(data stored in ACNUC1104 zone)

SWISSPROT: C0ZNL0_RHOE4

ID   C0ZNL0_RHOE4            Unreviewed;       441 AA.
AC   C0ZNL0;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   SubName: Full=Putative cysteine desulfurase {ECO:0000313|EMBL:BAH31262.1};
DE            EC=2.8.1.7 {ECO:0000313|EMBL:BAH31262.1};
GN   OrderedLocusNames=RER_05540 {ECO:0000313|EMBL:BAH31262.1};
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH31262.1, ECO:0000313|Proteomes:UP000002204};
RN   [1] {ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAH31262.1, ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX   PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA   Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA   Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA   Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT   "Sequence analysis of three plasmids harboured in Rhodococcus
RT   erythropolis strain PR4.";
RL   Environ. Microbiol. 8:334-346(2006).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU004504,
CC         ECO:0000256|SAAS:SAAS00608357};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU004075,
CC       ECO:0000256|SAAS:SAAS00544146}.
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DR   EMBL; AP008957; BAH31262.1; -; Genomic_DNA.
DR   RefSeq; WP_020906016.1; NC_012490.1.
DR   STRING; 234621.RER_05540; -.
DR   EnsemblBacteria; BAH31262; BAH31262; RER_05540.
DR   KEGG; rer:RER_05540; -.
DR   PATRIC; fig|234621.6.peg.998; -.
DR   eggNOG; ENOG4105C9B; Bacteria.
DR   eggNOG; COG0520; LUCA.
DR   HOGENOM; HOG000017511; -.
DR   OMA; ETRAGCS; -.
DR   BioCyc; RERY234621:GHDE-571-MONOMER; -.
DR   Proteomes; UP000002204; Chromosome.
DR   GO; GO:0031071; F:cysteine desulfurase 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; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
DR   PRODOM; C0ZNL0.
DR   SWISS-2DPAGE; C0ZNL0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002204};
KW   Pyridoxal phosphate {ECO:0000256|SAAS:SAAS00427524};
KW   Transferase {ECO:0000313|EMBL:BAH31262.1}.
FT   DOMAIN       38    395       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
SQ   SEQUENCE   441 AA;  46337 MW;  FB0ED9F9BDFA592D CRC64;
     MTAVLSADTC RTTAIAKVSG ADLQVPLVQG GECSYANFDY AASAPALAQV TDRIAELLPT
     YASVHRGAGY ASRISTLTYE NARESVARFV NCADDQVVVF TRNTTDSLNL LAQCVPGSTV
     VLDVEHHANL LPWNDARIVT AADTIEETIE RLIGELCTKP AALLAITGAS NVTGEILPIA
     RLADIAHRCG ARILVDAAQL APHRRIDLQE CGVDYIAFSG HKLYAPFGAG VLVGRRDWLD
     EAQPYLAGGG AVREVTIEST EWACAPARHE AGSPNVLGAA AIATACETLH ALDFDVIAEH
     EKALTAQLTD GLSAIESVSL VRLWNDAPDA VGIVTFTVDG FEAGEIAAFL SAEHGIGVRD
     GRFCAHPVLA RLGLSGGAVR ASLGLGSSSD DVTRLVDAVN ILVSNQRDWN YAKTAGAWNP
     VPETRPFLGA ADDNAGAAEC V
//

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