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Database: UniProt
Entry: A8ZX24_DESOH
LinkDB: A8ZX24_DESOH
Original site: A8ZX24_DESOH 
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
//
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