ID   E4TX47_SULKY            Unreviewed;       273 AA.
AC   E4TX47;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 68.
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=Sulku_2253 {ECO:0000313|EMBL:ADR34913.1};
OS   Sulfuricurvum kujiense (strain ATCC BAA-921 / DSM 16994 / JCM 11577 /
OS   YK-1).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurimonadaceae; Sulfuricurvum.
OX   NCBI_TaxID=709032 {ECO:0000313|EMBL:ADR34913.1, ECO:0000313|Proteomes:UP000008721};
RN   [1] {ECO:0000313|EMBL:ADR34913.1, ECO:0000313|Proteomes:UP000008721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-921 / DSM 16994 / JCM 11577 / YK-1
RC   {ECO:0000313|Proteomes:UP000008721};
RX   PubMed=22675602; DOI=10.4056/sigs.2456004;
RA   Han C., Kotsyurbenko O., Chertkov O., Held B., Lapidus A., Nolan M.,
RA   Lucas S., Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A.,
RA   Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K.,
RA   Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Brambilla E.M., Rohde M., Spring S.,
RA   Sikorski J., Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT   "Complete genome sequence of the sulfur compounds oxidizing
RT   chemolithoautotroph Sulfuricurvum kujiense type strain (YK-1(T)).";
RL   Stand. Genomic Sci. 6:94-103(2012).
CC   -!- FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in
CC       an ATP-dependent reaction via a pantoyl-adenylate intermediate.
CC       {ECO:0000256|HAMAP-Rule:MF_00158}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP +
CC         diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001155, ECO:0000256|HAMAP-
CC         Rule:MF_00158};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantothenate from (R)-pantoate and beta-alanine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004990, ECO:0000256|HAMAP-Rule:MF_00158}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00158}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00158}.
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|ARBA:ARBA00009256, ECO:0000256|HAMAP-Rule:MF_00158}.
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; CP002355; ADR34913.1; -; Genomic_DNA.
DR   RefSeq; WP_013461110.1; NC_014762.1.
DR   AlphaFoldDB; E4TX47; -.
DR   STRING; 709032.Sulku_2253; -.
DR   KEGG; sku:Sulku_2253; -.
DR   eggNOG; COG0414; Bacteria.
DR   HOGENOM; CLU_047148_0_0_7; -.
DR   OrthoDB; 9773087at2; -.
DR   UniPathway; UPA00028; UER00005.
DR   Proteomes; UP000008721; 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   CDD; cd00560; PanC; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.30.1300.10; Pantoate-beta-alanine ligase, C-terminal domain; 1.
DR   HAMAP; MF_00158; PanC; 1.
DR   InterPro; IPR003721; Pantoate_ligase.
DR   InterPro; IPR042176; Pantoate_ligase_C.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00018; panC; 1.
DR   PANTHER; PTHR21299; CYTIDYLATE KINASE/PANTOATE-BETA-ALANINE LIGASE; 1.
DR   PANTHER; PTHR21299:SF1; PANTOATE--BETA-ALANINE LIGASE; 1.
DR   Pfam; PF02569; Pantoate_ligase; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00158}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00158};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00158};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00158};
KW   Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655,
KW   ECO:0000256|HAMAP-Rule:MF_00158};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008721}.
FT   ACT_SITE        34
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00158"
FT   BINDING         27..34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00158"
FT   BINDING         58
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00158"
FT   BINDING         58
FT                   /ligand="beta-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57966"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00158"
FT   BINDING         144..147
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00158"
FT   BINDING         150
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00158"
FT   BINDING         173
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00158"
FT   BINDING         181..184
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00158"
SQ   SEQUENCE   273 AA;  30121 MW;  9A3C55BB0CDCC725 CRC64;
     MIIARSAQEL KDALETKTGS VGFVPTMGAL HIGHRTLIDA ARKGNDTVVV SIFVNPTQFL
     PGEDLSKYPR REEADFKICS LSGIDILFYP DVNAMYGDDE VRITAPDVRG FILEGASRPG
     HFDGVLTVVM KLFNIVRPTR AYFGKKDAQQ LAMIIQMVNN FFMDVEIVPM ETVRESDGLA
     LSSRNVYLSP SERQEALKLS AALKSATKMV MQGNLSSSDI KTNMESILSP LDVEYVAIVN
     RAFESIEKVV LGNTIILVAA RVGTTRLIDN VWM
//