(data stored in SCRATCH zone)

SWISSPROT: B4STE6_STRM5

ID   B4STE6_STRM5            Unreviewed;       420 AA.
AC   B4STE6;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 54.
DE   RecName: Full=Coenzyme A biosynthesis bifunctional protein CoaBC {ECO:0000256|RuleBase:RU364078};
DE            EC=4.1.1.36 {ECO:0000256|RuleBase:RU364078};
DE            EC=6.3.2.5 {ECO:0000256|RuleBase:RU364078};
DE   AltName: Full=DNA/pantothenate metabolism flavoprotein {ECO:0000256|RuleBase:RU364078};
GN   OrderedLocusNames=Smal_0284 {ECO:0000313|EMBL:ACF49989.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF49989.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49989.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49989.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes two steps in the biosynthesis of coenzyme A.
CC       In the first step cysteine is conjugated to 4'-phosphopantothenate
CC       to form 4-phosphopantothenoylcysteine, in the latter compound is
CC       decarboxylated to form 4'-phosphopantotheine.
CC       {ECO:0000256|RuleBase:RU364078}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-4'-phosphopantothenate + CTP + L-cysteine = CMP +
CC         diphosphate + H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine;
CC         Xref=Rhea:RHEA:19397, ChEBI:CHEBI:10986, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:35235, ChEBI:CHEBI:37563,
CC         ChEBI:CHEBI:59458, ChEBI:CHEBI:60377; EC=6.3.2.5;
CC         Evidence={ECO:0000256|RuleBase:RU364078};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine = CO2 +
CC         D-pantetheine 4'-phosphate; Xref=Rhea:RHEA:16793,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:59458,
CC         ChEBI:CHEBI:61723; EC=4.1.1.36;
CC         Evidence={ECO:0000256|RuleBase:RU364078};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|RuleBase:RU364078};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
CC       (R)-pantothenate: step 2/5. {ECO:0000256|RuleBase:RU364078}.
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
CC       (R)-pantothenate: step 3/5. {ECO:0000256|RuleBase:RU364078}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the PPC
CC       synthetase family. {ECO:0000256|RuleBase:RU364078}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the HFCD (homo-
CC       oligomeric flavin containing Cys decarboxylase) superfamily.
CC       {ECO:0000256|RuleBase:RU364078}.
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DR   EMBL; CP001111; ACF49989.1; -; Genomic_DNA.
DR   RefSeq; WP_012509815.1; NC_011071.1.
DR   STRING; 391008.Smal_0284; -.
DR   EnsemblBacteria; ACF49989; ACF49989; Smal_0284.
DR   KEGG; smt:Smal_0284; -.
DR   eggNOG; ENOG4105CJS; Bacteria.
DR   eggNOG; COG0452; LUCA.
DR   HOGENOM; HOG000037526; -.
DR   KO; K13038; -.
DR   OMA; LDMIVAN; -.
DR   OrthoDB; 1346419at2; -.
DR   BioCyc; SMAL391008:SMAL_RS01440-MONOMER; -.
DR   UniPathway; UPA00241; UER00353.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0004632; F:phosphopantothenate--cysteine ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004633; F:phosphopantothenoylcysteine decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0015941; P:pantothenate catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.10300; -; 1.
DR   Gene3D; 3.40.50.1950; -; 1.
DR   InterPro; IPR035929; CoaB-like_sf.
DR   InterPro; IPR005252; CoaBC.
DR   InterPro; IPR007085; DNA/pantothenate-metab_flavo_C.
DR   InterPro; IPR036551; Flavin_trans-like.
DR   InterPro; IPR003382; Flavoprotein.
DR   Pfam; PF04127; DFP; 1.
DR   Pfam; PF02441; Flavoprotein; 1.
DR   SUPFAM; SSF102645; SSF102645; 1.
DR   SUPFAM; SSF52507; SSF52507; 1.
DR   TIGRFAMs; TIGR00521; coaBC_dfp; 1.
PE   3: Inferred from homology;
DR   PRODOM; B4STE6.
DR   SWISS-2DPAGE; B4STE6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Decarboxylase {ECO:0000256|RuleBase:RU364078};
KW   Flavoprotein {ECO:0000256|RuleBase:RU364078};
KW   FMN {ECO:0000256|RuleBase:RU364078};
KW   Ligase {ECO:0000256|RuleBase:RU364078, ECO:0000313|EMBL:ACF49989.1};
KW   Lyase {ECO:0000256|RuleBase:RU364078, ECO:0000313|EMBL:ACF49989.1}.
FT   DOMAIN       19    188       Flavoprotein. {ECO:0000259|Pfam:PF02441}.
FT   DOMAIN      206    388       DFP. {ECO:0000259|Pfam:PF04127}.
SQ   SEQUENCE   420 AA;  43876 MW;  AFA0C895A63C8B99 CRC64;
     MADSPNASPA PARALEGQKL LLCVGGGIAA YKALELVRRL RDAGAQVQVA MTAGAQQFVT
     PLSFQALSGQ PTRTTLWDSA AEQAMGHIEL ARWADRIVVA PGTADLLARL AQGHADDLVS
     TLCLASTAPL TICPAMNHRM WLHPATQANI ALLRQRGAQV IGPVDGPLAE GESGPGRLAE
     PGDIVAALAA NGSAEAPAAA PETRALQGLR LLISAGPTYE DIDPVRYVGN RSSGKMGFAL
     AAAAAALGAQ VVLVSGPVQL PTPQGVQRID VRSAAQMRDA VLKSLPADIY IGAAAVSDYT
     PRQVAPQKLK KTADSQSLVI ELVRTPDILA EVAAQTQSLK LVVGFAAETH DVEKYARGKL
     VDKRLDLVIA NQVGISGGGF ESDNNAATAF WQDGEQVFPA TSKRELAEQL LALIARRLQA
//

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