ID   C3NMB8_SULIN            Unreviewed;       266 AA.
AC   C3NMB8;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=4-phosphopantoate--beta-alanine ligase {ECO:0000256|HAMAP-Rule:MF_02224};
DE            EC=6.3.2.36 {ECO:0000256|HAMAP-Rule:MF_02224};
DE   AltName: Full=Phosphopantothenate synthetase {ECO:0000256|HAMAP-Rule:MF_02224};
DE            Short=PPS {ECO:0000256|HAMAP-Rule:MF_02224};
GN   OrderedLocusNames=YN1551_2796 {ECO:0000313|EMBL:ACP49700.1};
OS   Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=419942 {ECO:0000313|EMBL:ACP49700.1, ECO:0000313|Proteomes:UP000006818};
RN   [1] {ECO:0000313|EMBL:ACP49700.1, ECO:0000313|Proteomes:UP000006818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y.N.15.51 / Yellowstone #2 {ECO:0000313|Proteomes:UP000006818};
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC   -!- FUNCTION: Catalyzes the condensation of (R)-4-phosphopantoate and beta-
CC       alanine to 4'-phosphopantothenate in the CoA biosynthesis pathway.
CC       {ECO:0000256|HAMAP-Rule:MF_02224}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-4-phosphopantoate + ATP + beta-alanine = (R)-4'-
CC         phosphopantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:27930,
CC         ChEBI:CHEBI:10986, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:61294,
CC         ChEBI:CHEBI:456215; EC=6.3.2.36; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02224};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02224}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02224}.
CC   -!- SIMILARITY: Belongs to the archaeal phosphopantothenate synthetase
CC       family. {ECO:0000256|HAMAP-Rule:MF_02224}.
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DR   EMBL; CP001404; ACP49700.1; -; Genomic_DNA.
DR   RefSeq; WP_012712859.1; NC_012623.1.
DR   AlphaFoldDB; C3NMB8; -.
DR   GeneID; 8760034; -.
DR   KEGG; sin:YN1551_2796; -.
DR   HOGENOM; CLU_078701_0_0_2; -.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000006818; Chromosome.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.12640; Phosphopantoate/pantothenate synthetase; 1.
DR   HAMAP; MF_02224; PPS; 1.
DR   InterPro; IPR002855; PPS/PS.
DR   InterPro; IPR038138; PPS/PS_sf.
DR   NCBIfam; NF041123; phpantohe_syn_Arch; 1.
DR   PANTHER; PTHR40695; 4-PHOSPHOPANTOATE--BETA-ALANINE LIGASE; 1.
DR   PANTHER; PTHR40695:SF1; 4-PHOSPHOPANTOATE--BETA-ALANINE LIGASE; 1.
DR   Pfam; PF02006; PPS_PS; 1.
DR   PIRSF; PIRSF004853; UCP004853; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_02224};
KW   Coenzyme A biosynthesis {ECO:0000256|ARBA:ARBA00022993, ECO:0000256|HAMAP-
KW   Rule:MF_02224}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02224};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_02224}.
FT   COILED          217..245
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         29
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02224"
FT   BINDING         51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02224"
FT   BINDING         194..196
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02224"
FT   BINDING         200..201
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02224"
FT   BINDING         212..213
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02224"
SQ   SEQUENCE   266 AA;  29594 MW;  8EA8BAC149790405 CRC64;
     MDKAQDSKSW SIRDIIPENH PRRESLLIRE KLIEAMGKSI LVPQGLIAHG RGECFDYLIG
     EKTQNFAEKA IEAAAATLLL AKTPVISING NMAALVPEGL VRLAEETNAK LEVNLFYRDE
     RREKVIAEVL YKANAKEVLG VGEDASTVIP ELFSQRRRVS PKGIYIADVV LLGLEDGDRT
     EALVKMGKKV IAIDINPLSR TSRTATITIV DNIIRAVPRL VEKAKELKSK NKEELEQIVL
     NYNNKNVLAE SLKFIANRLT QLSLSL
//