(data stored in ACNUC7421 zone)

SWISSPROT: D6ZBT8_SEGRD

ID   D6ZBT8_SEGRD            Unreviewed;       290 AA.
AC   D6ZBT8;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 53.
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=Srot_0428 {ECO:0000313|EMBL:ADG96915.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96915.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96915.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
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}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00158,
CC       ECO:0000256|SAAS:SAAS00573540}.
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; CP001958; ADG96915.1; -; Genomic_DNA.
DR   RefSeq; WP_013137371.1; NC_014168.1.
DR   STRING; 640132.Srot_0428; -.
DR   EnsemblBacteria; ADG96915; ADG96915; Srot_0428.
DR   KEGG; srt:Srot_0428; -.
DR   eggNOG; ENOG4108IAA; Bacteria.
DR   eggNOG; COG0414; LUCA.
DR   HOGENOM; HOG000175516; -.
DR   KO; K01918; -.
DR   OMA; FVNPSQF; -.
DR   OrthoDB; 1661843at2; -.
DR   BioCyc; SROT640132:G1GLH-429-MONOMER; -.
DR   UniPathway; UPA00028; UER00005.
DR   Proteomes; UP000002247; 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; 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; TIGR00018; panC; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6ZBT8.
DR   SWISS-2DPAGE; D6ZBT8.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00158,
KW   ECO:0000256|SAAS:SAAS00464754};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00158,
KW   ECO:0000256|SAAS:SAAS00464734};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00158,
KW   ECO:0000256|SAAS:SAAS00464803, ECO:0000313|EMBL:ADG96915.1};
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:UP000002247}.
FT   NP_BIND      37     44       ATP. {ECO:0000256|HAMAP-Rule:MF_00158}.
FT   NP_BIND     156    159       ATP. {ECO:0000256|HAMAP-Rule:MF_00158}.
FT   NP_BIND     193    196       ATP. {ECO:0000256|HAMAP-Rule:MF_00158}.
FT   ACT_SITE     44     44       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00158}.
FT   BINDING      69     69       Beta-alanine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00158}.
FT   BINDING      69     69       Pantoate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00158}.
FT   BINDING     162    162       Pantoate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00158}.
FT   BINDING     185    185       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00158}.
SQ   SEQUENCE   290 AA;  30989 MW;  D8F4565A27AEC27C CRC64;
     MSLGHTGPVL CHSPQQLREL ADRLRAVGKH IALVPTMGAL HHGHLALVEH AKRLPHATVV
     ASVFVNPLQF GQGEDFERYP RPLAADLEAL RQKKVRVVYT PAPAAMYPLD GGGTQVVPGP
     LADELEGALR PGHFTGVLTV VMKLLAACGA TWAVFGEKDY QQLTLIRQMI RDLDLPVSAI
     GVPTVREEDG LALSSRNVYL SPHERQQAAG LSAALRAGAA EGERGPDAVL GAARATLEGY
     PGLAVDYLEL RDPDLRQCPQ RGPARLLVAA RCGTTRLIDN MPVSLGDGGR
//

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