ID Q160B4_ROSDO Unreviewed; 413 AA.
AC Q160B4;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Aminotransferase, putative {ECO:0000313|EMBL:ABG33679.1};
GN OrderedLocusNames=RD1_4244 {ECO:0000313|EMBL:ABG33679.1};
OS Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS (strain OCh 114)) (Roseobacter denitrificans).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=375451 {ECO:0000313|EMBL:ABG33679.1, ECO:0000313|Proteomes:UP000007029};
RN [1] {ECO:0000313|EMBL:ABG33679.1, ECO:0000313|Proteomes:UP000007029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33942 / OCh 114 {ECO:0000313|Proteomes:UP000007029};
RX PubMed=17098896; DOI=10.1128/JB.01390-06;
RA Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA O'huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA Touchman J.W.;
RT "The complete genome sequence of Roseobacter denitrificans reveals a
RT mixotrophic rather than photosynthetic metabolism.";
RL J. Bacteriol. 189:683-690(2007).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000524-50};
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DR EMBL; CP000362; ABG33679.1; -; Genomic_DNA.
DR RefSeq; WP_011570289.1; NZ_FOOO01000027.1.
DR AlphaFoldDB; Q160B4; -.
DR STRING; 375451.RD1_4244; -.
DR KEGG; rde:RD1_4244; -.
DR eggNOG; COG0075; Bacteria.
DR HOGENOM; CLU_672349_0_0_5; -.
DR OrthoDB; 389074at2; -.
DR Proteomes; UP000007029; Chromosome.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR PANTHER; PTHR42778; 2-AMINOETHYLPHOSPHONATE--PYRUVATE TRANSAMINASE; 1.
DR PANTHER; PTHR42778:SF1; 2-AMINOETHYLPHOSPHONATE--PYRUVATE TRANSAMINASE; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Aminotransferase {ECO:0000313|EMBL:ABG33679.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000007029};
KW Transferase {ECO:0000313|EMBL:ABG33679.1}.
FT DOMAIN 123..196
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT MOD_RES 215
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 413 AA; 44246 MW; 817110A8837AF706 CRC64;
MTQIFPKLDI PQTIAAGPGP GNTDERVLAA YAGAGLADHM HGDVLRGMVE CKKMLRAVWG
TENIHTYGVA GTGWSGLDVM FSGVMPGDKV VIFTNGTFSG IDGLTVRMKA ATKDELAADS
LNPQAASVVT IEVPHGQSVT GDIIEAALAE HKPKWAAMAH WETGSGRIND IAGFSAACEK
HGAMGLVDAV SSLGVGDFRI DDFPGIHGWA SCPQKGICCL PLTYAPVSFT DRFIETLKAT
GTRTFVHHPI LEARHWGIID GKDVEKGTYH RTHSAYAVAA FHEALRITLE QGVSARAEEY
AFHESALRAA VEAMGCKVTS NMTSLIVLNL PDDLAGREME LVQSCRAQNF GIWPTLSEPV
QVRIGILNLL NRATITDIAH RFAQAIRDMG GKIEQSSVDN ALNTVYAKAI AAE
//
