ID A4J672_DESRM Unreviewed; 475 AA.
AC A4J672;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Aminotransferase {ECO:0000313|EMBL:ABO50575.1};
DE EC=2.6.1.- {ECO:0000313|EMBL:ABO50575.1};
GN OrderedLocusNames=Dred_2058 {ECO:0000313|EMBL:ABO50575.1};
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO50575.1, ECO:0000313|Proteomes:UP000001556};
RN [1] {ECO:0000313|EMBL:ABO50575.1, ECO:0000313|Proteomes:UP000001556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI-1 {ECO:0000313|EMBL:ABO50575.1,
RC ECO:0000313|Proteomes:UP000001556};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR EMBL; CP000612; ABO50575.1; -; Genomic_DNA.
DR AlphaFoldDB; A4J672; -.
DR STRING; 349161.Dred_2058; -.
DR KEGG; drm:Dred_2058; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_0_9; -.
DR Proteomes; UP000001556; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00610; OAT_like; 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; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF121; BLR3010 PROTEIN; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 4.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ABO50575.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000001556};
KW Transferase {ECO:0000313|EMBL:ABO50575.1}.
SQ SEQUENCE 475 AA; 51788 MW; D7C6B04A12B0C7ED CRC64;
MSHQHCKCGC MAPINLEQAL GLSQGEIKEM HSQYVNASLV TLLSLINFDT PFISAQGVSV
FDDQGNEYLD FLGAYGALNL GHNHPQILDA IQRVKTMPNL LQSSINGITA ALAHNLSHLT
PGNLQRSFFC NSGAEAVEGA LKLARIATGR QKFVHCHNSF HGKTFGALSV TGREKYQQPF
RPLIAPSIGV PFGDLEALQD HLRSRDVAAF IVEPIQGEGG ILEPPKGYLA KAKNLCAQYG
SLIIADEVQT GFGRTGALFA CETEKLVPDI LCLAKSLGGG VMPIGAYITT DEIWRKAYGT
MEKALLHTST FGGNTTACAA ALKTIEVIME QDLCQQAREK GSYFLTHLNN LKEKYPLLKD
VRGRGLMIGL EFQPPERISG KYSLKFTMNV INKLAQAYMG SLVAGELLNK HQIITAYTLN
NPNVIRLEPP LIVTYEQLDR VLDALEEVLS NHTGFFSMVG SGAKNIISKL THTKS
//
