HAL3A_ARATH
ID HAL3A_ARATH Reviewed; 209 AA.
AC Q9SWE5; Q6ID92;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Phosphopantothenoylcysteine decarboxylase {ECO:0000303|PubMed:11279129};
DE Short=PPCDC {ECO:0000305};
DE EC=4.1.1.36 {ECO:0000269|PubMed:11279129, ECO:0000269|PubMed:11923307};
DE AltName: Full=AtCoaC1 {ECO:0000303|PubMed:12860978};
DE AltName: Full=Halotolerance protein Hal3a {ECO:0000303|PubMed:10652125};
DE Short=AtHal3a {ECO:0000303|PubMed:10652125};
GN Name=HAL3A {ECO:0000303|PubMed:10652125};
GN Synonyms=COAC1 {ECO:0000303|PubMed:12860978}; OrderedLocusNames=At3g18030;
GN ORFNames=MBG14.2;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10652125; DOI=10.1046/j.1365-313x.1999.00626.x;
RA Espinosa-Ruiz A., Belles J.M., Serrano R., Culianez-Macia F.A.;
RT "Arabidopsis thaliana AtHAL3: a flavoprotein related to salt and osmotic
RT tolerance and plant growth.";
RL Plant J. 20:529-539(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF HIS-90.
RX PubMed=11279129; DOI=10.1074/jbc.m100776200;
RA Kupke T., Hernandez-Acosta P., Steinbacher S., Culianez-Macia F.A.;
RT "Arabidopsis thaliana flavoprotein AtHAL3a catalyzes the decarboxylation of
RT 4'-Phosphopantothenoylcysteine to 4'-phosphopantetheine, a key step in
RT coenzyme A biosynthesis.";
RL J. Biol. Chem. 276:19190-19196(2001).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF VAL-30; ILE-33; LYS-34;
RP ARG-95; ASN-142; MET-145; ALA-174; CYS-175; ASP-177; GLY-179 AND GLY-181.
RX PubMed=11923307; DOI=10.1074/jbc.m201557200;
RA Hernandez-Acosta P., Schmid D.G., Jung G., Culianez-Macia F.A., Kupke T.;
RT "Molecular characterization of the Arabidopsis thaliana flavoprotein
RT AtHAL3a reveals the general reaction mechanism of 4'-
RT phosphopantothenoylcysteine decarboxylases.";
RL J. Biol. Chem. 277:20490-20498(2002).
RN [8]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=12860978; DOI=10.1074/jbc.m306321200;
RA Kupke T., Hernandez-Acosta P., Culianez-Macia F.A.;
RT "4'-phosphopantetheine and coenzyme A biosynthesis in plants.";
RL J. Biol. Chem. 278:38229-38237(2003).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16415216; DOI=10.1104/pp.105.072066;
RA Rubio S., Larson T.R., Gonzalez-Guzman M., Alejandro S., Graham I.A.,
RA Serrano R., Rodriguez P.L.;
RT "An Arabidopsis mutant impaired in coenzyme A biosynthesis is sugar
RT dependent for seedling establishment.";
RL Plant Physiol. 140:830-843(2006).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH FMN, AND COFACTOR.
RX PubMed=10986463; DOI=10.1016/s0969-2126(00)00187-8;
RA Albert A., Martinez-Ripoll M., Espinosa-Ruiz A., Yenush L.,
RA Culianez-Macia F.A., Serrano R.;
RT "The X-ray structure of the FMN-binding protein AtHal3 provides the
RT structural basis for the activity of a regulatory subunit involved in
RT signal transduction.";
RL Structure 8:961-969(2000).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF MUTANT SER-175 IN COMPLEX WITH
RP SUBSTRATE ANALOG AND FMN, COFACTOR, AND ACTIVE SITE.
RX PubMed=12614618; DOI=10.1016/s0022-2836(03)00092-5;
RA Steinbacher S., Hernandez-Acosta P., Bieseler B., Blaesse M., Huber R.,
RA Culianez-Macia F.A., Kupke T.;
RT "Crystal structure of the plant PPC decarboxylase AtHAL3a complexed with an
RT ene-thiol reaction intermediate.";
RL J. Mol. Biol. 327:193-202(2003).
CC -!- FUNCTION: Involved in plant growth, and salt and osmotic tolerance
CC (PubMed:10652125). Catalyzes the decarboxylation of 4'-
CC phosphopantothenoylcysteine to 4'-phosphopantetheine, a key step in
CC coenzyme A biosynthesis (PubMed:11279129, PubMed:11923307,
CC PubMed:12860978, PubMed:16415216). The enzyme is also able to
CC decarboxylate pantothenoylcysteine to pantothenoylcysteamine
CC (PubMed:11923307). {ECO:0000269|PubMed:10652125,
CC ECO:0000269|PubMed:11279129, ECO:0000269|PubMed:11923307,
CC ECO:0000269|PubMed:12860978, ECO:0000269|PubMed:16415216}.
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:0000269|PubMed:11279129, ECO:0000269|PubMed:11923307};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16794;
CC Evidence={ECO:0000269|PubMed:11279129, ECO:0000269|PubMed:11923307};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:10986463, ECO:0000269|PubMed:12614618};
CC Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:10986463,
CC ECO:0000269|PubMed:12614618};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 3/5. {ECO:0000305}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:10986463,
CC ECO:0000269|PubMed:12614618}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots, leaves, flowers,
CC developing siliques and seeds with highest expression in seed embryos
CC and phloem. {ECO:0000269|PubMed:10652125}.
CC -!- INDUCTION: Induced by salt stress. {ECO:0000269|PubMed:10652125}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but homozygous double mutants hal3a-1 and hal3b are
CC embryonic lethal. {ECO:0000269|PubMed:16415216}.
CC -!- SIMILARITY: Belongs to the HFCD (homooligomeric flavin containing Cys
CC decarboxylase) superfamily. {ECO:0000305}.
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; AF166262; AAD51616.1; -; Genomic_DNA.
DR EMBL; AB026641; BAB01331.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76036.1; -; Genomic_DNA.
DR EMBL; BT014781; AAT41764.1; -; mRNA.
DR EMBL; BT015689; AAU29466.1; -; mRNA.
DR EMBL; AK228559; BAF00478.1; -; mRNA.
DR RefSeq; NP_188430.1; NM_112684.5.
DR PDB; 1E20; X-ray; 2.02 A; A=1-209.
DR PDB; 1MVL; X-ray; 2.00 A; A=1-209.
DR PDB; 1MVN; X-ray; 2.21 A; A=1-209.
DR PDBsum; 1E20; -.
DR PDBsum; 1MVL; -.
DR PDBsum; 1MVN; -.
DR AlphaFoldDB; Q9SWE5; -.
DR SMR; Q9SWE5; -.
DR BioGRID; 6660; 1.
DR STRING; 3702.AT3G18030.1; -.
DR PaxDb; Q9SWE5; -.
DR PRIDE; Q9SWE5; -.
DR ProteomicsDB; 247161; -.
DR DNASU; 821327; -.
DR EnsemblPlants; AT3G18030.1; AT3G18030.1; AT3G18030.
DR GeneID; 821327; -.
DR Gramene; AT3G18030.1; AT3G18030.1; AT3G18030.
DR KEGG; ath:AT3G18030; -.
DR Araport; AT3G18030; -.
DR TAIR; locus:2087669; AT3G18030.
DR eggNOG; KOG0672; Eukaryota.
DR HOGENOM; CLU_033319_3_2_1; -.
DR OMA; NTRMYDH; -.
DR OrthoDB; 1225808at2759; -.
DR PhylomeDB; Q9SWE5; -.
DR BRENDA; 4.1.1.36; 399.
DR UniPathway; UPA00241; UER00354.
DR EvolutionaryTrace; Q9SWE5; -.
DR PRO; PR:Q9SWE5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SWE5; baseline and differential.
DR Genevisible; Q9SWE5; AT.
DR GO; GO:0071513; C:phosphopantothenoylcysteine decarboxylase complex; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR GO; GO:0004633; F:phosphopantothenoylcysteine decarboxylase activity; IDA:TAIR.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IMP:CACAO.
DR GO; GO:0042538; P:hyperosmotic salinity response; IMP:TAIR.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1950; -; 1.
DR InterPro; IPR036551; Flavin_trans-like.
DR InterPro; IPR003382; Flavoprotein.
DR Pfam; PF02441; Flavoprotein; 1.
DR SUPFAM; SSF52507; SSF52507; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coenzyme A biosynthesis; Decarboxylase; Flavoprotein; FMN;
KW Growth regulation; Lyase; Reference proteome; Stress response.
FT CHAIN 1..209
FT /note="Phosphopantothenoylcysteine decarboxylase"
FT /id="PRO_0000182032"
FT ACT_SITE 90
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:11279129,
FT ECO:0000269|PubMed:12614618, ECO:0007744|PDB:1MVN"
FT ACT_SITE 175
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:12614618,
FT ECO:0007744|PDB:1MVN"
FT BINDING 28..30
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:10986463,
FT ECO:0000269|PubMed:12614618, ECO:0007744|PDB:1E20,
FT ECO:0007744|PDB:1MVL"
FT BINDING 53..55
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:10986463,
FT ECO:0000269|PubMed:12614618, ECO:0007744|PDB:1E20,
FT ECO:0007744|PDB:1MVL"
FT BINDING 106..109
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:10986463,
FT ECO:0000269|PubMed:12614618, ECO:0007744|PDB:1E20,
FT ECO:0007744|PDB:1MVL"
FT BINDING 140
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:10986463,
FT ECO:0000269|PubMed:12614618, ECO:0007744|PDB:1E20,
FT ECO:0007744|PDB:1MVL"
FT BINDING 142
FT /ligand="N-[(R)-4-phosphopantothenoyl]-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:59458"
FT /evidence="ECO:0000305|PubMed:12614618,
FT ECO:0007744|PDB:1MVN"
FT BINDING 172
FT /ligand="N-[(R)-4-phosphopantothenoyl]-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:59458"
FT /evidence="ECO:0000305|PubMed:12614618,
FT ECO:0007744|PDB:1MVN"
FT BINDING 174
FT /ligand="N-[(R)-4-phosphopantothenoyl]-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:59458"
FT /evidence="ECO:0000305|PubMed:12614618,
FT ECO:0007744|PDB:1MVN"
FT BINDING 183
FT /ligand="N-[(R)-4-phosphopantothenoyl]-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:59458"
FT /evidence="ECO:0000305|PubMed:12614618,
FT ECO:0007744|PDB:1MVN"
FT SITE 175
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000305|PubMed:12614618,
FT ECO:0007744|PDB:1MVN"
FT MUTAGEN 30
FT /note="V->I: No effect on activity."
FT /evidence="ECO:0000269|PubMed:11923307"
FT MUTAGEN 33
FT /note="I->L,V: No effect on activity."
FT /evidence="ECO:0000269|PubMed:11923307"
FT MUTAGEN 34
FT /note="K->N,R: No effect on activity."
FT /evidence="ECO:0000269|PubMed:11923307"
FT MUTAGEN 34
FT /note="K->Q: Small decrease of activity."
FT /evidence="ECO:0000269|PubMed:11923307"
FT MUTAGEN 90
FT /note="H->N: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:11279129"
FT MUTAGEN 95
FT /note="R->Q: Very low activity. Can reduce the oxidied
FT intermediate."
FT /evidence="ECO:0000269|PubMed:11923307"
FT MUTAGEN 142
FT /note="N->D: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:11923307"
FT MUTAGEN 145
FT /note="M->L: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:11923307"
FT MUTAGEN 174
FT /note="A->S: Significantly reduced activity. Can reduce the
FT oxidied intermediate."
FT /evidence="ECO:0000269|PubMed:11923307"
FT MUTAGEN 174
FT /note="A->V: No effect."
FT /evidence="ECO:0000269|PubMed:11923307"
FT MUTAGEN 175
FT /note="C->S: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:11923307"
FT MUTAGEN 177
FT /note="D->N: Very low activity. Can reduce the oxidied
FT intermediate."
FT /evidence="ECO:0000269|PubMed:11923307"
FT MUTAGEN 179
FT /note="G->A: Very low activity. Can reduce the oxidied
FT intermediate."
FT /evidence="ECO:0000269|PubMed:11923307"
FT MUTAGEN 181
FT /note="G->A: Significantly reduced activity."
FT /evidence="ECO:0000269|PubMed:11923307"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:1MVL"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:1MVL"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:1MVL"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:1MVL"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:1MVL"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1MVL"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1MVL"
FT HELIX 76..80
FT /evidence="ECO:0007829|PDB:1MVL"
FT HELIX 89..96
FT /evidence="ECO:0007829|PDB:1MVL"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:1MVL"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:1MVL"
FT HELIX 121..127
FT /evidence="ECO:0007829|PDB:1MVL"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:1MVL"
FT HELIX 143..147
FT /evidence="ECO:0007829|PDB:1MVL"
FT HELIX 149..161
FT /evidence="ECO:0007829|PDB:1MVL"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:1MVN"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:1MVN"
FT HELIX 186..199
FT /evidence="ECO:0007829|PDB:1MVL"
SQ SEQUENCE 209 AA; 23355 MW; 3AB1BB364F8E40DE CRC64;
MENGKRDRQD MEVNTTPRKP RVLLAASGSV AAIKFGNLCH CFTEWAEVRA VVTKSSLHFL
DKLSLPQEVT LYTDEDEWSS WNKIGDPVLH IELRRWADVL VIAPLSANTL GKIAGGLCDN
LLTCIIRAWD YTKPLFVAPA MNTLMWNNPF TERHLLSLDE LGITLIPPIK KRLACGDYGN
GAMAEPSLIY STVRLFWESQ AHQQTGGTS
