PNUC_HAEIN
ID PNUC_HAEIN Reviewed; 226 AA.
AC Q57425; P96338; Q8L2G5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Nicotinamide riboside transporter PnuC;
GN Name=pnuC; OrderedLocusNames=HI_1077.1;
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 [GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=12446641; DOI=10.1128/jb.184.24.6906-6917.2002;
RA Kurnasov O.V., Polanuyer B.M., Ananta S., Sloutsky R., Tam A., Gerdes S.Y.,
RA Osterman A.L.;
RT "Ribosylnicotinamide kinase domain of NadR protein: identification and
RT implications in NAD biosynthesis.";
RL J. Bacteriol. 184:6906-6917(2002).
RN [2]
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 [3]
RP FUNCTION, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION, AND TOPOLOGY.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=15561822; DOI=10.1128/aac.48.12.4532-4541.2004;
RA Sauer E., Merdanovic M., Mortimer A.P., Bringmann G., Reidl J.;
RT "PnuC and the utilization of the nicotinamide riboside analog 3-
RT aminopyridine in Haemophilus influenzae.";
RL Antimicrob. Agents Chemother. 48:4532-4541(2004).
CC -!- FUNCTION: Required for nicotinamide riboside transport across the inner
CC membrane. {ECO:0000269|PubMed:15561822}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15561822}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15561822}.
CC -!- INDUCTION: Repressed by NadR.
CC -!- SIMILARITY: Belongs to the nicotinamide ribonucleoside (NR) uptake
CC permease (TC 4.B.1) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC22744.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF503632; AAM27449.1; -; Genomic_DNA.
DR EMBL; L42023; AAC22744.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; Q57425; -.
DR SMR; Q57425; -.
DR STRING; 71421.HI_1077.1; -.
DR EnsemblBacteria; AAC22744; AAC22744; HI_1077.1.
DR KEGG; hin:HI_1077.1; -.
DR eggNOG; COG3201; Bacteria.
DR HOGENOM; CLU_1956896_0_0_6; -.
DR BRENDA; 2.7.1.22; 2529.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034257; F:nicotinamide riboside transmembrane transporter activity; IEA:InterPro.
DR InterPro; IPR006419; NMN_transpt_PnuC.
DR PANTHER; PTHR36122; PTHR36122; 1.
DR Pfam; PF04973; NMN_transporter; 1.
DR TIGRFAMs; TIGR01528; NMN_trans_PnuC; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; NAD; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..226
FT /note="Nicotinamide riboside transporter PnuC"
FT /id="PRO_0000078000"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15561822"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..90
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..153
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..202
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15561822"
FT BINDING 183
FT /ligand="beta-nicotinamide D-riboside"
FT /ligand_id="ChEBI:CHEBI:15927"
FT /evidence="ECO:0000250|UniProtKB:D2ZZC1"
FT BINDING 187
FT /ligand="beta-nicotinamide D-riboside"
FT /ligand_id="ChEBI:CHEBI:15927"
FT /evidence="ECO:0000250|UniProtKB:D2ZZC1"
SQ SEQUENCE 226 AA; 25530 MW; 6870235BA9C06EE3 CRC64;
MTLAARLKQE FVSGWKPFEV VWLALFIIAQ IWAYVQTPDS WLAMISGISG ILCVVLVSKG
KISNYFFGLI FAYTYFYVAW GSNFLGEMNT VLYVYLPSQF IGYFMWKANM QNSDGGESVI
AKALTVKGWM TLIVVTTVGT LLFVQALQAA GGSSTGLDGL TTIITVAAQI LMILRYREQW
LLWIGLNILS IFLWAETPAI YLMYSAYLLN SLYGYYNWTK LVKRTN
