(data stored in SCRATCH zone)

SWISSPROT: C5B9D3_EDWI9

ID   C5B9D3_EDWI9            Unreviewed;       405 AA.
AC   C5B9D3;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, 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=NT01EI_0053 {ECO:0000313|EMBL:ACR67313.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67313.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACR67313.1, ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|EMBL:ACR67313.1,
RC   ECO:0000313|Proteomes:UP000001485};
RX   PubMed=22247535; DOI=10.1128/JB.06522-11;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Banes M.M.,
RA   Lawrence M.L.;
RT   "Genome Sequence of Edwardsiella ictaluri 93-146, a Strain Associated
RT   with a Natural Channel Catfish Outbreak of Enteric Septicemia of
RT   Catfish.";
RL   J. Bacteriol. 194:740-741(2012).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001600; ACR67313.1; -; Genomic_DNA.
DR   RefSeq; WP_015869537.1; NC_012779.2.
DR   EnsemblBacteria; ACR67313; ACR67313; NT01EI_0053.
DR   GeneID; 7959772; -.
DR   KEGG; eic:NT01EI_0053; -.
DR   PATRIC; fig|634503.3.peg.46; -.
DR   eggNOG; ENOG4105CJS; Bacteria.
DR   eggNOG; COG0452; LUCA.
DR   HOGENOM; HOG000037526; -.
DR   KO; K13038; -.
DR   OMA; LDMIVAN; -.
DR   OrthoDB; 1346419at2; -.
DR   BioCyc; EICT634503:G1GVC-46-MONOMER; -.
DR   UniPathway; UPA00241; UER00353.
DR   Proteomes; UP000001485; 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; C5B9D3.
DR   SWISS-2DPAGE; C5B9D3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
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:ACR67313.1};
KW   Lyase {ECO:0000256|RuleBase:RU364078, ECO:0000313|EMBL:ACR67313.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
FT   DOMAIN        7    179       Flavoprotein. {ECO:0000259|Pfam:PF02441}.
FT   DOMAIN      189    370       DFP. {ECO:0000259|Pfam:PF04127}.
SQ   SEQUENCE   405 AA;  43334 MW;  CC05D39D1629AD26 CRC64;
     MTVLRGKRIL LGISGGIAAY KCPEIVRRLR ERGAEVRVVM TKGAQAFITP LTLQAVSGHP
     VADDLFDPAA EASMGHIELG KWADLVLLAP ATADLMARLA AGMADDLLAT LCLASGAPIA
     IAPAMNQQMF RAAATQDNLA TLTRRGALIW GPDSGEQACG DVGPGRMLDP LTLVSLTEQH
     FSQSQDLAAY RMIITAGPTR EALDPVRFIS NHSSGKMGFA IAEAAARRGA QVTLISGPVA
     LPTPPGVARV DVQSALEMQA AVAQRARDCD IFIACAAVAD YRAQQIAPEK MKKQRSDTLT
     LTLVKNPDIV AGVAAMTEAR PFVVGFAAET QNVEEYARQK LARKGLDLIC ANDVSQDGQG
     FNSDTNALHL FWPQGDTRLP LSSKSRLGCT LINEIVRHYE EKNRR
//

If you have problems or comments...

PBIL Back to PBIL home page