ID Q6ALV5_DESPS Unreviewed; 400 AA.
AC Q6ALV5;
DT 13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2004, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Related to aminotransferase {ECO:0000313|EMBL:CAG36670.1};
GN OrderedLocusNames=DP1941 {ECO:0000313|EMBL:CAG36670.1};
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439 {ECO:0000313|EMBL:CAG36670.1, ECO:0000313|Proteomes:UP000000602};
RN [1] {ECO:0000313|Proteomes:UP000000602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54 {ECO:0000313|Proteomes:UP000000602};
RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT permanently cold Arctic sediments.";
RL Environ. Microbiol. 6:887-902(2004).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CR522870; CAG36670.1; -; Genomic_DNA.
DR RefSeq; WP_011189182.1; NC_006138.1.
DR AlphaFoldDB; Q6ALV5; -.
DR STRING; 177439.DP1941; -.
DR KEGG; dps:DP1941; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_7_2_7; -.
DR OrthoDB; 9771070at2; -.
DR Proteomes; UP000000602; 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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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:CAG36670.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000000602};
KW Transferase {ECO:0000313|EMBL:CAG36670.1}.
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 186
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 400 AA; 43819 MW; B2815A58875638B9 CRC64;
MPGFEVFGEE EKQQVNEVLD SGVLFRYEFK DQRKGVYKVK EFENKFASYA NSTHGQAVTS
GSAALKVALM GLGVGPGDEV ITQGFTFVAT WEAILEIGAT PVFTEVDETM NMDPADLKKK
ITAKTKCIIP VHMLGAPARI EEIVAIAKAK NIFVLEDSAQ APGARINGKH VGSFGDCGTF
SFDSVKTITT GEGGMIITDN ADLWRTMSEY HDHGHDHLDN PGGRGGDKRR FIGSNYRMME
IQGAIGLAQL GKLDYIVSQH QKHKAILKEA ASAIPGVSFR HIMDEKGDSA SFFSFFLQDK
EHSSRVNEVL RAEGCGAINF AENTWHFYPK WEHLLGAKTC TASGWPFVGG ENRKRFVYDP
AALPQSADLI GRCLVYPIAV KTDEAKLAQM CTALKKAAQV
//
