; 13AB2739C1B45F1B CRC64;
MAQLSPLLKQ ATPVVVDHGE GVYLFDSDGR RYLDFTAGIG VTSTGHCHPK VVQAAQEQVG
KLIHGQYTTV MHQPMLELTR RLGEVLPPGL DSLFYSNSGS EAVEAALRLS RQATGRPNVV
VFHGGFHGRT VAASTMTTSG TRFSAGFSPL MSGVHVAPFP NAYRYGWDER TATEFALREL
DYLFATLSAP NETAAFFIEP VLGEGGYVPA NTAFLQGLRE RADEHGILLV IDEIQTGFGR
TGKFWGHDHF DVRPDIVLIA KGLASGFPIS GIAASKELMS KAWPGSQGGT YGGNAVACAA
ALATLEVIQE EGLVDNAAAR GLQLLEGARQ IGDKTPAIGD VRGLGLLVGS EFTTPDGKPD
TATAQAAQKE AAARGLLMLT CGAHMNVVRM IPALVVNSEQ IDEALGIWAD VVADVAK
//
