(data stored in SCRATCH zone)

SWISSPROT: C6WGH8_ACTMD

ID   C6WGH8_ACTMD            Unreviewed;       296 AA.
AC   C6WGH8;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 56.
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=Amir_0325 {ECO:0000313|EMBL:ACU34294.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34294.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34294.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(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}.
CC   -!- CATALYTIC ACTIVITY: ATP + (R)-pantoate + beta-alanine = AMP +
CC       diphosphate + (R)-pantothenate. {ECO:0000256|HAMAP-Rule:MF_00158,
CC       ECO:0000256|SAAS:SAAS00387728}.
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:SAAS00387774}.
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:SAAS00702622}.
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DR   EMBL; CP001630; ACU34294.1; -; Genomic_DNA.
DR   RefSeq; WP_012782957.1; NC_013093.1.
DR   STRING; 446462.Amir_0325; -.
DR   EnsemblBacteria; ACU34294; ACU34294; Amir_0325.
DR   KEGG; ami:Amir_0325; -.
DR   eggNOG; ENOG4107QQT; Bacteria.
DR   eggNOG; COG0414; LUCA.
DR   HOGENOM; HOG000175516; -.
DR   KO; K01918; -.
DR   OMA; LFNMVQP; -.
DR   OrthoDB; POG091H00FM; -.
DR   UniPathway; UPA00028; UER00005.
DR   Proteomes; UP000002213; 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-HAMAP.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-HAMAP.
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:SF4; PTHR21299:SF4; 1.
DR   Pfam; PF02569; Pantoate_ligase; 1.
DR   TIGRFAMs; TIGR00018; panC; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6WGH8.
DR   SWISS-2DPAGE; C6WGH8.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00158,
KW   ECO:0000256|SAAS:SAAS00094328};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00158,
KW   ECO:0000256|SAAS:SAAS00094346};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00158,
KW   ECO:0000256|SAAS:SAAS00094334, ECO:0000313|EMBL:ACU34294.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00158,
KW   ECO:0000256|SAAS:SAAS00094327};
KW   Pantothenate biosynthesis {ECO:0000256|HAMAP-Rule:MF_00158,
KW   ECO:0000256|SAAS:SAAS00094356};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213}.
FT   NP_BIND      44     51       ATP. {ECO:0000256|HAMAP-Rule:MF_00158}.
FT   NP_BIND     162    165       ATP. {ECO:0000256|HAMAP-Rule:MF_00158}.
FT   NP_BIND     199    202       ATP. {ECO:0000256|HAMAP-Rule:MF_00158}.
FT   ACT_SITE     51     51       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00158}.
FT   BINDING      76     76       Beta-alanine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00158}.
FT   BINDING      76     76       Pantoate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00158}.
FT   BINDING     168    168       Pantoate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00158}.
FT   BINDING     191    191       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00158}.
SQ   SEQUENCE   296 AA;  31512 MW;  58A5FCD86F1FABB6 CRC64;
     MTKPLTKDDY TPGGVTVHRD PERLRRVTRA LRSAGRNIAL VPTMGALHEG HRRLIREAHV
     LQNTVVVVSV FVNPTQFGEA ADLERYPRDL DADVEVCRQE RAPLVFAPEV ATMYPAGSQV
     TLDPGPLGSE LEGASRPGHF AGVLTVVSKL FNVVQPDYAL FGEKDYQQLS LIGRMATDLN
     VPTAVVGVPT VRESDGLALS SRNRFLSESE RESATALSAA LVAGSHVSAL GAEAVLSTAR
     ATLDAVPGLD LDYLELRAPD LGPAPVNGDA RLLVAARVGS TRLIDNVPVL LGAGDE
//

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