(data stored in ACNUC7421 zone)

SWISSPROT: C8W3U0_DESAS

ID   C8W3U0_DESAS            Unreviewed;       281 AA.
AC   C8W3U0;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 64.
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=Dtox_0241 {ECO:0000313|EMBL:ACV61194.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61194.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61194.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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; CP001720; ACV61194.1; -; Genomic_DNA.
DR   RefSeq; WP_015755915.1; NC_013216.1.
DR   STRING; 485916.Dtox_0241; -.
DR   EnsemblBacteria; ACV61194; ACV61194; Dtox_0241.
DR   KEGG; dae:Dtox_0241; -.
DR   eggNOG; ENOG4108IAA; Bacteria.
DR   eggNOG; COG0414; LUCA.
DR   HOGENOM; HOG000175517; -.
DR   KO; K01918; -.
DR   OMA; FVNPSQF; -.
DR   OrthoDB; 1661843at2; -.
DR   BioCyc; DACE485916:G1GFV-246-MONOMER; -.
DR   UniPathway; UPA00028; UER00005.
DR   Proteomes; UP000002217; 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; -; 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; C8W3U0.
DR   SWISS-2DPAGE; C8W3U0.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00158,
KW   ECO:0000256|SAAS:SAAS00464754};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
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:ACV61194.1};
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:UP000002217}.
FT   NP_BIND      30     37       ATP. {ECO:0000256|HAMAP-Rule:MF_00158}.
FT   NP_BIND     147    150       ATP. {ECO:0000256|HAMAP-Rule:MF_00158}.
FT   NP_BIND     184    187       ATP. {ECO:0000256|HAMAP-Rule:MF_00158}.
FT   ACT_SITE     37     37       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00158}.
FT   BINDING      61     61       Beta-alanine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00158}.
FT   BINDING      61     61       Pantoate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00158}.
FT   BINDING     153    153       Pantoate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00158}.
FT   BINDING     176    176       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00158}.
SQ   SEQUENCE   281 AA;  31183 MW;  099FCA2A53011E2E CRC64;
     MKTIKTIAEA KKFLKQARLQ GLTIGLVPTM GYLHEGHLTL MRECKKKCDL TVVSIFVNPL
     QFGPKEDFSG YPRDLGRDSS LAEGVGVDLL FCPEPQEVYP ANYSTYVDVE GLTGVLCGKS
     RPGHFRGVTT VVNKLFNIVR PDYAFFGQKD AQQVLVIKKM VRDLLMDLEI ITVPIVRESD
     GLALSSRNVY LSREERRAAL VLSLSLIMAR DAVKSGENNV ALLKDRVRQM ISAEPLARID
     YVEILSLPDL AEINSLEAPA LLALAVFFGK TRLIDNVVLE S
//

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