Q8TBE9 (NANP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N-acylneuraminate-9-phosphatase
EC=3.1.3.29

Alternative name(s):
Haloacid dehalogenase-like hydrolase domain-containing protein 4
Neu5Ac-9-Pase

Gene names

Name:	NANP
Synonyms:	C20orf147, HDHD4

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	248 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	N-acylneuraminate 9-phosphate + H2O = N-acylneuraminate + phosphate. Ref.5
Cofactor	Magnesium. Ref.5
Enzyme regulation	Inhibited by vanadate and calcium. Ref.5
Pathway	Amino-sugar metabolism; N-acetylneuraminate biosynthesis.
Sequence similarities	Belongs to the HAD-like hydrolase superfamily. NANP family.
Biophysicochemical properties	Kinetic parameters: KM=0.09 mM for N-acetylneuraminate 9-P Ref.5 KM=19.2 mM for fructose 1,6-P2 KM=2.7 mM for 6-P-gluconate KM=5.9 mM for N-acetylglucosamine 6-P Vmax=112 µmol/min/mg enzyme with N-acetylneuraminate 9-P as substrate Vmax=6.10 µmol/min/mg enzyme with fructose 1,6-P2 as substrate Vmax=2.79 µmol/min/mg enzyme with 6-P-gluconate as substrate Vmax=2.46 µmol/min/mg enzyme with N-acetylglucosamine 6-P as substrate Vmax=0.149 µmol/min/mg enzyme with sorbitol 6-P as substrate Vmax=0.140 µmol/min/mg enzyme with 3-P glycerate as substrate Vmax=0.095 µmol/min/mg enzyme with P-serine as substrate Vmax=0.094 µmol/min/mg enzyme with glycerol 3-P as substrate Vmax=0.090 µmol/min/mg enzyme with ribulose 5-P as substrate Vmax=0.072 µmol/min/mg enzyme with N-acetylmannosamine 6-P as substrate Vmax=0.063 µmol/min/mg enzyme with arabinose 6-P as substrate Vmax=0.042 µmol/min/mg enzyme with ribose 6-P as substrate Vmax=0.023 µmol/min/mg enzyme with glucosamine 6-P as substrate Vmax=0.019 µmol/min/mg enzyme with phosphoglycolate as substrate Vmax=0.019 µmol/min/mg enzyme with fructose 6-P as substrate Vmax=0.017 µmol/min/mg enzyme with glycerol 2-P as substrate Vmax=0.016 µmol/min/mg enzyme with glucose 6-P as substrate Vmax=0.015 µmol/min/mg enzyme with mannose 6-P as substrate Vmax=0.004 µmol/min/mg enzyme with glucose 1-P as substrate Vmax=0.002 µmol/min/mg enzyme with P-enolpyruvate as substrate Vmax=0.001 µmol/min/mg enzyme with ATP as substrate
Sequence caution	The sequence BAB85055.1 differs from that shown. Reason: It seems to be derived from genomic DNA and not from cDNA.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Ligand	Magnesium
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	N-acetylneuraminate biosynthetic process Inferred from direct assay Ref.5. Source: UniProtKB
Molecular function	N-acylneuraminate-9-phosphatase activity Inferred from direct assay Ref.5. Source: UniProtKB phosphoglycolate phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 248

248

N-acylneuraminate-9-phosphatase

PRO_0000083938

Regions

Region

12 – 14

3

Substrate binding

Region

131 – 132

2

Substrate binding

Sites

Binding site

164

1

Substrate

Experimental info

Sequence conflict

32 – 55

24

IKLLQ…KVQVK → TSPPMALLWAGSVRPAPSCT LTSP in BAB85055. Ref.1

Secondary structure

1

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248

Helix Strand Turn

Details...

Beta strand

8 – 11

4

Turn

14 – 16

3

Helix

29 – 37

9

Helix

44 – 57

14

Turn

63 – 65

3

Helix

68 – 83

16

Helix

90 – 106

17

Helix

112 – 124

13

Beta strand

125 – 130

6

Helix

135 – 144

10

Helix

148 – 150

3

Beta strand

152 – 155

4

Helix

167 – 176

10

Beta strand

184 – 187

4

Helix

191 – 195

5

Beta strand

205 – 209

5

Beta strand

224 – 228

5

Helix

230 – 232

3

Helix

233 – 240

8

Sequences

	Sequence		Length	Mass (Da)
	Q8TBE9 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 360E6D7AB965294B	FASTA	248	27,813
	10 20 30 40 50 60 MGLSRVRAVF FDLDNTLIDT AGASRRGMLE VIKLLQSKYH YKEEAEIICD KVQVKLSKEC 70 80 90 100 110 120 FHPYNTCITD LRTSHWEEAI QETKGGAANR KLAEECYFLW KSTRLQHMTL AEDVKAMLTE 130 140 150 160 170 180 LRKEVRLLLL TNGDRQTQRE KIEACACQSY FDAVVVGGEQ REEKPAPSIF YYCCNLLGVQ 190 200 210 220 230 240 PGDCVMVGDT LETDIQGGLN AGLKATVWIN KNGIVPLKSS PVPHYMVSSV LELPALLQSI DCKVSMST

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[2]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[5]	"Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase." Maliekal P., Vertommen D., Delpierre G., Van Schaftingen E. Glycobiology 16:165-172(2006) [PubMed: 16237198] [Abstract] Cited for: CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[6]	"The crystal structure of human N-acetylneuraminic acid phosphatase, NANP." Structural genomics consortium (SGC) Submitted (DEC-2008) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH PHOSPHATE IONS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK055472 mRNA. Translation: BAG51524.1.
AK074335 mRNA. Translation: BAB85055.1. Sequence problems.
AL031673 Genomic DNA. Translation: CAI22444.1.
CH471133 Genomic DNA. Translation: EAX10081.1.
BC022552 mRNA. Translation: AAH22552.1.

IPI

IPI00152196.

RefSeq

NP_689880.1. NM_152667.2.

UniGene

Hs.143137.
Hs.606268.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2W4M	X-ray	2.60	A	1-248	[»]

ProteinModelPortal

Q8TBE9.

SMR

Q8TBE9. Positions 1-244.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8TBE9. 1 interaction.

STRING

Q8TBE9.

PTM databases

PhosphoSite

Q8TBE9.

Polymorphism databases

DMDM

30315932.

Proteomic databases

PRIDE

Q8TBE9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000304788; ENSP00000302441; ENSG00000170191.

GeneID

140838.

KEGG

hsa:140838.

NMPDR

fig|9606.3.peg.20010.

UCSC

uc002wuy.1. human.

Organism-specific databases

CTD

140838.

GeneCards

GC20M025543.

H-InvDB

HIX0203043.

HGNC

HGNC:16140. NANP.

MIM

610763. gene.

neXtProt

NX_Q8TBE9.

PharmGKB

PA25689.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12749.

GeneTree

ENSGT00390000003094.

HOGENOM

HBG716739.

HOVERGEN

HBG051895.

InParanoid

Q8TBE9.

OMA

HYIVSSV.

OrthoDB

EOG483D5Q.

PhylomeDB

Q8TBE9.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-14518.

Gene expression databases

ArrayExpress

Q8TBE9.

Bgee

Q8TBE9.

CleanEx

HS_NANP.

Genevestigator

Q8TBE9.

GermOnline

ENSG00000170191. Homo sapiens.

Family and domain databases

InterPro

IPR005834. Dehalogen-like_hydro.
IPR023214. HAD-like_dom.
IPR011950. HAD-SF_hydro_IA_CTE7.
IPR006439. HAD-SF_hydro_IA_v1.
IPR005833. Haloacid_DH/epoxide_hydro.
[Graphical view]

Gene3D

G3DSA:3.40.50.1000. HAD-like_dom. 1 hit.

KO

K01097.

Pfam

PF00702. Hydrolase. 1 hit.
[Graphical view]

PRINTS

PR00413. HADHALOGNASE.

SUPFAM

SSF56784. HAD-like_dom. 1 hit.

TIGRFAMs

TIGR02253. CTE7. 1 hit.
TIGR01549. HAD-SF-IA-v1. 1 hit.

ProtoNet

Search...

Other

NextBio

84460.

SOURCE

Search...

Entry information

Entry name

NANP_HUMAN

Accession

Primary (citable) accession number: Q8TBE9
Secondary accession number(s): B3KP12 , Q5JYN8, Q8TE97, Q9Y3N0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	June 1, 2002
Last modified:	December 14, 2011
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.