Q04066 (BNA7_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable kynurenine formamidase
EC=3.5.1.9

Alternative name(s):
Biosynthesis of nicotinic acid protein 7
Probable N-formylkynurenine formamidase

Gene names

Name:	BNA7
Ordered Locus Names:	YDR428C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the conversion of tryptophan to nicotinic acid, NAD(H) and NADP(H). Ref.6
Catalytic activity	N-formyl-L-kynurenine + H2O = formate + L-kynurenine. Ref.6
Pathway	Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 2/2. Ref.6
Disruption phenotype	Cells exhibit slow growth in the absence of nicotinate. Ref.6
Sequence similarities	Belongs to the BNA7 family.

Ontologies

Keywords
Biological process	Tryptophan catabolism
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	NAD biosynthetic process Inferred from direct assay Ref.6. Source: SGD tryptophan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	arylformamidase activity Inferred from direct assay Ref.6. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 261

261

Probable kynurenine formamidase

PRO_0000234660

Sites

Active site

36

1

Potential

Active site

110

1

Potential

Amino acid modifications

Modified residue

9

1

Phosphoserine Ref.4 Ref.5 Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

261

Helix Strand Turn

Details...

Helix

15 – 17

3

Beta strand

19 – 22

4

Beta strand

30 – 35

6

Turn

39 – 41

3

Helix

47 – 50

4

Helix

51 – 60

10

Beta strand

66 – 71

6

Turn

76 – 78

3

Helix

83 – 99

17

Beta strand

104 – 109

6

Helix

111 – 120

10

Helix

121 – 124

4

Turn

127 – 129

3

Helix

132 – 141

10

Beta strand

144 – 151

8

Helix

156 – 162

7

Helix

164 – 166

3

Helix

167 – 173

7

Helix

178 – 180

3

Helix

185 – 199

15

Beta strand

202 – 208

7

Helix

217 – 228

12

Beta strand

234 – 238

5

Helix

243 – 248

6

Helix

250 – 258

9

Sequences

	Sequence		Length	Mass (Da)
	Q04066 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: F07FE52DD9D2EF92	FASTA	261	29,991
	10 20 30 40 50 60 MSNTVRAISP DITLFNKTLT FQEISQNTRE AVIYIHGGAW NDPENTPNDF NQLANTIKSM 70 80 90 100 110 120 DTESTVCQYS IEYRLSPEIT NPRNLYDAVS NITRLVKEKG LTNINMVGHS VGATFIWQIL 130 140 150 160 170 180 AALKDPQEKM SEAQLQMLGL LQIVKRVFLL DGIYSLKELL VEYPEYDCFT RLAFPDGIQM 190 200 210 220 230 240 YEEEPSRVMP YVKKALSRFS IDMHLVHSYS DELLTLRQTN CLISCLQDYQ LSFKLYLDDL 250 260 GLHNDVYKNG KVAKYIFDNI C

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Synergistic computational and experimental proteomics approaches for more accurate detection of active serine hydrolases in yeast." Baxter S.M., Rosenblum J.S., Knutson S., Nelson M.R., Montimurro J.S., Di Gennaro J.A., Speir J.A., Burbaum J.J., Fetrow J.S. Mol. Cell. Proteomics 3:209-225(2004) [PubMed: 14645503] [Abstract] Cited for: IDENTIFICATION AS A SERINE HYDROLASE, MASS SPECTROMETRY.
[4]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, MASS SPECTROMETRY. Strain: YAL6B.
[5]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, MASS SPECTROMETRY. Strain: ADR376.
[6]	"Identification of formyl kynurenine formamidase and kynurenine aminotransferase from Saccharomyces cerevisiae using crystallographic, bioinformatic and biochemical evidence." Wogulis M., Chew E.R., Donohoue P.D., Wilson D.K. Biochemistry 47:1608-1621(2008) [PubMed: 18205391] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DISRUPTION PHENOTYPE.
[7]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, MASS SPECTROMETRY.
[8]	"Crystal structure of an alpha/beta serine hydrolase (YDR428C) from Saccharomyces cerevisiae at 1.85 A resolution." Arndt J.W., Schwarzenbacher R., Page R., Abdubek P., Ambing E., Biorac T., Canaves J.M., Chiu H.-J., Dai X., Deacon A.M., DiDonato M., Elsliger M.-A., Godzik A., Grittini C., Grzechnik S.K., Hale J., Hampton E., Han G.W. , Haugen J., Hornsby M., Klock H.E., Koesema E., Kreusch A., Kuhn P., Jaroszewski L., Lesley S.A., Levin I., McMullan D., McPhillips T.M., Miller M.D., Morse A., Moy K., Nigoghossian E., Ouyang J., Peti W.S., Quijano K., Reyes R., Sims E., Spraggon G., Stevens R.C., van den Bedem H., Velasquez J., Vincent J., von Delft F., Wang X., West B., White A., Wolf G., Xu Q., Zagnitko O., Hodgson K.O., Wooley J., Wilson I.A. Proteins 58:755-758(2005) [PubMed: 15624212] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U33007 Genomic DNA. Translation: AAB64885.1.
BK006938 Genomic DNA. Translation: DAA12267.1.

PIR

S69709.

RefSeq

NP_010716.1. NM_001180736.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VKH	X-ray	1.85	A/B	1-261	[»]

ProteinModelPortal

Q04066.

SMR

Q04066. Positions 4-261.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4139N.

IntAct

Q04066. 1 interaction.

MINT

MINT-555667.

STRING

Q04066.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDR428C; YDR428C; YDR428C.

GeneID

852038.

KEGG

sce:YDR428C.

NMPDR

fig|4932.3.peg.1489.

Organism-specific databases

CYGD

YDR428c.

SGD

S000002836. BNA7.

Phylogenomic databases

eggNOG

fuNOG11665.

GeneTree

EFGT00070000009980.

HOGENOM

HBG203294.

OMA

NTHSANV.

OrthoDB

EOG4GMZ6M.

Gene expression databases

ArrayExpress

Q04066.

Genevestigator

Q04066.

GermOnline

YDR428C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR013094. AB_hydrolase_3.
[Graphical view]

KO

K14263.

Pfam

PF07859. Abhydrolase_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

970281.

Entry information

Entry name

BNA7_YEAST

Accession

Primary (citable) accession number: Q04066
Secondary accession number(s): D6VT57

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program