(data stored in ACNUC7421 zone)

SWISSPROT: Q5LWD4_RUEPO

ID   Q5LWD4_RUEPO            Unreviewed;       398 AA.
AC   Q5LWD4;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 81.
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   Name=coaBC {ECO:0000313|EMBL:AAV93726.1};
GN   OrderedLocusNames=SPO0408 {ECO:0000313|EMBL:AAV93726.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93726.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93726.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93726.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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; CP000031; AAV93726.1; -; Genomic_DNA.
DR   RefSeq; WP_011046169.1; NC_003911.12.
DR   STRING; 246200.SPO0408; -.
DR   EnsemblBacteria; AAV93726; AAV93726; SPO0408.
DR   KEGG; sil:SPO0408; -.
DR   eggNOG; ENOG4105CJS; Bacteria.
DR   eggNOG; COG0452; LUCA.
DR   HOGENOM; HOG000037526; -.
DR   KO; K13038; -.
DR   OMA; LDMIVAN; -.
DR   OrthoDB; 1346419at2; -.
DR   BioCyc; RPOM246200:G1G48-415-MONOMER; -.
DR   UniPathway; UPA00241; UER00353.
DR   Proteomes; UP000001023; 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; Q5LWD4.
DR   SWISS-2DPAGE; Q5LWD4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
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:AAV93726.1};
KW   Lyase {ECO:0000256|RuleBase:RU364078, ECO:0000313|EMBL:AAV93726.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023}.
FT   DOMAIN        5    177       Flavoprotein. {ECO:0000259|Pfam:PF02441}.
FT   DOMAIN      184    368       DFP. {ECO:0000259|Pfam:PF04127}.
SQ   SEQUENCE   398 AA;  41770 MW;  7278BAA7275EAE30 CRC64;
     MLASKRILLI IGGGIAAYKT LDLIRRLRER GAAVTPVLTG AAEEFVTPLS VSALAGEKVY
     RALFDLTDEA EMGHIQLSRS ADLVVVAPAT ADLMGKMAAG LANDLASTLL MATDTPVLIA
     PAMNVRMWQH PATRRNHAQL AADGIRFIGP NEGDMACGEY GPGRMSEPLE IVAAIEAALG
     DGPLKGKRVL VTSGPTHEPI DPVRYIANRS SGAQGTAVAR ALAALGAEVV FVTGPADVPP
     PDGVEVVRVQ SAREMDAAVD AALPVDAGVF AAAVADWRVA SASDRKLKKS RDGLPVLEFA
     ENPDILKRVS RMEAGRPPLV VGFAAETNDV IENATAKRLR KGCDWIVAND VSPATGIMGG
     SENAVILITG EGAEEWPRMS KEAVADRLAR RIAETLVG
//

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