5NTD_HAEIN
ID 5NTD_HAEIN Reviewed; 603 AA.
AC P44569;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=NAD 5'-nucleotidase;
DE Short=NadN;
DE EC=3.1.3.5;
DE Flags: Precursor;
GN OrderedLocusNames=HI_0206;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP PROTEIN SEQUENCE OF 26-38.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=10675023;
RX DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA Fountoulakis M.;
RT "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL Electrophoresis 21:411-429(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 25-603, FUNCTION, SUBSTRATE
RP SPECIFICITY, COFACTOR, SUBSTRATE-BINDING SITES, ZINC-BINDING SITES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21933152; DOI=10.1042/bj20111263;
RA Garavaglia S., Bruzzone S., Cassani C., Canella L., Allegrone G.,
RA Sturla L., Mannino E., Millo E., De Flora A., Rizzi M.;
RT "The high-resolution crystal structure of periplasmic Haemophilus
RT influenzae NAD nucleotidase reveals a novel enzymatic function of human
RT CD73 related to NAD metabolism.";
RL Biochem. J. 441:131-141(2012).
CC -!- FUNCTION: Degrades NAD into adenosine and nicotinamide riboside, the
CC latter being subsequently internalized by a specific permease. Also
CC endowed with NAD(P) pyrophosphatase activity. Exhibits a broad
CC substrate specificity, recognizing either mono- or dinucleotide
CC nicotinamides and different adenosine phosphates with a maximal
CC activity on 5'-adenosine monophosphate. {ECO:0000269|PubMed:21933152}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
CC phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:21933152};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:21933152};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:21933152}.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000305}.
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DR EMBL; L42023; AAC21874.1; -; Genomic_DNA.
DR PIR; E64054; E64054.
DR RefSeq; NP_438375.1; NC_000907.1.
DR RefSeq; WP_010868956.1; NC_000907.1.
DR PDB; 3ZTV; X-ray; 1.30 A; A=25-603.
DR PDB; 3ZU0; X-ray; 2.00 A; A/B=25-603.
DR PDBsum; 3ZTV; -.
DR PDBsum; 3ZU0; -.
DR AlphaFoldDB; P44569; -.
DR SMR; P44569; -.
DR STRING; 71421.HI_0206; -.
DR EnsemblBacteria; AAC21874; AAC21874; HI_0206.
DR KEGG; hin:HI_0206; -.
DR PATRIC; fig|71421.8.peg.211; -.
DR eggNOG; COG0737; Bacteria.
DR HOGENOM; CLU_005854_7_1_6; -.
DR OMA; WLATINS; -.
DR PhylomeDB; P44569; -.
DR BioCyc; HINF71421:G1GJ1-217-MON; -.
DR BioCyc; MetaCyc:MON-8341; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0008253; F:5'-nucleotidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0008768; F:UDP-sugar diphosphatase activity; IBA:GO_Central.
DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009166; P:nucleotide catabolic process; IBA:GO_Central.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; -; 1.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006146; 5'-Nucleotdase_CS.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006420; NadN.
DR PANTHER; PTHR11575; PTHR11575; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; SSF55816; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR TIGRFAMs; TIGR01530; nadN; 1.
DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1.
DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Metal-binding;
KW Nucleotide-binding; Periplasm; Reference proteome; Signal; Zinc.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:10675023"
FT CHAIN 26..603
FT /note="NAD 5'-nucleotidase"
FT /id="PRO_0000000026"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 397
FT /ligand="substrate"
FT BINDING 437
FT /ligand="substrate"
FT BINDING 456
FT /ligand="substrate"
FT BINDING 540..546
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 127
FT /note="Transition state stabilizer"
FT SITE 130
FT /note="Transition state stabilizer"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:3ZTV"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:3ZTV"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:3ZTV"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:3ZTV"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:3ZTV"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:3ZTV"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:3ZTV"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:3ZTV"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:3ZTV"
FT HELIX 203..214
FT /evidence="ECO:0007829|PDB:3ZTV"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:3ZTV"
FT HELIX 230..239
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:3ZTV"
FT HELIX 258..262
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 267..276
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 282..288
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 294..302
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 308..319
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:3ZTV"
FT HELIX 338..349
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:3ZTV"
FT HELIX 361..377
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 380..388
FT /evidence="ECO:0007829|PDB:3ZTV"
FT HELIX 394..396
FT /evidence="ECO:0007829|PDB:3ZTV"
FT HELIX 410..420
FT /evidence="ECO:0007829|PDB:3ZTV"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:3ZU0"
FT STRAND 428..432
FT /evidence="ECO:0007829|PDB:3ZTV"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 442..446
FT /evidence="ECO:0007829|PDB:3ZTV"
FT HELIX 447..453
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 459..466
FT /evidence="ECO:0007829|PDB:3ZTV"
FT HELIX 467..482
FT /evidence="ECO:0007829|PDB:3ZTV"
FT HELIX 487..489
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 491..503
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 506..508
FT /evidence="ECO:0007829|PDB:3ZU0"
FT STRAND 511..517
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 531..538
FT /evidence="ECO:0007829|PDB:3ZTV"
FT HELIX 539..542
FT /evidence="ECO:0007829|PDB:3ZTV"
FT HELIX 545..547
FT /evidence="ECO:0007829|PDB:3ZTV"
FT HELIX 549..554
FT /evidence="ECO:0007829|PDB:3ZTV"
FT HELIX 558..560
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 563..568
FT /evidence="ECO:0007829|PDB:3ZTV"
FT HELIX 569..579
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 582..584
FT /evidence="ECO:0007829|PDB:3ZTV"
FT STRAND 590..594
FT /evidence="ECO:0007829|PDB:3ZTV"
SQ SEQUENCE 603 AA; 66245 MW; B641C32A5A2B6AEA CRC64;
MLLSKKSASF ALSAFAMLFT SVALAKEAPQ AHKAVELSIL HINDHHSYLE PHETRINLNG
QQTKVDIGGF SAVNAKLNKL RKKYKNPLVL HAGDAITGTL YFTLFGGSAD AAVMNAGNFH
YFTLGNHEFD AGNEGLLKLL EPLKIPVLSA NVIPDKNSIL YNKWKPYDIF TVDGEKIAII
GLDTVNKTVN SSSPGKDVKF YDEIATAQIM ANALKQQGIN KIILLSHAGS EKNIEIAQKV
NDIDVIVTGD SHYLYGNDEL RSLKLPVIYE YPLEFKNPNG DPVFVMEGWA YSAVVGDLGV
KFSPEGIASI TRKIPHVLMS SHKLQVKNAE GKWTELTGDE RKKALDTLKS MKSISLDDHD
AKTDMLISKY KSEKDRLAQE IVGVITGSAM PGGSANRIPN KAGSNPEGSI ATRFIAETMY
NELKTVDLTI QNAGGVRADI LPGNVTFNDA YTFLPFGNTL YTYKMEGSLV KQVLEDAMQF
ALVDGSTGAF PYGAGIRYEA NETPNAEGKR LVSVEVLNKQ TQQWEPIDDN KRYLVGTNAY
VAGGKDGYKT FGKLFNDPKY EGVDTYLPDA ESFIKFMKKH PHFEAYTSSN VKFNASTDAL
PKK
