COABC_METJA
ID COABC_METJA Reviewed; 403 AA.
AC Q58323;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Coenzyme A biosynthesis bifunctional protein CoaBC {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000305};
DE AltName: Full=DNA/pantothenate metabolism flavoprotein {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000305};
DE AltName: Full=Phosphopantothenoylcysteine synthetase/decarboxylase {ECO:0000255|HAMAP-Rule:MF_02225};
DE Short=PPCS-PPCDC {ECO:0000255|HAMAP-Rule:MF_02225};
DE Includes:
DE RecName: Full=Phosphopantothenoylcysteine decarboxylase {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000303|PubMed:16371361};
DE Short=PPC decarboxylase {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000303|PubMed:16371361};
DE Short=PPC-DC {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000305};
DE EC=4.1.1.36 {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000269|PubMed:16371361};
DE AltName: Full=CoaC {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000303|PubMed:16371361};
DE Includes:
DE RecName: Full=Phosphopantothenate--cysteine ligase {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000305};
DE EC=6.3.2.5 {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000269|PubMed:16371361};
DE AltName: Full=CoaB {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000303|PubMed:16371361};
DE AltName: Full=Phosphopantothenoylcysteine synthetase {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000303|PubMed:16371361};
DE Short=PPC synthetase {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000303|PubMed:16371361};
DE Short=PPC-S {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000305};
GN Name=coaBC {ECO:0000255|HAMAP-Rule:MF_02225};
GN Synonyms=dfp {ECO:0000303|PubMed:16371361}; OrderedLocusNames=MJ0913;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, SUBUNIT, AND MUTAGENESIS
RP OF HIS-87; HIS-139; ASN-141; GLU-167; GLU-168; ASN-217 AND LYS-310.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=16371361; DOI=10.1074/jbc.m510056200;
RA Kupke T., Schwarz W.;
RT "4'-phosphopantetheine biosynthesis in Archaea.";
RL J. Biol. Chem. 281:5435-5444(2006).
CC -!- FUNCTION: Catalyzes two sequential steps in the biosynthesis of
CC coenzyme A. In the first step cysteine is conjugated to 4'-
CC phosphopantothenate to form 4-phosphopantothenoylcysteine. In the
CC second step the latter compound is decarboxylated to form 4'-
CC phosphopantotheine. {ECO:0000255|HAMAP-Rule:MF_02225,
CC ECO:0000269|PubMed:16371361}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine = (R)-4'-
CC phosphopantetheine + CO2; 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:0000255|HAMAP-Rule:MF_02225,
CC ECO:0000269|PubMed:16371361};
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:0000255|HAMAP-Rule:MF_02225,
CC ECO:0000269|PubMed:16371361};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0ABQ0,
CC ECO:0000255|HAMAP-Rule:MF_02225};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02225,
CC ECO:0000269|PubMed:16371361};
CC Note=Binds 1 FMN per subunit. {ECO:0000250|UniProtKB:P0ABQ0,
CC ECO:0000255|HAMAP-Rule:MF_02225};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000269|PubMed:16371361}.
CC -!- SUBUNIT: Homododecamer. The CoaC domain is responsible for dodecamer
CC formation. {ECO:0000269|PubMed:16371361}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the HFCD (homo-
CC oligomeric flavin containing Cys decarboxylase) superfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PPC synthetase
CC family. {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000305}.
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DR EMBL; L77117; AAB98918.1; -; Genomic_DNA.
DR PIR; A64414; A64414.
DR AlphaFoldDB; Q58323; -.
DR SMR; Q58323; -.
DR STRING; 243232.MJ_0913; -.
DR EnsemblBacteria; AAB98918; AAB98918; MJ_0913.
DR KEGG; mja:MJ_0913; -.
DR eggNOG; arCOG01704; Archaea.
DR HOGENOM; CLU_033319_0_3_2; -.
DR InParanoid; Q58323; -.
DR OMA; LDMIVAN; -.
DR PhylomeDB; Q58323; -.
DR BioCyc; MetaCyc:MON-21896; -.
DR BRENDA; 6.3.2.5; 3260.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0071513; C:phosphopantothenoylcysteine decarboxylase complex; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004632; F:phosphopantothenate--cysteine ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004633; F:phosphopantothenoylcysteine decarboxylase activity; IBA:GO_Central.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central.
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 HAMAP; MF_02225; CoaBC; 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 1: Evidence at protein level;
KW Decarboxylase; Flavoprotein; FMN; Ligase; Lyase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Reference proteome.
FT CHAIN 1..403
FT /note="Coenzyme A biosynthesis bifunctional protein CoaBC"
FT /id="PRO_0000232696"
FT REGION 1..197
FT /note="Phosphopantothenoylcysteine decarboxylase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225"
FT REGION 198..403
FT /note="Phosphopantothenate--cysteine ligase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225"
FT BINDING 285
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225"
FT BINDING 294
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225"
FT BINDING 327
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225"
FT MUTAGEN 87
FT /note="H->A: Loss of PPC decarboxylase activity."
FT /evidence="ECO:0000269|PubMed:16371361"
FT MUTAGEN 87
FT /note="H->N: Strong decrease in PPC decarboxylase
FT activity."
FT /evidence="ECO:0000269|PubMed:16371361"
FT MUTAGEN 139
FT /note="H->A: No change in PPC decarboxylase activity."
FT /evidence="ECO:0000269|PubMed:16371361"
FT MUTAGEN 139
FT /note="H->D,N: Strong decrease in PPC decarboxylase
FT activity."
FT /evidence="ECO:0000269|PubMed:16371361"
FT MUTAGEN 141
FT /note="N->D: No change in PPC decarboxylase activity."
FT /evidence="ECO:0000269|PubMed:16371361"
FT MUTAGEN 167
FT /note="E->A: No change in PPC decarboxylase activity."
FT /evidence="ECO:0000269|PubMed:16371361"
FT MUTAGEN 168
FT /note="E->A,D,K: Strong decrease in PPC decarboxylase
FT activity."
FT /evidence="ECO:0000269|PubMed:16371361"
FT MUTAGEN 217
FT /note="N->H: Shows only residual PPC synthetase activity."
FT /evidence="ECO:0000269|PubMed:16371361"
FT MUTAGEN 310
FT /note="K->Q: Shows very low PPC synthetase activity."
FT /evidence="ECO:0000269|PubMed:16371361"
SQ SEQUENCE 403 AA; 45671 MW; B8B51AA81A115B94 CRC64;
MISEIMHPTK LLKGTKSKLL ENKKILVAVT SSIAAIETPK LMRELIRHGA EVYCIITEET
KKIIGKEALK FGCGNEVYEE ITGDIEHILL YNECDCLLIY PATANIISKI NLGIADNIVN
TTALMFFGNK PIFIVPAMHE NMFNAIKRHI DKLKEKDKIY IISPKFEEGK AKVANIEDVV
KAVIEKIGNN LKKEGNRVLI LNGGTVEFID KVRVISNLSS GKMGVALAEA FCKEGFYVEV
ITAMGLEPPY YIKNHKVLTA KEMLNKAIEL AKDFDIIISS AAISDFTVES FEGKLSSEEE
LILKLKRNPK VLEELRRIYK DKVIIGFKAE YNLDEKELIN RAKERLNKYN LNMIIANDLS
KHYFGDDYIE VYIITKYEVE KISGSKKEIS ERIVEKVKKL VKS
