(data stored in SCRATCH zone)

SWISSPROT: Q13DH9_RHOPS

ID   Q13DH9_RHOPS            Unreviewed;       275 AA.
AC   Q13DH9;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 90.
DE   RecName: Full=Sulfur carrier protein FdhD {ECO:0000256|HAMAP-Rule:MF_00187, ECO:0000256|SAAS:SAAS01091386};
GN   Name=fdhD {ECO:0000256|HAMAP-Rule:MF_00187};
GN   OrderedLocusNames=RPD_0622 {ECO:0000313|EMBL:ABE37860.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37860.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37860.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37860.1,
RC   ECO:0000313|Proteomes:UP000001818};
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for formate dehydrogenase (FDH) activity. Acts
CC       as a sulfur carrier protein that transfers sulfur from IscS to the
CC       molybdenum cofactor prior to its insertion into FDH.
CC       {ECO:0000256|HAMAP-Rule:MF_00187}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00187,
CC       ECO:0000256|SAAS:SAAS00093831}.
CC   -!- SIMILARITY: Belongs to the FdhD family. {ECO:0000256|HAMAP-
CC       Rule:MF_00187, ECO:0000256|SAAS:SAAS00573239}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00187}.
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DR   EMBL; CP000283; ABE37860.1; -; Genomic_DNA.
DR   RefSeq; WP_011501047.1; NC_007958.1.
DR   STRING; 316057.RPD_0622; -.
DR   EnsemblBacteria; ABE37860; ABE37860; RPD_0622.
DR   KEGG; rpd:RPD_0622; -.
DR   eggNOG; ENOG4107H9G; Bacteria.
DR   eggNOG; COG1526; LUCA.
DR   HOGENOM; HOG000079468; -.
DR   KO; K02379; -.
DR   OMA; TPGHDVE; -.
DR   OrthoDB; 948173at2; -.
DR   BioCyc; RPAL316057:RPD_RS03190-MONOMER; -.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097163; F:sulfur carrier activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016783; F:sulfurtransferase activity; IEA:InterPro.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00187; FdhD; 1.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   InterPro; IPR003786; FdhD.
DR   PANTHER; PTHR30592; PTHR30592; 1.
DR   Pfam; PF02634; FdhD-NarQ; 1.
DR   PIRSF; PIRSF015626; FdhD; 1.
DR   SUPFAM; SSF53927; SSF53927; 1.
DR   TIGRFAMs; TIGR00129; fdhD_narQ; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13DH9.
DR   SWISS-2DPAGE; Q13DH9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00187,
KW   ECO:0000256|SAAS:SAAS00464188};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|HAMAP-Rule:MF_00187,
KW   ECO:0000256|SAAS:SAAS00512471}.
FT   ACT_SITE    109    109       Cysteine persulfide intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00187}.
SQ   SEQUENCE   275 AA;  28831 MW;  EBC4EA31416D826B CRC64;
     MRPTVQTTTT RTWRNGRMQD GARAIPEETP VAISYNGGTH AVMMATPADL EDFAIGFSLS
     EGVIDTPSQI DTFEIVPLDD GIELRMWIGG AEAERLQQRR RHIAGPTGCG LCGVDSITEA
     LRPAAIVGAG GHFAPEQIIA AIEAMPPLQT LNIETRAVHA AAFWTSARGI VSLREDVGRH
     NALDKLAGAL ARQQIATGDG IVLLTSRVSV EMVQKTAALG APLLVAVSAP TALAVRMAEA
     AGVTLAAIAR ADGFEVFSHP GRISGGTHEE ATDVA
//

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