ID   PNCC_SHEON              Reviewed;         424 AA.
AC   Q8EK32;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Nicotinamide-nucleotide amidohydrolase PncC;
DE            Short=NMN amidohydrolase PncC;
DE            EC=3.5.1.42;
DE   AltName: Full=NMN deamidase;
DE   AltName: Full=Nicotinamide-nucleotide amidase;
GN   Name=pncC; OrderedLocusNames=SO_0272;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-14, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, DISRUPTION PHENOTYPE, AND FUNCTION.
RC   STRAIN=MR-1;
RX   PubMed=21953451; DOI=10.1074/jbc.m111.275818;
RA   Galeazzi L., Bocci P., Amici A., Brunetti L., Ruggieri S., Romine M.,
RA   Reed S., Osterman A.L., Rodionov D.A., Sorci L., Raffaelli N.;
RT   "Identification of nicotinamide mononucleotide deamidase of the bacterial
RT   pyridine nucleotide cycle reveals a novel broadly conserved amidohydrolase
RT   family.";
RL   J. Biol. Chem. 286:40365-40375(2011).
CC   -!- FUNCTION: One of the key enzymes of the pyridine nucleotide cycle which
CC       permits cells to recycle the by products of NAD consumption back to
CC       NAD. Has no activity on NAD, NADP, nicotinamide or nicotinamide
CC       riboside. {ECO:0000269|PubMed:21953451}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-nicotinamide D-ribonucleotide + H2O = NH4(+) + nicotinate
CC         beta-D-ribonucleotide; Xref=Rhea:RHEA:12400, ChEBI:CHEBI:14649,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:57502; EC=3.5.1.42;
CC         Evidence={ECO:0000269|PubMed:21953451};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.5-9.0. {ECO:0000269|PubMed:21953451};
CC   -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:21953451}.
CC   -!- DISRUPTION PHENOTYPE: Not essential for growth on defined medium, loss
CC       of NMN amidohydrolase activity. {ECO:0000269|PubMed:21953451}.
CC   -!- SIMILARITY: Belongs to the CinA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00226}.
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DR   EMBL; AE014299; AAN53357.1; -; Genomic_DNA.
DR   RefSeq; NP_715912.1; NC_004347.2.
DR   RefSeq; WP_011070644.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EK32; -.
DR   SMR; Q8EK32; -.
DR   STRING; 211586.SO_0272; -.
DR   PaxDb; Q8EK32; -.
DR   KEGG; son:SO_0272; -.
DR   PATRIC; fig|211586.12.peg.263; -.
DR   eggNOG; COG1058; Bacteria.
DR   eggNOG; COG1546; Bacteria.
DR   HOGENOM; CLU_030805_9_2_6; -.
DR   OMA; PGVPYEM; -.
DR   OrthoDB; 1834406at2; -.
DR   PhylomeDB; Q8EK32; -.
DR   BioCyc; SONE211586:G1GMP-262-MON; -.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0019159; F:nicotinamide-nucleotide amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019363; P:pyridine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00885; cinA; 1.
DR   Gene3D; 3.40.980.10; -; 1.
DR   Gene3D; 3.90.950.20; -; 1.
DR   HAMAP; MF_00226_B; CinA_B; 1.
DR   InterPro; IPR036653; CinA-like_C.
DR   InterPro; IPR008136; CinA_C.
DR   InterPro; IPR008135; Competence-induced_CinA.
DR   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
DR   Pfam; PF02464; CinA; 1.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   PIRSF; PIRSF006728; CinA; 1.
DR   SMART; SM00852; MoCF_biosynth; 1.
DR   SUPFAM; SSF142433; SSF142433; 1.
DR   SUPFAM; SSF53218; SSF53218; 1.
DR   TIGRFAMs; TIGR00200; cinA_nterm; 1.
DR   TIGRFAMs; TIGR00177; molyb_syn; 1.
DR   TIGRFAMs; TIGR00199; PncC_domain; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Pyridine nucleotide biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..424
FT                   /note="Nicotinamide-nucleotide amidohydrolase PncC"
FT                   /id="PRO_0000336525"
SQ   SEQUENCE   424 AA;  46182 MW;  7216C66B90FD52E0 CRC64;
     MKLEMICTGE EVLSGQIVDT NAAWFASTMM EHGIEIQRRV TVGDRLEDLI AVFQERSLHA
     DVILVNGGLG PTSDDMSAEA MAKAKGESLV ENSEWRQRLE DWFTRNNREM PVSNLKQAML
     PVSAVMVDNP VGTACGFRVK LNRAWLFFTP GVPFELKHMV KEQFIPFIRD EFNLDAKVAL
     KKLLTIGHGE SALADKIEPL ELPEGITIGY RSSMPHIEIK IFARGEKAIA LLPRVAGHIK
     MVLGTAVVAE DKATLAEEIH FRLLNSGLTL SAAESCTGGM ITSQLVDFPG SSSYLQHGLV
     TYSNESKVRV LGVNPATLDD HGAVSIPTVE EMAKGARAIL DSDFALATSG IAGPDGGTED
     KPVGTVAIAL ATRSGVYSQM IKLPRRSRDL VRSLSAAVAY DMLRRELLSE AVIVDYQSIG
     RFSK