ID A8ZX24_DESOH Unreviewed; 402 AA.
AC A8ZX24;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:ABW66880.1};
GN OrderedLocusNames=Dole_1071 {ECO:0000313|EMBL:ABW66880.1};
OS Desulfosudis oleivorans (strain DSM 6200 / JCM 39069 / Hxd3) (Desulfococcus
OS oleovorans).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfosudaceae; Desulfosudis.
OX NCBI_TaxID=96561 {ECO:0000313|EMBL:ABW66880.1, ECO:0000313|Proteomes:UP000008561};
RN [1] {ECO:0000313|EMBL:ABW66880.1, ECO:0000313|Proteomes:UP000008561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6200 / JCM 39069 / Hxd3
RC {ECO:0000313|Proteomes:UP000008561};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Wawrik B.,
RA Richardson P.;
RT "Complete sequence of Desulfococcus oleovorans Hxd3.";
RL Submitted (OCT-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; CP000859; ABW66880.1; -; Genomic_DNA.
DR RefSeq; WP_012174498.1; NC_009943.1.
DR AlphaFoldDB; A8ZX24; -.
DR STRING; 96561.Dole_1071; -.
DR KEGG; dol:Dole_1071; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_0_7; -.
DR OMA; MRTGEMW; -.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000008561; 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; 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:SF112; PUTRESCINE AMINOTRANSFERASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ABW66880.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000008561};
KW Transferase {ECO:0000313|EMBL:ABW66880.1}.
SQ SEQUENCE 402 AA; 43349 MW; 8E0396DA33721EA4 CRC64;
MNKLMADAQQ VFGKGVVENL VAKGLDWVES GREGWVVHDS NGNELIDCYC SSGTYNLGRK
NPAIARALKQ AIHETDQGNF VMISREKAML SEKLARFTPS GLDCCLFTVV RGEAVDAACK
LARGYTGRSE LITVDGGCYG QTGFAMTLSE RADKKDFGSL IPDVQTVPFN DIDAAGRSIT
KKTAAVILEP VQTENNCRTA DKDYLVALRK SCDQTGALLI FDESQTGFGR TGEKFASDYF
GVLPDIMLLG EALGGGMFPF SAMAFTSTVK TFFDAHPLIH LLTFGGHDVG CRVAAAALTE
YDQVQPWQNA KKQGKILSEK LKQLAGSNPK LKSVQGVGLL LSLEFENAEA AEAFCRNAIQ
QGVLVKSGEV AKQSVVIRPP LTITDQDLEK IVTGIEKALS AL
//