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}. 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; 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 //