PPS_METHJ
ID PPS_METHJ Reviewed; 243 AA.
AC Q2FUA9;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=4-phosphopantoate--beta-alanine ligase {ECO:0000255|HAMAP-Rule:MF_02224, ECO:0000305};
DE EC=6.3.2.36 {ECO:0000255|HAMAP-Rule:MF_02224, ECO:0000269|PubMed:23200110};
DE AltName: Full=Phosphopantothenate synthetase {ECO:0000255|HAMAP-Rule:MF_02224, ECO:0000303|PubMed:23200110};
DE Short=PPS {ECO:0000255|HAMAP-Rule:MF_02224, ECO:0000303|PubMed:23200110};
GN OrderedLocusNames=Mhun_0832 {ECO:0000312|EMBL:ABD40584.1};
OS Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS JF-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX NCBI_TaxID=323259;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL Stand. Genomic Sci. 11:2-2(2016).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX PubMed=23200110; DOI=10.1016/j.jbiosc.2012.10.019;
RA Katoh H., Tamaki H., Tokutake Y., Hanada S., Chohnan S.;
RT "Identification of pantoate kinase and phosphopantothenate synthetase from
RT Methanospirillum hungatei.";
RL J. Biosci. Bioeng. 115:372-376(2013).
CC -!- FUNCTION: Catalyzes the condensation of (R)-4-phosphopantoate and beta-
CC alanine to 4'-phosphopantothenate in the CoA biosynthesis pathway.
CC {ECO:0000255|HAMAP-Rule:MF_02224, ECO:0000269|PubMed:23200110}.
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:0000255|HAMAP-
CC Rule:MF_02224, ECO:0000269|PubMed:23200110};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02224, ECO:0000305|PubMed:23200110}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02224}.
CC -!- SIMILARITY: Belongs to the archaeal phosphopantothenate synthetase
CC family. {ECO:0000255|HAMAP-Rule:MF_02224, ECO:0000305}.
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DR EMBL; CP000254; ABD40584.1; -; Genomic_DNA.
DR RefSeq; WP_011447863.1; NC_007796.1.
DR AlphaFoldDB; Q2FUA9; -.
DR SMR; Q2FUA9; -.
DR STRING; 323259.Mhun_0832; -.
DR EnsemblBacteria; ABD40584; ABD40584; Mhun_0832.
DR GeneID; 3922283; -.
DR KEGG; mhu:Mhun_0832; -.
DR eggNOG; arCOG04262; Archaea.
DR HOGENOM; CLU_078701_0_0_2; -.
DR OMA; PKSHPRY; -.
DR OrthoDB; 76877at2157; -.
DR BRENDA; 6.3.2.36; 3282.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000001941; 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; -; 1.
DR HAMAP; MF_02224; PPS; 1.
DR InterPro; IPR002855; PPS/PS.
DR InterPro; IPR038138; PPS/PS_sf.
DR PANTHER; PTHR40695; PTHR40695; 1.
DR Pfam; PF02006; PPS_PS; 1.
DR PIRSF; PIRSF004853; UCP004853; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coenzyme A biosynthesis; Ligase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..243
FT /note="4-phosphopantoate--beta-alanine ligase"
FT /id="PRO_0000448251"
FT BINDING 15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02224"
FT BINDING 37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02224"
FT BINDING 176..178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02224"
FT BINDING 182..183
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02224"
SQ SEQUENCE 243 AA; 26633 MW; EEC500308DF788AF CRC64;
MIPESHPRYK SLITREKLAQ YTKTGIVSLE GLTAHGRGEA FDYLLGEETT ESALRAEKIA
AALLLSANHP VISVNGNTAA LAAKEIAQLQ LASKARVEVN LFHRTDERVQ AISGLLKEHG
ITLVEGTVSR YIPLDHDRGL CHFDGMHSAD VVLVPLEDGD RAQALIDLGK KVIAIDLNPL
SRTSKVATVP VIDEVTRALA NIARFCTELD QDEITGLTRE IHGTGFIRDA LEYIRERLLN
VLD
