NFT1_CAEEL
ID NFT1_CAEEL Reviewed; 440 AA.
AC O76463;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Nitrilase and fragile histidine triad fusion protein NitFhit;
DE Includes:
DE RecName: Full=Bis(5'-adenosyl)-triphosphatase;
DE EC=3.6.1.29;
DE AltName: Full=AP3A hydrolase;
DE Short=AP3Aase;
DE AltName: Full=Diadenosine 5',5'''-P1,P3-triphosphate hydrolase;
DE AltName: Full=Dinucleosidetriphosphatase;
DE Includes:
DE RecName: Full=Nitrilase homolog;
DE EC=3.5.-.-;
GN Name=nft-1 {ECO:0000312|WormBase:Y56A3A.13}; ORFNames=Y56A3A.13;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC39136.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=9671749; DOI=10.1073/pnas.95.15.8744;
RA Pekarsky Y., Campiglio M., Siprashvili Z., Druck T., Sedkov Y., Tillib S.,
RA Draganescu A., Wermuth P., Rothman J.H., Huebner K., Buchberg A.M.,
RA Mazo A., Brenner C., Croce C.M.;
RT "Nitrilase and Fhit homologs are encoded as fusion proteins in Drosophila
RT melanogaster and Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8744-8749(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), PROTEIN SEQUENCE OF N-TERMINUS,
RP ACTIVE SITES, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=10959838; DOI=10.1016/s0960-9822(00)00621-7;
RA Pace H.C., Hodawadekar S.C., Draganescu A., Huang J., Bieganowski P.,
RA Pekarsky Y., Croce C.M., Brenner C.;
RT "Crystal structure of the worm NitFhit Rosetta stone protein reveals a Nit
RT tetramer binding two Fhit dimers.";
RL Curr. Biol. 10:907-917(2000).
CC -!- FUNCTION: Cleaves A-5'-PPP-5'A to yield AMP and ADP.
CC {ECO:0000269|PubMed:10959838}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + P(1),P(3)-bis(5'-adenosyl) triphosphate = ADP + AMP + 2
CC H(+); Xref=Rhea:RHEA:13893, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58529, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC EC=3.6.1.29; Evidence={ECO:0000269|PubMed:10959838};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10959838}.
CC -!- DEVELOPMENTAL STAGE: Expressed in adult. {ECO:0000269|PubMed:9671749}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the UPF0012 family.
CC {ECO:0000255}.
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DR EMBL; AF069986; AAC39136.1; -; mRNA.
DR EMBL; AL132860; CAB60517.1; -; Genomic_DNA.
DR PIR; T43198; T43198.
DR RefSeq; NP_499556.1; NM_067155.6.
DR PDB; 1EMS; X-ray; 2.80 A; A/B=1-440.
DR PDBsum; 1EMS; -.
DR AlphaFoldDB; O76463; -.
DR SMR; O76463; -.
DR BioGRID; 41808; 17.
DR DIP; DIP-26945N; -.
DR IntAct; O76463; 2.
DR STRING; 6239.Y56A3A.13; -.
DR EPD; O76463; -.
DR PaxDb; O76463; -.
DR PeptideAtlas; O76463; -.
DR EnsemblMetazoa; Y56A3A.13.1; Y56A3A.13.1; WBGene00003594.
DR GeneID; 176628; -.
DR KEGG; cel:CELE_Y56A3A.13; -.
DR UCSC; Y56A3A.13.1; c. elegans.
DR CTD; 176628; -.
DR WormBase; Y56A3A.13; CE22580; WBGene00003594; nft-1.
DR eggNOG; KOG0807; Eukaryota.
DR eggNOG; KOG3379; Eukaryota.
DR GeneTree; ENSGT00550000075099; -.
DR HOGENOM; CLU_030130_12_1_1; -.
DR InParanoid; O76463; -.
DR OMA; GWHNKKR; -.
DR OrthoDB; 1154369at2759; -.
DR PhylomeDB; O76463; -.
DR EvolutionaryTrace; O76463; -.
DR PRO; PR:O76463; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003594; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0047710; F:bis(5'-adenosyl)-triphosphatase activity; ISS:ARUK-UCL.
DR GO; GO:0110050; F:deaminated glutathione amidase activity; ISS:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0043605; P:cellular amide catabolic process; ISS:UniProtKB.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IBA:GO_Central.
DR CDD; cd01275; FHIT; 1.
DR CDD; cd07572; nit; 1.
DR Gene3D; 3.30.428.10; -; 1.
DR Gene3D; 3.60.110.10; -; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR039383; FHIT.
DR InterPro; IPR019808; Histidine_triad_CS.
DR InterPro; IPR011146; HIT-like.
DR InterPro; IPR036265; HIT-like_sf.
DR InterPro; IPR045254; Nit1/2_C-N_Hydrolase.
DR InterPro; IPR001110; UPF0012_CS.
DR Pfam; PF00795; CN_hydrolase; 1.
DR Pfam; PF01230; HIT; 1.
DR SUPFAM; SSF54197; SSF54197; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
DR PROSITE; PS00892; HIT_1; 1.
DR PROSITE; PS51084; HIT_2; 1.
DR PROSITE; PS01227; UPF0012; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Multifunctional enzyme;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..440
FT /note="Nitrilase and fragile histidine triad fusion protein
FT NitFhit"
FT /id="PRO_0000109791"
FT DOMAIN 14..264
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT DOMAIN 297..405
FT /note="HIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT MOTIF 390..394
FT /note="Histidine triad motif"
FT ACT_SITE 54
FT /evidence="ECO:0000303|PubMed:9671749"
FT ACT_SITE 127
FT /evidence="ECO:0000303|PubMed:9671749"
FT ACT_SITE 169
FT /evidence="ECO:0000303|PubMed:9671749"
FT ACT_SITE 392
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P49789,
FT ECO:0000255|PROSITE-ProRule:PRU00054"
FT STRAND 13..20
FT /evidence="ECO:0007829|PDB:1EMS"
FT HELIX 28..44
FT /evidence="ECO:0007829|PDB:1EMS"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:1EMS"
FT HELIX 63..87
FT /evidence="ECO:0007829|PDB:1EMS"
FT STRAND 91..101
FT /evidence="ECO:0007829|PDB:1EMS"
FT STRAND 104..115
FT /evidence="ECO:0007829|PDB:1EMS"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:1EMS"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:1EMS"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:1EMS"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:1EMS"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1EMS"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:1EMS"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:1EMS"
FT HELIX 169..173
FT /evidence="ECO:0007829|PDB:1EMS"
FT HELIX 175..183
FT /evidence="ECO:0007829|PDB:1EMS"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:1EMS"
FT HELIX 197..215
FT /evidence="ECO:0007829|PDB:1EMS"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:1EMS"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:1EMS"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:1EMS"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:1EMS"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:1EMS"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:1EMS"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:1EMS"
FT HELIX 264..273
FT /evidence="ECO:0007829|PDB:1EMS"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:1EMS"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:1EMS"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:1EMS"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:1EMS"
FT STRAND 316..322
FT /evidence="ECO:0007829|PDB:1EMS"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:1EMS"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:1EMS"
FT HELIX 348..368
FT /evidence="ECO:0007829|PDB:1EMS"
FT STRAND 372..377
FT /evidence="ECO:0007829|PDB:1EMS"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:1EMS"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:1EMS"
FT STRAND 393..398
FT /evidence="ECO:0007829|PDB:1EMS"
FT HELIX 426..437
FT /evidence="ECO:0007829|PDB:1EMS"
SQ SEQUENCE 440 AA; 49936 MW; 34EED223CEF92975 CRC64;
MLSTVFRRTM ATGRHFIAVC QMTSDNDLEK NFQAAKNMIE RAGEKKCEMV FLPECFDFIG
LNKNEQIDLA MATDCEYMEK YRELARKHNI WLSLGGLHHK DPSDAAHPWN THLIIDSDGV
TRAEYNKLHL FDLEIPGKVR LMESEFSKAG TEMIPPVDTP IGRLGLSICY DVRFPELSLW
NRKRGAQLLS FPSAFTLNTG LAHWETLLRA RAIENQCYVV AAAQTGAHNP KRQSYGHSMV
VDPWGAVVAQ CSERVDMCFA EIDLSYVDTL REMQPVFSHR RSDLYTLHIN EKSSETGGLK
FARFNIPADH IFYSTPHSFV FVNLKPVTDG HVLVSPKRVV PRLTDLTDAE TADLFIVAKK
VQAMLEKHHN VTSTTICVQD GKDAGQTVPH VHIHILPRRA GDFGDNEIYQ KLASHDKEPE
RKPRSNEQMA EEAVVYRNLM
