ID I3TJ46_TISMK Unreviewed; 440 AA.
AC I3TJ46;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Omega-amino acid--pyruvate aminotransferase {ECO:0000313|EMBL:AFK52784.1};
GN OrderedLocusNames=TMO_0945 {ECO:0000313|EMBL:AFK52784.1};
OS Tistrella mobilis (strain KA081020-065).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC Geminicoccaceae; Tistrella.
OX NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK52784.1, ECO:0000313|Proteomes:UP000005258};
RN [1] {ECO:0000313|EMBL:AFK52784.1, ECO:0000313|Proteomes:UP000005258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK52784.1,
RC ECO:0000313|Proteomes:UP000005258};
RX PubMed=22458477; DOI=10.1021/ja301735a;
RA Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT agents.";
RL J. Am. Chem. Soc. 134:8625-8632(2012).
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; CP003236; AFK52784.1; -; Genomic_DNA.
DR RefSeq; WP_014744463.1; NC_017956.1.
DR AlphaFoldDB; I3TJ46; -.
DR STRING; 1110502.TMO_0945; -.
DR KEGG; tmo:TMO_0945; -.
DR PATRIC; fig|1110502.3.peg.980; -.
DR eggNOG; COG0161; Bacteria.
DR HOGENOM; CLU_016922_4_3_5; -.
DR Proteomes; UP000005258; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
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 SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:AFK52784.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Pyruvate {ECO:0000313|EMBL:AFK52784.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005258};
KW Transferase {ECO:0000313|EMBL:AFK52784.1}.
SQ SEQUENCE 440 AA; 47980 MW; 5FD43F1C8386053F CRC64;
MARITVPNDL DAHWMPFTAN RQFKAAPRLL VGAKDMYYTS HDGRQVLDGC AGLWCVNAGH
GRDKISEAVA RQISEMDYSP SFQMGHPLSF ELASRLVELA PDGIDHVFYC NSGSEAVDTA
LKMALAYHRI RGEGSRTRLI GRERGYHGVG FGGISVGGIV SNRKHFGTLL SGVDHLRHTH
DPARNAFSWG QPEHGAELAD DLERLVALHD ASTIAAVIVE PIAGSTGVLI PPKGYLKRLR
EICDRHGILL IFDEVICGFG RTGKAFGADS FEVTPDLMTT AKGITNGAVP MGAVFAKKEI
YDTFMTGPEH LIEFFHGYTY SGHPLACAAA LATLDIYAEE KLFDRAANLS EYFGKAAHAL
RDLPNVIDIR NYGMVAAVEL SPRAGEPTKR AYEIFVRAYE QGVLLRFTGD IIAISPPLII
DEAQIDHLYA VLAEAIKATA
//
