B0BYP7 (PANB_ACAM1) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-methyl-2-oxobutanoate hydroxymethyltransferase
EC=2.1.2.11

Alternative name(s):
Ketopantoate hydroxymethyltransferase
Short name=KPHMT

Gene names

Name:	panB
Ordered Locus Names:	AM1_2048

Organism

Acaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]

Taxonomic identifier

329726 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Acaryochloris

Protein attributes

Sequence length	259 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is tranferred onto alpha-ketoisovalerate to form ketopantoate By similarity. HAMAP MF_00156
Catalytic activity	5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate. HAMAP MF_00156
Cofactor	Binds 1 magnesium ion per subunit By similarity. HAMAP MF_00156
Pathway	Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. HAMAP MF_00156
Subunit structure	Homodecamer; pentamer of dimers By similarity. HAMAP MF_00156
Subcellular location	Cytoplasm Potential HAMAP MF_00156.
Sequence similarities	Belongs to the PanB family.

Ontologies

Keywords
Biological process	Pantothenate biosynthesis
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Methyltransferase Transferase
Technical term	Complete 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	3-methyl-2-oxobutanoate hydroxymethyltransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW methyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 259	259	3-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156		PRO_1000076814
Regions
	Region	44 – 45	2	Alpha-ketoisovalerate binding By similarity
Sites
	Active site	183	1	Proton acceptor By similarity
	Metal binding	44	1	Magnesium By similarity
	Metal binding	83	1	Magnesium By similarity
	Metal binding	115	1	Magnesium By similarity
	Binding site	83	1	Alpha-ketoisovalerate By similarity
	Binding site	113	1	Alpha-ketoisovalerate By similarity

Sequences

	Sequence		Length	Mass (Da)
	B0BYP7 [UniParc]. Last modified February 26, 2008. Version 1. Checksum: 48D3A06EBC8C9CDF	FASTA	259	27,847
	10 20 30 40 50 60 MAVTIHQLRT WKEQGRPISV LTAWDFPFAT LLDQAGVDVL LVGDSLAMVA LGYPTTLPLT 70 80 90 100 110 120 LDEMLYHAQA VTRGVNHALV ICDLPFLSYQ ESPQQALRSA GTLLQQAGVA AVKLEGGYPD 130 140 150 160 170 180 MAKTVHYLVD RGIPVMGHVG LTPQSVHQFS GYRRQGTSDV EADRILQEAI ALEAAGAFAI 190 200 210 220 230 240 VLEHIPAPLA TKITQTLTIP TIGIGAGPGC DGQVLVTADM LGLSAWQPPF AKAYTNLQES 250 ITGAVQQFCD DVRHHQFPQ

References

[1]

"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina." Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W. Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed: 18252824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MBIC 11017.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000828 Genomic DNA. Translation: ABW27063.1.
RefSeq	YP_001516377.1. NC_009925.1.
3D structure databases
ProteinModelPortal	B0BYP7.
ModBase	Search...
Protein-protein interaction databases
STRING	B0BYP7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5680862.
GenomeReviews	Gene locus AM1_2048 in contig CP000828_GR.
KEGG	amr:AM1_2048.
PATRIC	20618434. VBIAcaMar40141_1853.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG299908.
OMA	YDATFAH.
PhylomeDB	B0BYP7.
Enzyme and pathway databases
BioCyc	AMAR329726:AM1_2048-MONOMER.
Family and domain databases
HAMAP	MF_00156. PanB. [Tree]
InterPro	IPR003700. Pantoate_hydroxy_MeTrfase. IPR015813. Pyrv/PenolPyrv_Kinase. [Graphical view]
Gene3D	G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
KO	K00606.
PANTHER	PTHR20881. Pantoate_transf. 1 hit.
Pfam	PF02548. Pantoate_transf. 1 hit. [Graphical view]
PIRSF	PIRSF000388. Pantoate_hydroxy_MeTrfase. 1 hit.
SUPFAM	SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMs	TIGR00222. PanB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PANB_ACAM1

Accession

Primary (citable) accession number: B0BYP7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 26, 2008
Last modified:	January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program