ID   A0A2N7PM00_9BACT        Unreviewed;       403 AA.
AC   A0A2N7PM00;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   11-DEC-2019, entry version 5.
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:PMP65406.1};
GN   ORFNames=C0190_06770 {ECO:0000313|EMBL:PMP65406.1};
OS   Thermodesulfobacterium geofontis.
OC   Bacteria; Thermodesulfobacteria; Thermodesulfobacteriales;
OC   Thermodesulfobacteriaceae; Thermodesulfobacterium.
OX   NCBI_TaxID=1295609 {ECO:0000313|EMBL:PMP65406.1, ECO:0000313|Proteomes:UP000235460};
RN   [1] {ECO:0000313|EMBL:PMP65406.1, ECO:0000313|Proteomes:UP000235460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZAV-08 {ECO:0000313|EMBL:PMP65406.1};
RA   Wilkins L., Ettinger C.;
RT   "Metagenomic assembled genomes from two thermal pools in the Uzon Caldera,
RT   Kamchatka, Russia.";
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes two steps in the biosynthesis of coenzyme A. In the
CC       first step cysteine is conjugated to 4'-phosphopantothenate to form 4-
CC       phosphopantothenoylcysteine, in the latter compound is decarboxylated
CC       to form 4'-phosphopantotheine. {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 + D-
CC         pantetheine 4'-phosphate; Xref=Rhea:RHEA:16793, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:59458, 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 (R)-
CC       pantothenate: step 2/5. {ECO:0000256|RuleBase:RU364078}.
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC       pantothenate: step 3/5. {ECO:0000256|RuleBase:RU364078}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the PPC synthetase
CC       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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PMP65406.1}.
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DR   EMBL; PNIK01000097; PMP65406.1; -; Genomic_DNA.
DR   UniPathway; UPA00241; UER00353.
DR   Proteomes; UP000235460; Unassembled WGS sequence.
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;
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:PMP65406.1};
KW   Lyase {ECO:0000256|RuleBase:RU364078}.
FT   DOMAIN          9..180
FT                   /note="Flavoprotein"
FT                   /evidence="ECO:0000259|Pfam:PF02441"
FT   DOMAIN          189..372
FT                   /note="DFP"
FT                   /evidence="ECO:0000259|Pfam:PF04127"
SQ   SEQUENCE   403 AA;  45420 MW;  8E41188CD884F0C2 CRC64;
     MYSGSLKNKN ILIGVCGGIA IYKVCNLIRI LKKEEANVKV VLTTGAEKFV SPLLFSSLSE
     NKAYTNEDFF KADGSILHIE LGRYPDLILI LPATASFISK LATGSTSELL LAILLSTKAP
     VYIFPSMNTS MWEHPATQEN IKKLRNYGYF VYEPAEGILA CGEIGRGRLP EVEEIFEVVK
     AHFVEKNLLG KRILITGGPT REYIDEVRFI TNASSGKTAF FLAKEAYYRG AEVHLIWGLD
     TFPYVLPKLN YFSDIPFPKL YFVKTTQEMF EVAKDLFPLC EISIFAGAPC DFKPKMPFKG
     KLKKKEGFTI ELELTIDIAK TLNSYKSEKQ ITIGFALEEE KELVNYGKKE KKEKFFDFLV
     ANPLETVGKD ESDYIIFTPK ESLEFKNLPK SQLAKVLFDL IGS
//