ID D1B9G3_THEAS Unreviewed; 374 AA.
AC D1B9G3;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=DegT/DnrJ/EryC1/StrS aminotransferase {ECO:0000313|EMBL:ACZ18916.1};
GN OrderedLocusNames=Taci_0680 {ECO:0000313|EMBL:ACZ18916.1};
OS Thermanaerovibrio acidaminovorans (strain ATCC 49978 / DSM 6589 / Su883)
OS (Selenomonas acidaminovorans).
OC Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC Thermanaerovibrio.
OX NCBI_TaxID=525903 {ECO:0000313|EMBL:ACZ18916.1, ECO:0000313|Proteomes:UP000002030};
RN [1] {ECO:0000313|EMBL:ACZ18916.1, ECO:0000313|Proteomes:UP000002030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49978 / DSM 6589 / Su883
RC {ECO:0000313|Proteomes:UP000002030};
RX PubMed=21304665; DOI=10.4056/sigs.40645;
RA Chovatia M., Sikorski J., Schroder M., Lapidus A., Nolan M., Tice H.,
RA Glavina Del Rio T., Copeland A., Cheng J.F., Lucas S., Chen F., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Chain P., Saunders E., Detter J.C., Brettin T., Rohde M.,
RA Goker M., Spring S., Bristow J., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Eisen J.A.;
RT "Complete genome sequence of Thermanaerovibrio acidaminovorans type strain
RT (Su883).";
RL Stand. Genomic Sci. 1:254-261(2009).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CP001818; ACZ18916.1; -; Genomic_DNA.
DR RefSeq; WP_012869432.1; NC_013522.1.
DR RefSeq; YP_003317198.1; NC_013522.1.
DR AlphaFoldDB; D1B9G3; -.
DR STRING; 525903.Taci_0680; -.
DR EnsemblBacteria; ACZ18916; ACZ18916; Taci_0680.
DR KEGG; tai:Taci_0680; -.
DR PATRIC; fig|525903.6.peg.685; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_0_3_0; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000002030; 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:ACZ18916.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000002030};
KW Transferase {ECO:0000313|EMBL:ACZ18916.1}.
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 374 AA; 41621 MW; 4885025AF5FAA0A6 CRC64;
MAFIPYGRQY VDDDDVAAVV KVLRGDWLTQ GPNVADFEEA FAQKVGARFA VSFSNGTAAL
HGAYYAAGVG KGDQVITSPM TFVATANAAR FLGAHVRFVD VDPSTLCMDP DRLQEMVSPR
TKVIAPVSYA GYPVPLDKIT AVARSVGAIV VEDACHALGA SREGGMVGAQ ADMTVFSFHP
VKHITTAEGG MVTTNNEELA RRLRLFRSHG VERDPSRMSR NDGPWYYEMV DLGYNYRLTD
IQCALGLSQL AKLDRFVQAR RRIARRYAEL LKGVPPVGLP PHHPGHSYHL YPIRVPAERR
RDVFEALRRE GVGVQVHYLP VHMHPYYKDL YGIPDDDLPN ALNYYRETIS LPMFPSLEDH
EQDRVVELLS SYLG
//
