ID Q7NWG4_CHRVO Unreviewed; 459 AA. AC Q7NWG4; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 27-MAR-2024, entry version 127. DE RecName: Full=Putative 8-amino-7-oxononanoate synthase {ECO:0000256|ARBA:ARBA00021531}; GN OrderedLocusNames=CV_2025 {ECO:0000313|EMBL:AAQ59697.1}; OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC OS 12614 / NCIMB 9131 / NCTC 9757). OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; OC Chromobacteriaceae; Chromobacterium. OX NCBI_TaxID=243365 {ECO:0000313|EMBL:AAQ59697.1, ECO:0000313|Proteomes:UP000001424}; RN [1] {ECO:0000313|EMBL:AAQ59697.1, ECO:0000313|Proteomes:UP000001424} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / RC NCTC 9757 {ECO:0000313|Proteomes:UP000001424}; RX PubMed=14500782; DOI=10.1073/pnas.1832124100; RA Vasconcelos A.T.R., de Almeida D.F., Almeida F.C., de Almeida L.G.P., RA de Almeida R., Goncalves J.A.A., Andrade E.M., Antonio R.V., Araripe J., RA de Araujo M.F.F., Filho S.A., Azevedo V., Batista A.J., Bataus L.A.M., RA Batista J.S., Belo A., vander Berg C., Blamey J., Bogo M., Bonato S., RA Bordignon J., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., RA Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., RA Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Pasa T.B.C., Duran N., RA Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., RA Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., RA Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., RA Grattapaglia D., Grisard E.C., Guimaraes C.T., Hanna E.S., Hungria M., RA Jardim S.N., Laurino J., Leoi L.C.T., Fassarella L., Lima A., RA Loureiro M.F., Lyra M.C.P., Macedo M., Madeira H.M.F., Manfio G.P., RA Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., RA Meissner R.D.V., Menck C.F.M., Moreira M.A.M., Nascimento F.F., RA Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., RA Pedrosa F.O., Pena S.J.D., Perreira J.O., Perreira M., Pinto L.S.R.C., RA Pinto L.S., Porto J.I.R., Potrich D.P., Neto C.E.R., Reis A.M.M., RA Rigo L.U., Rondinelli E., dos Santos E.B.P., Santos F.R., Schneider M.P.C., RA Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., RA Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., RA Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., RA Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.; RT "The complete genome sequence of Chromobacterium violaceum reveals RT remarkable and exploitable bacterial adaptability."; RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003). RN [2] {ECO:0007829|PDB:4A6R, ECO:0007829|PDB:4A6T} RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS), AND PYRIDOXAL PHOSPHATE AT LYS-288. RX PubMed=22268978; DOI=10.1111/j.1742-4658.2012.08468.x; RA Humble M.S., Cassimjee K.E., Hakansson M., Kimbung Y.R., Walse B., RA Abedi V., Federsel H.J., Berglund P., Logan D.T.; RT "Crystal structures of the Chromobacterium violaceumomega-transaminase RT reveal major structural rearrangements upon binding of coenzyme PLP."; RL FEBS J. 279:779-792(2012). RN [3] {ECO:0007829|PDB:4AH3, ECO:0007829|PDB:4BA4} RP X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS), AND PYRIDOXAL PHOSPHATE AT LYS-288. RX PubMed=23519665; DOI=10.1107/S0907444912051670; RA Sayer C., Isupov M.N., Westlake A., Littlechild J.A.; RT "Structural studies of Pseudomonas and Chromobacterium omega- RT aminotransferases provide insights into their differing substrate RT specificity."; RL Acta Crystallogr. D 69:564-576(2013). RN [4] {ECO:0007829|PDB:6S4G} RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS), AND PYRIDOXAL PHOSPHATE AT GLY-120; RP SER-121 AND THR-321. RX PubMed=31740704; DOI=10.1038/s41598-019-53177-3; RA Ruggieri F., Campillo-Brocal J.C., Chen S., Humble M.S., Walse B., RA Logan D.T., Berglund P.; RT "Insight into the dimer dissociation process of the Chromobacterium RT violaceum (S)-selective amine transaminase."; RL Sci. Rep. 9:16946-16946(2019). RN [5] {ECO:0007829|PDB:7Q9X, ECO:0007829|PDB:7Q9Z} RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL RP 5'-PHOSPHATE. RA Isupov M.N., Mitchell D., Sayer C., Littlechild J.A.; RT "Aminotransferase from Chromobacterium violaceum in complex with PLP- RT pyruvate adduct."; RL Submitted (NOV-2021) to the PDB data bank. CC -!- INTERACTION: CC Q7NWG4; Q7NWG4: CV_2025; NbExp=3; IntAct=EBI-7663449, EBI-7663449; CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954, CC ECO:0000256|RuleBase:RU003560}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE016825; AAQ59697.1; -; Genomic_DNA. DR RefSeq; WP_011135573.1; NC_005085.1. DR PDB; 4A6R; X-ray; 1.35 A; A/B=1-459. DR PDB; 4A6T; X-ray; 1.80 A; A/B/C/D=1-459. DR PDB; 4A6U; X-ray; 1.69 A; A/B=1-459. DR PDB; 4A72; X-ray; 2.40 A; A/B/C/D=1-459. DR PDB; 4AH3; X-ray; 1.57 A; A/B/C/D=1-459. DR PDB; 4BA4; X-ray; 1.73 A; A/B=1-459. DR PDB; 4BA5; X-ray; 1.76 A; A/B=1-459. DR PDB; 6S4G; X-ray; 1.67 A; A/B/C/D=1-459. DR PDB; 7Q9X; X-ray; 1.60 A; AAA/BBB/CCC/DDD=1-459. DR PDB; 7Q9Z; X-ray; 1.95 A; AAA/BBB=1-459. DR PDBsum; 4A6R; -. DR PDBsum; 4A6T; -. DR PDBsum; 4A6U; -. DR PDBsum; 4A72; -. DR PDBsum; 4AH3; -. DR PDBsum; 4BA4; -. DR PDBsum; 4BA5; -. DR PDBsum; 6S4G; -. DR AlphaFoldDB; Q7NWG4; -. DR SMR; Q7NWG4; -. DR MINT; Q7NWG4; -. DR STRING; 243365.CV_2025; -. DR GeneID; 66367689; -. DR KEGG; cvi:CV_2025; -. DR eggNOG; COG0161; Bacteria. DR HOGENOM; CLU_016922_4_1_4; -. DR OrthoDB; 3398487at2; -. DR Proteomes; UP000001424; Chromosome. DR GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IEA:UniProtKB-EC. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. 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; PTHR43094; AMINOTRANSFERASE; 1. DR PANTHER; PTHR43094:SF1; 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 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:4A6R, ECO:0007829|PDB:4A6T}; KW Aminotransferase {ECO:0000313|EMBL:AAQ59697.1}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, KW ECO:0000256|RuleBase:RU003560}; KW Reference proteome {ECO:0000313|Proteomes:UP000001424}; KW Transferase {ECO:0000313|EMBL:AAQ59697.1}. FT BINDING 120 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0007829|PDB:4A6T, ECO:0007829|PDB:4A72" FT BINDING 121 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0007829|PDB:4A6T, ECO:0007829|PDB:4A72" FT BINDING 288 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /ligand_note="covalent" FT /evidence="ECO:0007829|PDB:4A6T, ECO:0007829|PDB:4A72" FT BINDING 321 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0007829|PDB:4A6T, ECO:0007829|PDB:4A72" FT MOD_RES 120 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0007829|PDB:6S4G" FT MOD_RES 121 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0007829|PDB:6S4G" FT MOD_RES 321 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0007829|PDB:6S4G" SQ SEQUENCE 459 AA; 51213 MW; 5CD2CC1AF273D260 CRC64; MQKQRTTSQW RELDAAHHLH PFTDTASLNQ AGARVMTRGE GVYLWDSEGN KIIDGMAGLW CVNVGYGRKD FAEAARRQME ELPFYNTFFK TTHPAVVELS SLLAEVTPAG FDRVFYTNSG SESVDTMIRM VRRYWDVQGK PEKKTLIGRW NGYHGSTIGG ASLGGMKYMH EQGDLPIPGM AHIEQPWWYK HGKDMTPDEF GVVAARWLEE KILEIGADKV AAFVGEPIQG AGGVIVPPAT YWPEIERICR KYDVLLVADE VICGFGRTGE WFGHQHFGFQ PDLFTAAKGL SSGYLPIGAV FVGKRVAEGL IAGGDFNHGF TYSGHPVCAA VAHANVAALR DEGIVQRVKD DIGPYMQKRW RETFSRFEHV DDVRGVGMVQ AFTLVKNKAK RELFPDFGEI GTLCRDIFFR NNLIMRACGD HIVSAPPLVM TRAEVDEMLA VAERCLEEFE QTLKARGLA //