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Database: UniProt
Entry: A0A127FAR9_STEDE
LinkDB: A0A127FAR9_STEDE
Original site: A0A127FAR9_STEDE 
ID   A0A127FAR9_STEDE        Unreviewed;       213 AA.
AC   A0A127FAR9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Probable nicotinate-nucleotide adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00244};
DE            EC=2.7.7.18 {ECO:0000256|HAMAP-Rule:MF_00244};
DE   AltName: Full=Deamido-NAD(+) diphosphorylase {ECO:0000256|HAMAP-Rule:MF_00244};
DE   AltName: Full=Deamido-NAD(+) pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00244};
DE   AltName: Full=Nicotinate mononucleotide adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00244};
DE            Short=NaMN adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00244};
GN   Name=nadD {ECO:0000256|HAMAP-Rule:MF_00244};
GN   ORFNames=ACG33_05910 {ECO:0000313|EMBL:AMN46639.1};
OS   Steroidobacter denitrificans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Steroidobacterales;
OC   Steroidobacteraceae; Steroidobacter.
OX   NCBI_TaxID=465721 {ECO:0000313|EMBL:AMN46639.1, ECO:0000313|Proteomes:UP000070250};
RN   [1] {ECO:0000313|EMBL:AMN46639.1, ECO:0000313|Proteomes:UP000070250}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18526 {ECO:0000313|EMBL:AMN46639.1,
RC   ECO:0000313|Proteomes:UP000070250};
RA   Yang F.-C., Chen Y.-L., Yu C.-P., Tang S.-L., Wang P.-H., Ismail W.,
RA   Wang C.-H., Yang C.-Y., Chiang Y.-R.;
RT   "A Comprehensive Approach to Explore the Metabolic and Phylogenetic
RT   Diversity of Bacterial Steroid Degradation in the Environment: Testosterone
RT   as an Example.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible adenylation of nicotinate
CC       mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
CC       {ECO:0000256|ARBA:ARBA00002324, ECO:0000256|HAMAP-Rule:MF_00244}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+)
CC         + diphosphate; Xref=Rhea:RHEA:22860, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502,
CC         ChEBI:CHEBI:58437; EC=2.7.7.18;
CC         Evidence={ECO:0000256|ARBA:ARBA00001785, ECO:0000256|HAMAP-
CC         Rule:MF_00244};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+)
CC       from nicotinate D-ribonucleotide: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005019, ECO:0000256|HAMAP-Rule:MF_00244}.
CC   -!- SIMILARITY: Belongs to the NadD family. {ECO:0000256|ARBA:ARBA00009014,
CC       ECO:0000256|HAMAP-Rule:MF_00244}.
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DR   EMBL; CP011971; AMN46639.1; -; Genomic_DNA.
DR   RefSeq; WP_066919527.1; NZ_CP011971.1.
DR   AlphaFoldDB; A0A127FAR9; -.
DR   STRING; 465721.ACG33_05910; -.
DR   KEGG; sdf:ACG33_05910; -.
DR   PATRIC; fig|465721.4.peg.1260; -.
DR   OrthoDB; 5295945at2; -.
DR   UniPathway; UPA00253; UER00332.
DR   Proteomes; UP000070250; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02165; NMNAT; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00244; NaMN_adenylyltr; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR005248; NadD/NMNAT.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR   NCBIfam; TIGR00482; nicotinate (nicotinamide) nucleotide adenylyltransferase; 1.
DR   PANTHER; PTHR39321; NICOTINATE-NUCLEOTIDE ADENYLYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR39321:SF3; PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE; 1.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00244};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00244};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00244};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00244,
KW   ECO:0000313|EMBL:AMN46639.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW   ECO:0000256|HAMAP-Rule:MF_00244};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070250};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00244, ECO:0000313|EMBL:AMN46639.1}.
FT   DOMAIN          6..183
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
SQ   SEQUENCE   213 AA;  24026 MW;  C50A073CA5A9AE0D CRC64;
     MTTIGIFGGT FDPIHFGHLR TALELLQALR LNEIRFLPAG NPPHRETTVA SAAERLAMVR
     AAIRDQSGFK VDDREIRREG LSYSVDTMRS LRTDFPESSL CLIVGMDAFL GLTKWYRWRE
     LLELTHLVVA HRPGWRAPAM GLLGELLVDR GTSRIDDLHE AHAGRILIHA VTQLEISSTE
     VRKLIGAGRD PRYLMPEEVR GIIEESGCYR TKK
//
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