Q1IHA8 (PANC_KORVE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pantothenate synthetase
Short name=PS
EC=6.3.2.1

Alternative name(s):
Pantoate--beta-alanine ligase
Pantoate-activating enzyme

Gene names

Name:	panC
Ordered Locus Names:	Acid345_4743

Organism

Koribacter versatilis (strain Ellin345)

Taxonomic identifier

204669 [NCBI]

Taxonomic lineage

Bacteria › Acidobacteria › Candidatus Koribacter

Protein attributes

Sequence length	291 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate By similarity. HAMAP MF_00158
Catalytic activity	ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP MF_00158
Pathway	Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. HAMAP MF_00158
Subunit structure	Homodimer By similarity. HAMAP MF_00158
Subcellular location	Cytoplasm Potential HAMAP MF_00158.
Miscellaneous	The reaction proceeds by a bi uni uni bi ping pong mechanism By similarity. HAMAP MF_00158
Sequence similarities	Belongs to the pantothenate synthetase family.

Ontologies

Keywords
Biological process	Pantothenate biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	pantothenate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW pantoate-beta-alanine ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 291	291	Pantothenate synthetase HAMAP MF_00158		PRO_0000305381
Regions
	Nucleotide binding	30 – 37	8	ATP By similarity
	Nucleotide binding	147 – 150	4	ATP By similarity
	Nucleotide binding	184 – 187	4	ATP By similarity
Sites
	Active site	37	1	Proton donor By similarity
	Binding site	61	1	Beta-alanine By similarity
	Binding site	61	1	Pantoate By similarity
	Binding site	153	1	Pantoate By similarity
	Binding site	176	1	ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1IHA8 [UniParc]. Last modified June 13, 2006. Version 1. Checksum: 5250848795BD6034	FASTA	291	31,878
	10 20 30 40 50 60 MRVVRTIAEM QAICRTLHRE GKSIGLVPTM GALHAGHISL VRTARTQNDS VVVSIFVNPI 70 80 90 100 110 120 QFGPNEDLAK YPRTFEQDCA QLDHEGVDFV FSPGVEEMYP EGTATFVHVD GLSEKLDGRS 130 140 150 160 170 180 RPGHFKGVTT VVSKLFHIIP ADHAYFGQKD AAQVAVIRKM VRDQNFDIDL MICPIVREKD 190 200 210 220 230 240 GLALSSRNAY LDPTQRQQAL VLHRALMRVQ MLADTGHTDA YYLAEAGRAV IAEEPGAKLD 250 260 270 280 290 YLEIVDPNTL EPITEIGKGA LVAVAAQIGN TRLIDNLVLQ AAGNARGPRT S

References

[1]

"Three genomes from the phylum Acidobacteria provide insight into the lifestyles of these microorganisms in soils." Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C., Davidsen T.M. , DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R. Appl. Environ. Microbiol. 75:2046-2056(2009) [PubMed: 19201974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ellin345.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000360 Genomic DNA. Translation: ABF43742.1.
RefSeq	YP_593816.1. NC_008009.1.
3D structure databases
ProteinModelPortal	Q1IHA8.
SMR	Q1IHA8. Positions 1-279.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1IHA8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4070681.
GenomeReviews	Gene locus Acid345_4743 in contig CP000360_GR.
KEGG	aba:Acid345_4743.
NMPDR	fig|204669.6.peg.4720.
PATRIC	31986925. VBICanKor57425_5069.
Phylogenomic databases
eggNOG	COG0414.
HOGENOM	HBG428839.
OMA	LNMPIQI.
PhylomeDB	Q1IHA8.
ProtClustDB	PRK00380.
Enzyme and pathway databases
BioCyc	ABAC204669:ACID345_4743-MONOMER.
Family and domain databases
HAMAP	MF_00158. PanC. [Tree]
InterPro	IPR004821. Cyt_trans-rel. IPR003721. Pantoate_ligase. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KO	K01918.
PANTHER	PTHR21299:SF1. Pantoate_ligase. 1 hit.
Pfam	PF02569. Pantoate_ligase. 1 hit. [Graphical view]
TIGRFAMs	TIGR00125. Cyt_tran_rel. 1 hit. TIGR00018. PanC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PANC_KORVE

Accession

Primary (citable) accession number: Q1IHA8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	June 13, 2006
Last modified:	January 25, 2012
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program