ID B1I5F6_DESAP Unreviewed; 387 AA.
AC B1I5F6;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=DegT/DnrJ/EryC1/StrS aminotransferase {ECO:0000313|EMBL:ACA60266.1};
GN OrderedLocusNames=Daud_1770 {ECO:0000313|EMBL:ACA60266.1};
OS Desulforudis audaxviator (strain MP104C).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforudis.
OX NCBI_TaxID=477974 {ECO:0000313|EMBL:ACA60266.1, ECO:0000313|Proteomes:UP000008544};
RN [1] {ECO:0000313|Proteomes:UP000008544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP104C {ECO:0000313|Proteomes:UP000008544};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F., Land M.L.,
RA Hauser L., Kyrpides N., Ivanova N.N., Richardson P.;
RT "Complete sequence of chromosome of Desulforudis audaxviator MP104C.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACA60266.1, ECO:0000313|Proteomes:UP000008544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP104C {ECO:0000313|EMBL:ACA60266.1,
RC ECO:0000313|Proteomes:UP000008544};
RX PubMed=18845759; DOI=10.1126/science.1155495;
RA Chivian D., Brodie E.L., Alm E.J., Culley D.E., Dehal P.S., Desantis T.Z.,
RA Gihring T.M., Lapidus A., Lin L.H., Lowry S.R., Moser D.P.,
RA Richardson P.M., Southam G., Wanger G., Pratt L.M., Andersen G.L.,
RA Hazen T.C., Brockman F.J., Arkin A.P., Onstott T.C.;
RT "Environmental genomics reveals a single-species ecosystem deep within
RT Earth.";
RL Science 322:275-278(2008).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CP000860; ACA60266.1; -; Genomic_DNA.
DR RefSeq; WP_012302845.1; NC_010424.1.
DR AlphaFoldDB; B1I5F6; -.
DR STRING; 477974.Daud_1770; -.
DR KEGG; dau:Daud_1770; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_0_3_9; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000008544; Chromosome.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR020026; PseC.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR03588; PseC; 1.
DR PANTHER; PTHR30244:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ACA60266.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000008544};
KW Transferase {ECO:0000313|EMBL:ACA60266.1}.
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 182
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 387 AA; 43269 MW; 30E76A27A0C16851 CRC64;
MRFIPYGRQA IDEEDIRSVV EVLRSDRLTQ GPKVAEFEEA LAAYCGARYA VVFSSGTAAL
HGAYFAARVQ PGSEVITSPI TFAATANAAL YLGAKPVFAD IEPDTANIDV TRIENLINKR
TRAIAPVHFA GQPCDMDEIH QIARRHGLYV IEDACHALGA TYKGQRIGSL SDMTVFSFHP
VKHIATGEGG AVLTDNPDFV HKLRMFREHG ITRDAALPGS TNPETEPDPW YYEMQHLGYN
YRLTDIQCAL GISQLKKLDG FLERRREIAR TYDRAFAEVP AIRPPAQKPD RESAYHIYVV
QIDWKAIGRT RREVCALLRQ NGIGTQVHYL PVYRHPYYRS LGYPAGLCPR AEAYYEAALT
LPLFPAMTDE EVQWVIKAVG RLATGTR
//
