ID A0A2N7PM00_9BACT Unreviewed; 403 AA. AC A0A2N7PM00; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 23-MAY-2018, entry version 2. 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}; RN [1] {ECO:0000313|EMBL:PMP65406.1} RP NUCLEOTIDE SEQUENCE. 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 RT Caldera, Kamchatka, Russia."; RL Submitted (JAN-2018) 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}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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 Flavoprotein. {ECO:0000259|Pfam:PF02441}. FT DOMAIN 189 372 DFP. {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 //