ID D9T0J2_MICAI Unreviewed; 280 AA.
AC D9T0J2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 01-MAY-2013, entry version 17.
DE RecName: Full=Pantothenate synthetase;
DE Short=PS;
DE EC=6.3.2.1;
DE AltName: Full=Pantoate--beta-alanine ligase;
DE AltName: Full=Pantoate-activating enzyme;
GN Name=panC; OrderedLocusNames=Micau_5858;
OS Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / JCM 10878 /
OS NBRC 16125 / INA 9442).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Micromonosporineae; Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=644283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442;
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., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA Ovchinnikova G., Hirsch A.M., Woyke T.;
RT "Complete sequence of Micromonospora aurantiaca ATCC 27029.";
RL Submitted (AUG-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 (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + (R)-pantoate + beta-alanine = AMP +
CC diphosphate + (R)-pantothenate.
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis;
CC (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- MISCELLANEOUS: The reaction proceeds by a bi uni uni bi ping pong
CC mechanism (By similarity).
CC -!- SIMILARITY: Belongs to the pantothenate synthetase family.
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DR EMBL; CP002162; ADL49362.1; -; Genomic_DNA.
DR RefSeq; YP_003838938.1; NC_014391.1.
DR EnsemblBacteria; ADL49362; ADL49362; Micau_5858.
DR GeneID; 9603966; -.
DR KEGG; mau:Micau_5858; -.
DR PATRIC; 42397541; VBIMicAur74833_5906.
DR HOGENOM; HOG000175516; -.
DR KO; K01918; -.
DR OMA; EDFGSYP; -.
DR BioCyc; MAUR644283:GHOD-5911-MONOMER; -.
DR UniPathway; UPA00028; UER00005.
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:HAMAP.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:HAMAP.
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;
KW ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW Pantothenate biosynthesis.
FT NP_BIND 28 35 ATP (By similarity).
FT NP_BIND 146 149 ATP (By similarity).
FT NP_BIND 183 186 ATP (By similarity).
FT ACT_SITE 35 35 Proton donor (By similarity).
FT BINDING 59 59 Beta-alanine (By similarity).
FT BINDING 59 59 Pantoate (By similarity).
FT BINDING 152 152 Pantoate (By similarity).
FT BINDING 175 175 ATP; via amide nitrogen and carbonyl
FT oxygen (By similarity).
SQ SEQUENCE 280 AA; 30266 MW; 227AA0A99EECF7E6 CRC64;
MAEVLHTRKE LAAAREAMAG PVGVVMTMGA LHAGHEALLR AARERAGHVI VTIFVNPLQF
GPNEDFDRYP RTLDTDLEIC RRAGVDVVFA PSVTEMYPEG RPTVRLDPGP LGEDLEGLSR
PGFFHGVLTV VMKLLQLTRP DLAFFGEKDY QQLTLVRRMV RDLDVPAEIV GVPTVREPDG
LAMSSRNRYL SAPERETALS LSAALRAGAT AAERGEDAGA VLAAAHRAFD APDARLDYLV
LTDTELEPGP VAGPARLLIA AWVGATRLID NTAIHLAPRP
//
