PPCS2_ARATH
ID PPCS2_ARATH Reviewed; 309 AA.
AC Q9LZM3; F4KAZ0;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Phosphopantothenate--cysteine ligase 2;
DE EC=6.3.2.5;
DE AltName: Full=Phosphopantothenoylcysteine synthetase 2;
DE Short=PPC synthetase 2;
GN Name=PPCS2; Synonyms=COAB2; OrderedLocusNames=At5g02080;
GN ORFNames=T7H20.130;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
CC -!- FUNCTION: Catalyzes the first step in the biosynthesis of coenzyme A
CC from vitamin B5, where cysteine is conjugated to 4'-phosphopantothenate
CC to form 4-phosphopantothenoylcysteine. {ECO:0000250}.
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 -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 2/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PPC synthetase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AED90429.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AED90429.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB82981.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB82981.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL162508; CAB82981.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90429.1; ALT_SEQ; Genomic_DNA.
DR PIR; T48229; T48229.
DR RefSeq; NP_195828.1; NM_120286.2.
DR AlphaFoldDB; Q9LZM3; -.
DR SMR; Q9LZM3; -.
DR STRING; 3702.AT5G02080.1; -.
DR PeptideAtlas; Q9LZM3; -.
DR PRIDE; Q9LZM3; -.
DR GeneID; 831921; -.
DR KEGG; ath:AT5G02080; -.
DR Araport; AT5G02080; -.
DR eggNOG; KOG2728; Eukaryota.
DR InParanoid; Q9LZM3; -.
DR PhylomeDB; Q9LZM3; -.
DR UniPathway; UPA00241; UER00353.
DR PRO; PR:Q9LZM3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZM3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004632; F:phosphopantothenate--cysteine ligase activity; IBA:GO_Central.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.10300; -; 1.
DR InterPro; IPR035929; CoaB-like_sf.
DR InterPro; IPR007085; DNA/pantothenate-metab_flavo_C.
DR Pfam; PF04127; DFP; 2.
DR SUPFAM; SSF102645; SSF102645; 1.
PE 2: Evidence at transcript level;
KW Coenzyme A biosynthesis; Ligase; Reference proteome.
FT CHAIN 1..309
FT /note="Phosphopantothenate--cysteine ligase 2"
FT /id="PRO_0000398832"
SQ SEQUENCE 309 AA; 34824 MW; BCE4B734242B1E4A CRC64;
MEDEISSFFE SSPPQKNMEE ILENLNEFIK LNSSSQGGRR IVCVTSGGTT VPLEQRCVRY
IDNFSSGNRG AASTENFVKA GYAVIFLYRR GTCQPYCRSL PDDPFLECFE FSDKTNIQVH
TSHLEAVKMA VMDQQTAVAE GSLLKLPFST IYEYLQMLRL IAEALKDVGP CSMFYLAAAV
SDFYVPWKSM TEHKIESGSG PLDIRLAQVP KMLSVLRSNW APKAFCISFK LETDSKILME
KATKALRKYK VHAVVANELS TRKEEVVVVS SSGNVVVRRE CDKPESFVED NLIRLIVDRH
STYIKESHN
