ID E1QIZ2_DESB2 Unreviewed; 402 AA.
AC E1QIZ2;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=DegT/DnrJ/EryC1/StrS aminotransferase {ECO:0000313|EMBL:ADK85535.1};
GN OrderedLocusNames=Deba_2171 {ECO:0000313|EMBL:ADK85535.1};
OS Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802
OS / 2st14).
OC Bacteria; Thermodesulfobacteriota; Desulfarculia; Desulfarculales;
OC Desulfarculaceae; Desulfarculus.
OX NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK85535.1, ECO:0000313|Proteomes:UP000009047};
RN [1] {ECO:0000313|EMBL:ADK85535.1, ECO:0000313|Proteomes:UP000009047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802 / 2st14
RC {ECO:0000313|Proteomes:UP000009047};
RX PubMed=21304732; DOI=10.4056/sigs.1243258;
RA Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H.,
RA Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L.,
RA Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G., Pati A.,
RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Han C., Rohde M., Brambilla E., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Land M.;
RT "Complete genome sequence of Desulfarculus baarsii type strain (2st14).";
RL Stand. Genomic Sci. 3:276-284(2010).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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; CP002085; ADK85535.1; -; Genomic_DNA.
DR RefSeq; WP_013258976.1; NC_014365.1.
DR AlphaFoldDB; E1QIZ2; -.
DR STRING; 644282.Deba_2171; -.
DR KEGG; dbr:Deba_2171; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_1_1_7; -.
DR OrthoDB; 9771070at2; -.
DR Proteomes; UP000009047; 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; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF9; PROTEIN RV3402C; 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:ADK85535.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000009047};
KW Transferase {ECO:0000313|EMBL:ADK85535.1}.
FT ACT_SITE 202
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 202
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 402 AA; 43906 MW; 6DE105956DD2504A CRC64;
MKRRLEDLAI FGGPRLFESF RPTGQLSLPD SRVFFKHART IFDQRRLTNN GPLVRMLEER
LALLHQSAHC VSFCNASVAI VLLLRLLGGD DGGNVLMPTF TYPGLPHIAL WAGFKPVFCD
VDQHTHAIDV ASVAANLTPR SVVILAVHQV QSPCQIDELT TLARQRGVAL LFDSVHGLGC
THRGKPIGGF GAAEVFSLHA TKLLNGFEGG YVTTNDDALA AELRSARSFG FQGKDNVVRL
GLNGKLNEIH AALALAALDD LEQTIQANRA RHEAYRRLFA DLPGLNILEY ATNERHNYEL
TIFEMTTAWP LSRDDTLRLL NAENALARPY YSPPLHHSEH CPPGCGDVSL PVAEALATRF
IQMPVGDLVS LADIEALAEL MTFVGANGPT VAARLARDGR PS
//
