NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
DOI=10.1126/science.1080029; PubMed=12663928 [NCBI, ExPASy, EBI, Israel, Japan]
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.;
"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
Science 299:2074-2076(2003).

Comments

FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate (By similarity).
CATALYTIC ACTIVITY: ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate.
PATHWAY: Cofactor biosynthesis; pantothenate biosynthesis; pantothenate from beta-alanine and pantoate: step 1/1 .
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (Potential).
MISCELLANEOUS: The reaction proceeds by a bi uni uni bi ping pong mechanism (By similarity).
SIMILARITY: Belongs to the pantothenate synthetase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE015928; AAO79413.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_813219.1; -.

3D structure databases

HSSP

O06280; 1N2E. [HSSP ENTRY / PDB]

ModBase

Q89ZR8.

Enzyme and pathway databases

BioCyc

BTHE226186:BT_4308-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004592;	Molecular function: pantoate-beta-alanine ligase activity (inferred from electronic annotation from HAMAP).
GO:0015940;	Biological process: pantothenate biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00158; -; 1.
PBIL [Tree]

InterPro

IPR003721; Pantoate_ligase.
IPR014729; Rossmann-like_a/b/a_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.

PANTHER

PTHR21299:SF1; Pantoate_ligase; 1.

Pfam

PF02569; Pantoate_ligase; 1.
Pfam graphical view of domain structure.

TIGR00018; panC; 1.

Genome annotation databases

GeneID

1073735; -.

GenomeReviews

AE015928_GR; BT_4308.

KEGG

bth:BT_4308; -.

NMPDR

fig|226186.1.peg.4306; -.

Phylogenomic databases

HOGENOM

Q89ZR8; -.

Genome annotation databases

CMR

Q89ZR8; BT_4308.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Pantothenate biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 282`	`282`	`Pantothenate synthetase.`	`PRO_0000305400`
`NP_BIND`	`30 37`	`8`	`ATP (By similarity).`
`NP_BIND`	`147 150`	`4`	`ATP (By similarity).`
`NP_BIND`	`184 187`	`4`	`ATP (By similarity).`
`ACT_SITE`	`37 37`		`Proton donor (By similarity).`
`BINDING`	`61 61`		`Beta-alanine (By similarity).`
`BINDING`	`61 61`		`Pantoate (By similarity).`
`BINDING`	`153 153`		`Pantoate (By similarity).`
`BINDING`	`176 176`		`ATP; via amide nitrogen and carbonyl oxygen (By similarity).`

Sequence information

Length: 282 AA [This is the length of the unprocessed precursor]

Molecular weight: 31564 Da [This is the MW of the unprocessed precursor]

CRC64: F2D107024D54785E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKVIHTIKDL QAELTALRAQ GKKVGLVPTM GALHAGHASL VKRSVSENGV TVVSVFVNPT 

        70         80         90        100        110        120 
QFNDKNDLAK YPRTLDADCR LLEDCGAAFA FAPSVEEMYP QPDTREFSYA PLDTVMEGAF 

       130        140        150        160        170        180 
RPGHFNGVCQ IVSKLFDAVQ PDRAYFGEKD FQQLAIIREM VRQMDYKLEI VGCPIVREED 

       190        200        210        220        230        240 
GLALSSRNKR LSARERENAL NISQTLFKSR TFAASHTVSE TQKMVEEAIE DAPGLRLEYF 

       250        260        270        280 
EIVDGNTLQK VSSWEDSLYV VGCITVFCGE VRLIDNIKYK EI

Q89ZR8 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools