(data stored in SCRATCH zone)

SWISSPROT: A8FQ74_SHESH

ID   A8FQ74_SHESH            Unreviewed;       400 AA.
AC   A8FQ74;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   30-AUG-2017, entry version 56.
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=Ssed_0384 {ECO:0000313|EMBL:ABV34997.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34997.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34997.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34997.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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: CTP + (R)-4'-phosphopantothenate + L-cysteine
CC       = CMP + diphosphate + N-((R)-4'-phosphopantothenoyl)-L-cysteine.
CC       {ECO:0000256|RuleBase:RU364078}.
CC   -!- CATALYTIC ACTIVITY: N-((R)-4'-phosphopantothenoyl)-L-cysteine =
CC       pantotheine 4'-phosphate + CO(2). {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; CP000821; ABV34997.1; -; Genomic_DNA.
DR   RefSeq; WP_012140735.1; NC_009831.1.
DR   ProteinModelPortal; A8FQ74; -.
DR   STRING; 425104.Ssed_0384; -.
DR   EnsemblBacteria; ABV34997; ABV34997; Ssed_0384.
DR   KEGG; sse:Ssed_0384; -.
DR   eggNOG; ENOG4105CJS; Bacteria.
DR   eggNOG; COG0452; LUCA.
DR   HOGENOM; HOG000037526; -.
DR   KO; K13038; -.
DR   OMA; VRFIGNH; -.
DR   OrthoDB; POG091H021V; -.
DR   BioCyc; SSED425104:GH7Q-393-MONOMER; -.
DR   UniPathway; UPA00241; UER00353.
DR   Proteomes; UP000002015; 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:InterPro.
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; IPR005252; CoaBC.
DR   InterPro; IPR007085; DNA/pantothenate-metab_flavo_C.
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; A8FQ74.
DR   SWISS-2DPAGE; A8FQ74.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
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:ABV34997.1};
KW   Lyase {ECO:0000256|RuleBase:RU364078, ECO:0000313|EMBL:ABV34997.1}.
FT   DOMAIN        8    180       Flavoprotein. {ECO:0000259|Pfam:PF02441}.
FT   DOMAIN      187    369       DFP. {ECO:0000259|Pfam:PF04127}.
SQ   SEQUENCE   400 AA;  42699 MW;  6B3FD5FECE7762D8 CRC64;
     MNQSLTNKQI LLAIGGGIAA YKSADLIRRL KERGADVRVV MSQSAKEFIT PLTLQALSGY
     PVASDLLDTA AEAAMGHIEL ARWADLVLVA PATANLIARI NAGMADELIT TTCLATESPV
     AICPAMNQQM YRNQATQDNI KNLSERGLTI WGPDSGSQAC GEVGPGRMQE PLEIAMQVEQ
     FFAPKLLSGR SLLLTAGPTR EAIDPVRYIS NHSSGKMGFA LAKAAADMGA NVTLVSGPVN
     LPTPTGVNRV DVESTDDMLN AVMAQVDAHD IFIGCAAVAD YRVADIATDK IKKSATEMQL
     SLVRNPDILA SVASHTPRPF TVGFAAETQD VARYAKDKLI RKKLDMIAAN DVSSPELGFN
     ADSNALKVIW EKGEQDLPAT DKLTLATQLL TLIAKRIDNA
//

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