ID R8WTG3_9ENTR Unreviewed; 285 AA.
AC R8WTG3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Putative pyrophosphorylase ModD {ECO:0000256|ARBA:ARBA00019205};
GN ORFNames=WC7_02439 {ECO:0000313|EMBL:EOQ48200.1};
OS Citrobacter sp. KTE151.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=1169322 {ECO:0000313|EMBL:EOQ48200.1, ECO:0000313|Proteomes:UP000014006};
RN [1] {ECO:0000313|EMBL:EOQ48200.1, ECO:0000313|Proteomes:UP000014006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KTE151 {ECO:0000313|EMBL:EOQ48200.1,
RC ECO:0000313|Proteomes:UP000014006};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Nielsen K.L., Frimodt-Moller N., Andersen P.S., Walker B.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Larimer J., McCowan C., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Escherichia coli KTE151.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the NadC/ModD family.
CC {ECO:0000256|ARBA:ARBA00009400, ECO:0000256|PIRNR:PIRNR006250}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOQ48200.1}.
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DR EMBL; ASQK01000005; EOQ48200.1; -; Genomic_DNA.
DR RefSeq; WP_016153361.1; NZ_KB976064.1.
DR AlphaFoldDB; R8WTG3; -.
DR PATRIC; fig|1169322.3.peg.2435; -.
DR HOGENOM; CLU_039622_2_1_6; -.
DR Proteomes; UP000014006; Unassembled WGS sequence.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro.
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 {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|PIRNR:PIRNR006250};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250}.
FT DOMAIN 18..104
FT /note="Quinolinate phosphoribosyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02749"
FT DOMAIN 118..276
FT /note="Quinolinate phosphoribosyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01729"
SQ SEQUENCE 285 AA; 30177 MW; B6BB516ED2B2B235 CRC64;
MIYFSQAQTD ALLLEDIQGG DLTTRALGIG AQPGVIEFSH RQGGCVSGTA VARQMLTSLG
LTVTDILSDG ERANAGQRLI RAHGPAAALH QGWKAVQNVL EWSCGVSGYL VEMLSMLHQR
YPDGQIACTR KAIPGTRLLA TQAILAAGGI IHRGGCAETV LLFANHRRFL TNPNDWTGAI
ARLRSHAPEK KIVVEADTPD EALAALRAAP DVLQLDKFTP EQAAEIARQA PALAPHCTLA
LTGGITLASL AGYLDCGIRL FITSAPYYAP PADIKVSLSP DARGL
//