ID   MODD_HAEIN              Reviewed;         281 AA.
AC   Q57278; O05066;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Putative pyrophosphorylase ModD;
DE            EC=2.4.2.-;
GN   Name=modD; OrderedLocusNames=HI_1473;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Pseudomonadota; 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).
CC   -!- SIMILARITY: Belongs to the NadC/ModD family. {ECO:0000305}.
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DR   EMBL; L42023; AAC23121.1; -; Genomic_DNA.
DR   PIR; H64125; H64125.
DR   RefSeq; NP_439624.1; NC_000907.1.
DR   AlphaFoldDB; Q57278; -.
DR   SMR; Q57278; -.
DR   STRING; 71421.HI_1473; -.
DR   EnsemblBacteria; AAC23121; AAC23121; HI_1473.
DR   KEGG; hin:HI_1473; -.
DR   PATRIC; fig|71421.8.peg.1540; -.
DR   eggNOG; COG0157; Bacteria.
DR   HOGENOM; CLU_039622_2_1_6; -.
DR   OrthoDB; 8216773at2; -.
DR   PhylomeDB; Q57278; -.
DR   BioCyc; HINF71421:G1GJ1-1498-MONOMER; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IBA:GO_Central.
DR   GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
DR   GO; GO:0034213; P:quinolinate catabolic process; IBA:GO_Central.
DR   CDD; cd01573; modD_like; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.90.1170.20; Quinolinate phosphoribosyl transferase, N-terminal domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006242; ModD.
DR   InterPro; IPR027277; NadC/ModD.
DR   InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR   InterPro; IPR037128; Quinolinate_PRibosylTase_N_sf.
DR   InterPro; IPR002638; Quinolinate_PRibosylTrfase_C.
DR   InterPro; IPR022412; Quinolinate_PRibosylTrfase_N.
DR   NCBIfam; TIGR01334; modD; 1.
DR   PANTHER; PTHR32179; NICOTINATE-NUCLEOTIDE PYROPHOSPHORYLASE [CARBOXYLATING]; 1.
DR   PANTHER; PTHR32179:SF4; PYROPHOSPHORYLASE MODD-RELATED; 1.
DR   Pfam; PF01729; QRPTase_C; 1.
DR   Pfam; PF02749; QRPTase_N; 1.
DR   PIRSF; PIRSF006250; NadC_ModD; 1.
DR   SUPFAM; SSF51690; Nicotinate/Quinolinate PRTase C-terminal domain-like; 1.
DR   SUPFAM; SSF54675; Nicotinate/Quinolinate PRTase N-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..281
FT                   /note="Putative pyrophosphorylase ModD"
FT                   /id="PRO_0000155960"
SQ   SEQUENCE   281 AA;  31436 MW;  2CB8BF3681F2DC45 CRC64;
     MIYFSDKELD DLLLEDIYRG DLTTHALSIE NIPAKILFKR KNAGVVAGVS VAEKLLKKLD
     IQPHLYVKEG EWVESGALLI SAEGMSEQLH QAWKVVQLVL EWSCGVAQYT AEMIANAKSV
     NPTAVVACTR KSIPNTRKLA TNAVLAAGGH IHRQGVSETL LVFTNHRNLL SDPNDWTKIV
     DRLRQEAPEN KITLEADNYA QFEQMYMAEP DIIQLDKWLL EDVKKALDLL QSKQKDILLS
     VAGGVNKNNV SDYAKLGIRL FITSAPYYVP PEDIKVVIEK I
//