(data stored in ACNUC7421 zone)

SWISSPROT: Q13EP0_RHOPS

ID   Q13EP0_RHOPS            Unreviewed;       511 AA.
AC   Q13EP0;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 70.
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=RPD_0209 {ECO:0000313|EMBL:ABE37449.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37449.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37449.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37449.1,
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: 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; CP000283; ABE37449.1; -; Genomic_DNA.
DR   STRING; 316057.RPD_0209; -.
DR   EnsemblBacteria; ABE37449; ABE37449; RPD_0209.
DR   KEGG; rpd:RPD_0209; -.
DR   eggNOG; ENOG4105CJS; Bacteria.
DR   eggNOG; COG0452; LUCA.
DR   HOGENOM; HOG000037526; -.
DR   KO; K13038; -.
DR   OMA; LDMIVAN; -.
DR   UniPathway; UPA00241; UER00353.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.1220.10; -; 1.
DR   Gene3D; 3.40.50.10300; -; 1.
DR   Gene3D; 3.40.50.1950; -; 1.
DR   InterPro; IPR013321; Arc_rbn_hlx_hlx.
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   InterPro; IPR010985; Ribbon_hlx_hlx.
DR   Pfam; PF04127; DFP; 1.
DR   Pfam; PF02441; Flavoprotein; 1.
DR   SUPFAM; SSF102645; SSF102645; 1.
DR   SUPFAM; SSF47598; SSF47598; 1.
DR   SUPFAM; SSF52507; SSF52507; 1.
DR   TIGRFAMs; TIGR00521; coaBC_dfp; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13EP0.
DR   SWISS-2DPAGE; Q13EP0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Decarboxylase {ECO:0000256|RuleBase:RU364078};
KW   DNA-binding {ECO:0000256|SAAS:SAAS00993492};
KW   Flavoprotein {ECO:0000256|RuleBase:RU364078};
KW   FMN {ECO:0000256|RuleBase:RU364078};
KW   Ligase {ECO:0000256|RuleBase:RU364078, ECO:0000313|EMBL:ABE37449.1};
KW   Lyase {ECO:0000256|RuleBase:RU364078, ECO:0000313|EMBL:ABE37449.1}.
FT   DOMAIN      108    276       Flavoprotein. {ECO:0000259|Pfam:PF02441}.
FT   DOMAIN      290    474       DFP. {ECO:0000259|Pfam:PF04127}.
SQ   SEQUENCE   511 AA;  54466 MW;  1D6E217278DEBFD4 CRC64;
     MQCDRAARWH CIHGLLALPA SVNLRVMANL TIRKLDDALK AELRQRAAAN GRSMEDEVRV
     ILRDVCHKRH GFAASFPQPG EDPAAPGKIE PSPGKDEGFP SEPAASVRIT LIVGGGIAAY
     KAMDLIRRLK ERGAEVRVVL TRAAQQFVTP LTASALSHQR CYTDLFDPQS EFDAGHIRLA
     RDCDLIVVAP ATADLMAKIA GGHADDLATA ILLATNRQIL LAPAMNPLMW NNAATRRNVD
     QLKRDGVALV GPNAGEMAER GEAGTGRMAE PIEIAAAAQA FWTPQPQRPL RGRRVLITAG
     PTHEAIDPVR YIANRSSGKQ GYAIAAAAAA AGAEVVLISG PVDLRAPDGV TLTRVESARE
     MLDAVQAALP TDIAIFAAAV ADWRVESEGG QKIKKGAGGP PPLQLTENPD ILATISKRGE
     NRPNLVIGFA AETENLLDNA RAKLARKGCD WIVANDVSPA TGVMGGDRNT VHLLMNTTDA
     VDVESWPLMT KDEVASALVA RIAQTMEVHA P
//

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