(data stored in ACNUC7421 zone)

SWISSPROT: E3J4U1_FRAIE

ID   E3J4U1_FRAIE            Unreviewed;       320 AA.
AC   E3J4U1;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   08-MAY-2019, entry version 51.
DE   RecName: Full=Pantothenate synthetase {ECO:0000256|HAMAP-Rule:MF_00158};
DE            Short=PS {ECO:0000256|HAMAP-Rule:MF_00158};
DE            EC=6.3.2.1 {ECO:0000256|HAMAP-Rule:MF_00158};
DE   AltName: Full=Pantoate--beta-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00158};
DE   AltName: Full=Pantoate-activating enzyme {ECO:0000256|HAMAP-Rule:MF_00158};
GN   Name=panC {ECO:0000256|HAMAP-Rule:MF_00158};
GN   OrderedLocusNames=FraEuI1c_0172 {ECO:0000313|EMBL:ADP78260.1};
OS   Frankia inefficax (strain DSM 45817 / CECT 9037 / EuI1c).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298654 {ECO:0000313|EMBL:ADP78260.1, ECO:0000313|Proteomes:UP000002484};
RN   [1] {ECO:0000313|EMBL:ADP78260.1, ECO:0000313|Proteomes:UP000002484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45817 / CECT 9037 / EuI1c
RC   {ECO:0000313|Proteomes:UP000002484};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Beauchemin N., Sen A., Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.;
RT   "Complete sequence of Frankia sp. EuI1c.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the condensation of pantoate with beta-alanine
CC       in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
CC       {ECO:0000256|HAMAP-Rule:MF_00158, ECO:0000256|SAAS:SAAS00247587}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate +
CC         AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966,
CC         ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00158, ECO:0000256|SAAS:SAAS01125062};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis;
CC       (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00158, ECO:0000256|SAAS:SAAS00094317}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00158,
CC       ECO:0000256|SAAS:SAAS00247581}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00158,
CC       ECO:0000256|SAAS:SAAS00247620}.
CC   -!- MISCELLANEOUS: The reaction proceeds by a bi uni uni bi ping pong
CC       mechanism. {ECO:0000256|HAMAP-Rule:MF_00158}.
CC   -!- SIMILARITY: Belongs to the pantothenate synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00158, ECO:0000256|SAAS:SAAS00921032}.
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DR   EMBL; CP002299; ADP78260.1; -; Genomic_DNA.
DR   STRING; 298654.FraEuI1c_0172; -.
DR   EnsemblBacteria; ADP78260; ADP78260; FraEuI1c_0172.
DR   KEGG; fri:FraEuI1c_0172; -.
DR   eggNOG; ENOG4108IAA; Bacteria.
DR   eggNOG; COG0414; LUCA.
DR   HOGENOM; HOG000175516; -.
DR   KO; K01918; -.
DR   OMA; FVNPSQF; -.
DR   UniPathway; UPA00028; UER00005.
DR   Proteomes; UP000002484; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004592; F:pantoate-beta-alanine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00158; PanC; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR003721; Pantoate_ligase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR21299:SF1; PTHR21299:SF1; 1.
DR   Pfam; PF02569; Pantoate_ligase; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
DR   TIGRFAMs; TIGR00018; panC; 1.
PE   3: Inferred from homology;
DR   PRODOM; E3J4U1.
DR   SWISS-2DPAGE; E3J4U1.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00158,
KW   ECO:0000256|SAAS:SAAS00464754};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002484};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00158,
KW   ECO:0000256|SAAS:SAAS00247608};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00158,
KW   ECO:0000256|SAAS:SAAS00464803, ECO:0000313|EMBL:ADP78260.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00158,
KW   ECO:0000256|SAAS:SAAS00464749};
KW   Pantothenate biosynthesis {ECO:0000256|HAMAP-Rule:MF_00158,
KW   ECO:0000256|SAAS:SAAS00464740};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002484}.
FT   NP_BIND      63     70       ATP. {ECO:0000256|HAMAP-Rule:MF_00158}.
FT   NP_BIND     178    181       ATP. {ECO:0000256|HAMAP-Rule:MF_00158}.
FT   NP_BIND     215    218       ATP. {ECO:0000256|HAMAP-Rule:MF_00158}.
FT   ACT_SITE     70     70       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00158}.
FT   BINDING      94     94       Beta-alanine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00158}.
FT   BINDING      94     94       Pantoate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00158}.
FT   BINDING     184    184       Pantoate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00158}.
FT   BINDING     207    207       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00158}.
SQ   SEQUENCE   320 AA;  33706 MW;  C41285DB070A7773 CRC64;
     MRWGYSRPDV RYRREDWNGP MPYAPTAQPV PGARLRPVVA RTRPELARVL AEPAGTRAVV
     MTMGALHDGH AALIREARRR ADQVVVTIYV NPLQFGPTED LDRYPRSFDA DLEVCAREGA
     DVVFAPAVIH DPRPLVTLHA GPLGEILEGA SRPGHFDGML TVVATLLHLV RPDLAFFGRK
     DAQQLVCIRR MVADLAFPVT VVGVPTVREP DGLALSSRNT YLTTPQRAAA LALSRALAAG
     VAAADGGTDA TLAAARAVLA GETGVEVDYL ALASPDNLGP VGAAGGPALL LVAARVGSTR
     LIDNIELTVA PAPGPGAGEP
//

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