ID F6BJJ3_THEXL Unreviewed; 282 AA.
AC F6BJJ3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 03-APR-2013, entry version 12.
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=Thexy_1920;
OS Thermoanaerobacterium xylanolyticum (strain ATCC 49914 / DSM 7097 /
OS LX-11).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family III. Incertae Sedis;
OC Thermoanaerobacterium.
OX NCBI_TaxID=858215;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Lu M., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Hemme C., Woyke T.;
RT "Complete sequence of Thermoanaerobacterium xylanolyticum LX-11.";
RL Submitted (MAY-2011) 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; CP002739; AEF17939.1; -; Genomic_DNA.
DR RefSeq; YP_004471611.1; NC_015555.1.
DR EnsemblBacteria; AEF17939; AEF17939; Thexy_1920.
DR GeneID; 10660156; -.
DR KEGG; txy:Thexy_1920; -.
DR KO; K01918; -.
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; 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;
KW ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW Pantothenate biosynthesis.
FT NP_BIND 29 36 ATP (By similarity).
FT NP_BIND 146 149 ATP (By similarity).
FT NP_BIND 183 186 ATP (By similarity).
FT ACT_SITE 36 36 Proton donor (By similarity).
FT BINDING 60 60 Beta-alanine (By similarity).
FT BINDING 60 60 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 282 AA; 31608 MW; 8AB3530DDF10EA13 CRC64;
MVVEKIKDVR EIIKSQKKQN KKIGLVPTMG YLHEGHLSLI KKAKENSDFV CASIFVNPIQ
FGPNEDYNKY PRDIERDIKL LENQGCDLVF IPSVEEMYPN ERLTTITVSK ITDKLCGAYR
PGHFDGVCTV VAKLFNIFAP DIAVFGQKDA QQVAVIKKMV EDLNIPVEII ASPIVRDEDG
LALSSRNTYL TYEERHAALI LNKSLKVAEK LLVSGERSAE KVLDAVRKTL ESEPQCKVQY
VSCVHPDTLE DLTTIGDKAL IAIACYIGNT RLIDNLLWGV DE
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