Q81VW8 (Q81VW8_BACAN) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Dihydropteroate synthase EMBL AAP24126.1
EC=2.5.1.15 EMBL AAP24126.1

Gene names

Name:	folP EMBL AAP24126.1
Ordered Locus Names:	BA_0071 EMBL AAP24126.1, BAS0071 EMBL AAT52409.1, GBAA_0071 EMBL AAT29149.1

Organism

Bacillus anthracis [Reference proteome] [HAMAP]

Taxonomic identifier

1392 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	280 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Molecular function	Transferase EMBL AAP24126.1
Technical term	3D-structure PDB 3H2O PDB 3H2N PDB 3H2M PDB 1TWZ PDB 1TWW PDB 1TWS PDB 1TX2 PDB 1TX0 PDB 3H22 PDB 3H21 PDB 3H24 PDB 4DB7 PDB 3H23 PDB 4D8Z PDB 3H26 PDB 3H2A PDB 3H2C PDB 3TYE PDB 4D9P PDB 3TYD PDB 4DAF PDB 4D8A PDB 3TYC PDB 3TYB PDB 3TYA PDB 3H2E PDB 3H2F PDB 4DAI Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	folic acid-containing compound biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular_function	dihydropteroate synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q81VW8 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: ACEB54F50658A69B	FASTA	280	30,976
	10 20 30 40 50 60 MCSLKWDYDL RCGEYTLNLN EKTLIMGILN VTPDSFSDGG SYNEVDAAVR HAKEMRDEGA 70 80 90 100 110 120 HIIDIGGEST RPGFAKVSVE EEIKRVVPMI QAVSKEVKLP ISIDTYKAEV AKQAIEAGAH 130 140 150 160 170 180 IINDIWGAKA EPKIAEVAAH YDVPIILMHN RDNMNYRNLM ADMIADLYDS IKIAKDAGVR 190 200 210 220 230 240 DENIILDPGI GFAKTPEQNL EAMRNLEQLN VLGYPVLLGT SRKSFIGHVL DLPVEERLEG 250 260 270 280 TGATVCLGIE KGCEFVRVHD VKEMSRMAKM MDAMIGKGVK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M. Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames EMBL AAP24126.1 and Ames / isolate Porton.
[2]	"Crystal structure of 7,8-dihydropteroate synthase from Bacillus anthracis: mechanism and novel inhibitor design." Babaoglu K., Qi J., Lee R.E., White S.W. Structure 12:1705-1717(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 5-277.
[3]	"Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne EMBL AAT52409.1.
[4]	"Genetic basis for sulfonamide resistance in Bacillus anthracis." Valderas M.W., Bourne P.C., Barrow W.W. Microb. Drug Resist. 13:11-20(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: Sterne EMBL AAZ65853.1.
[5]	"The complete genome sequence of Bacillus anthracis Ames "Ancestor"." Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A. J. Bacteriol. 191:445-446(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames Ancestor EMBL AAT29149.1 and Ames ancestor.
[6]	Joardar V., Shrivastava S., Brinkac L.M., Harkins D.M., Durkin A.S., Sutton G. Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: Ames EMBL AAP24126.1.
[7]	"Structural studies of pterin-based inhibitors of dihydropteroate synthase." Hevener K.E., Yun M.K., Qi J., Kerr I.D., Babaoglu K., Hurdle J.G., Balakrishna K., White S.W., Lee R.E. J. Med. Chem. 53:166-177(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 5-280.
[8]	"Structure-based design of novel pyrimido[4,5-c]pyridazine derivatives as dihydropteroate synthase inhibitors with increased affinity." Zhao Y., Hammoudeh D., Yun M.K., Qi J., White S.W., Lee R.E. ChemMedChem 7:861-870(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 5-280.
[9]	"Catalysis and sulfa drug resistance in dihydropteroate synthase." Yun M.K., Wu Y., Li Z., Zhao Y., Waddell M.B., Ferreira A.M., Lee R.E., Bashford D., White S.W. Science 335:1110-1114(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 5-280.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE016879 Genomic DNA. Translation: AAP24126.1.
AE017334 Genomic DNA. Translation: AAT29149.1.
AE017225 Genomic DNA. Translation: AAT52409.1.
DQ139876 Genomic DNA. Translation: AAZ65853.1.

RefSeq

NP_842640.1. NC_003997.3.
YP_016674.1. NC_007530.2.
YP_026358.1. NC_005945.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TWS	X-ray	2.00	A/B	5-277	[»]
1TWW	X-ray	2.50	A/B	5-277	[»]
1TWZ	X-ray	2.75	A/B	5-277	[»]
1TX0	X-ray	2.15	A/B	5-277	[»]
1TX2	X-ray	1.83	A/B	5-277	[»]
3H21	X-ray	2.32	A/B	5-280	[»]
3H22	X-ray	2.40	A/B	5-280	[»]
3H23	X-ray	2.20	A/B	5-280	[»]
3H24	X-ray	2.50	A/B	5-280	[»]
3H26	X-ray	2.50	A/B	5-280	[»]
3H2A	X-ray	2.40	A/B	5-280	[»]
3H2C	X-ray	2.60	A/B	5-280	[»]
3H2E	X-ray	2.00	A/B	5-280	[»]
3H2F	X-ray	2.20	A/B	5-280	[»]
3H2M	X-ray	2.31	A/B	5-280	[»]
3H2N	X-ray	2.40	A/B	5-280	[»]
3H2O	X-ray	2.70	A/B	5-280	[»]
3TYA	X-ray	2.61	A/B	5-280	[»]
3TYB	X-ray	2.60	A/B	5-280	[»]
3TYC	X-ray	2.30	A/B	5-280	[»]
3TYD	X-ray	2.50	A/B	5-280	[»]
3TYE	X-ray	2.30	A/B	5-280	[»]
4D8A	X-ray	2.18	A/B	5-280	[»]
4D8Z	X-ray	2.20	A/B	5-280	[»]
4D9P	X-ray	2.26	A/B	5-280	[»]
4DAF	X-ray	2.50	A/B	5-280	[»]
4DAI	X-ray	2.50	A/B	5-280	[»]
4DB7	X-ray	2.50	A/B	5-280	[»]

SMR

Q81VW8. Positions 5-277.

ModBase

Search...

Protein-protein interaction databases

STRING

198094.BA_0071.

Protocols and materials databases

DNASU

1083704.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAP24126; AAP24126; BA_0071.
AAT29149; AAT29149; GBAA_0071.
AAT52409; AAT52409; BAS0071.

GeneID

1083704.
2814968.
2852651.

KEGG

ban:BA_0071.
bar:GBAA_0071.
bat:BAS0071.

Phylogenomic databases

KO

K00796.

OMA

KSMIGNL.

ProtClustDB

CLSK915700.

Enzyme and pathway databases

BioCyc

BANT260799:GJAJ-80-MONOMER.
BANT261594:GJ7F-82-MONOMER.

Family and domain databases

Gene3D

3.20.20.20. 1 hit.

InterPro

IPR006390. DHP_synth.
IPR011005. Dihydropteroate_synth-like.
IPR000489. Pterin-binding.
[Graphical view]

Pfam

PF00809. Pterin_bind. 1 hit.
[Graphical view]

SUPFAM

SSF51717. DHP_synth_like. 1 hit.

TIGRFAMs

TIGR01496. DHPS. 1 hit.

PROSITE

PS00792. DHPS_1. 1 hit.
PS00793. DHPS_2. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1075045.

EvolutionaryTrace

Q81VW8.

Entry information

Entry name

Q81VW8_BACAN

Accession

Primary (citable) accession number: Q81VW8
Secondary accession number(s): E9QTW3 , E9QTW4, E9QTW5, Q2QCA4, Q6I4X2, Q6KYL6

Entry history

Integrated into UniProtKB/TrEMBL:	June 1, 2003
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)