(data stored in ACNUC7421 zone)

SWISSPROT: A5FTU3_ACICJ

ID   A5FTU3_ACICJ            Unreviewed;       400 AA.
AC   A5FTU3;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 71.
DE   SubName: Full=Serine--glyoxylate transaminase {ECO:0000313|EMBL:ABQ29025.1};
DE            EC=2.6.1.45 {ECO:0000313|EMBL:ABQ29025.1};
GN   OrderedLocusNames=Acry_3418 {ECO:0000313|EMBL:ABQ29025.1};
OS   Acidiphilium cryptum (strain JF-5).
OG   Plasmid pACRY02 {ECO:0000313|EMBL:ABQ29025.1,
OG   ECO:0000313|Proteomes:UP000000245}.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidiphilium.
OX   NCBI_TaxID=349163 {ECO:0000313|EMBL:ABQ29025.1, ECO:0000313|Proteomes:UP000000245};
RN   [1] {ECO:0000313|EMBL:ABQ29025.1, ECO:0000313|Proteomes:UP000000245}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JF-5 {ECO:0000313|Proteomes:UP000000245};
RC   PLASMID=Plasmid pACRY02 {ECO:0000313|Proteomes:UP000000245};
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.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Magnuson T.,
RA   Richardson P.;
RT   "Complete sequence of plasmid2 pACRY02 of Acidiphilium cryptum JF-5.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000524-50,
CC         ECO:0000256|SAAS:SAAS00607652};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|SAAS:SAAS00538721}.
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DR   EMBL; CP000690; ABQ29025.1; -; Genomic_DNA.
DR   EnsemblBacteria; ABQ29025; ABQ29025; Acry_3418.
DR   KEGG; acr:Acry_3418; -.
DR   HOGENOM; HOG000171814; -.
DR   KO; K00830; -.
DR   OMA; CVTGSQK; -.
DR   BioCyc; ACRY349163:GHET-3413-MONOMER; -.
DR   Proteomes; UP000000245; Plasmid pACRY02.
DR   GO; GO:0050281; F:serine-glyoxylate transaminase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000524; SPT; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5FTU3.
DR   SWISS-2DPAGE; A5FTU3.
KW   Aminotransferase {ECO:0000256|SAAS:SAAS00420543,
KW   ECO:0000313|EMBL:ABQ29025.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000245};
KW   Plasmid {ECO:0000313|EMBL:ABQ29025.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000524-50,
KW   ECO:0000256|SAAS:SAAS00420535};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000245};
KW   Transferase {ECO:0000256|SAAS:SAAS00420534,
KW   ECO:0000313|EMBL:ABQ29025.1}.
FT   DOMAIN        7    315       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
FT   MOD_RES     196    196       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR000524-50}.
SQ   SEQUENCE   400 AA;  43363 MW;  1D921F6189851ACB CRC64;
     MHTGRHFLQI PGPTNVPDRV LRAIDMPTID HRGPEFGRLG LEVIEGCKAV FRTGNPVIIY
     PSSGTGAWEA AILNTLSPGD RVLVAETGHF ATLWGRMAAK LKLEVETIPG DWRHGADPGE
     IGARLAEDRG HVIKAVMVVH NETSTGVTSR IPDIRRAIDA ARHPALFLVD TISSLGSIDY
     RHDEWGVDVT VGGSQKGLML PPGLGFNAVS DKALAAARGN SSRRSYWDWH EIIAANADGY
     WPYTPATNLL YGLRESLAML QEEGMDSVFA RHDRHAAATR AAIRAWELEI LCVDPYAYSS
     ALTAVVMPEG HDADRYREVV LNKFDMSLGT GLAKLKGCVF RIGHLGHFND LMLMGTLAGV
     EMGFALAGVP YRKGGVGAAM AVLEHTVPPG KHHMKDEDAA
//

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