ID A0A0C1UBA8_9CLOT Unreviewed; 1615 AA.
AC A0A0C1UBA8;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=nicotinate-nucleotide adenylyltransferase {ECO:0000256|ARBA:ARBA00012389};
DE EC=2.7.7.18 {ECO:0000256|ARBA:ARBA00012389};
GN ORFNames=U732_314 {ECO:0000313|EMBL:KIE44855.1};
OS Clostridium argentinense CDC 2741.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1418104 {ECO:0000313|EMBL:KIE44855.1, ECO:0000313|Proteomes:UP000031366};
RN [1] {ECO:0000313|EMBL:KIE44855.1, ECO:0000313|Proteomes:UP000031366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 2741 {ECO:0000313|EMBL:KIE44855.1,
RC ECO:0000313|Proteomes:UP000031366};
RX PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA Karavis M.A., Smith L.A.;
RT "Genomic sequences of six botulinum neurotoxin-producing strains
RT representing three clostridial species illustrate the mobility and
RT diversity of botulinum neurotoxin genes.";
RL Infect. Genet. Evol. 30:102-113(2014).
CC -!- FUNCTION: Catalyzes the reversible adenylation of nicotinate
CC mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
CC {ECO:0000256|ARBA:ARBA00002324}.
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};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+)
CC from nicotinate D-ribonucleotide: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005019}.
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:KIE44855.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AYSO01000020; KIE44855.1; -; Genomic_DNA.
DR STRING; 29341.RSJ17_04380; -.
DR Proteomes; UP000031366; Unassembled WGS sequence.
DR GO; GO:0070566; F:adenylyltransferase activity; IEA:UniProt.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR005248; NadD/NMNAT.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR39321; NICOTINATE-NUCLEOTIDE ADENYLYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR39321:SF3; PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Nucleotidyltransferase {ECO:0000313|EMBL:KIE44855.1};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW Reference proteome {ECO:0000313|Proteomes:UP000031366};
KW Transferase {ECO:0000313|EMBL:KIE44855.1}.
FT DOMAIN 927..1085
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
SQ SEQUENCE 1615 AA; 188916 MW; 1D1D4E52E54C9347 CRC64;
MEVNFENIYV RIQRKVLSVK WINKVNLDKI IIDSHIKSEY FVAKLKEMIF KKDYTAKSTL
VLLKPLILEL SSEDILENSE NHLLVYLYEY SLSKVFPEAV NIKLNPNLDS ICNLYFRVLR
IISVFEKHCN GESFISKYPM EFLKDEELEF LEYSDEYLRF AKAFEDSYIY EMMKVNGEIT
GFNTLEHISG VHYLAMYIAR QVKHQGLKVD LGRVSGSAAG HDIGKYGCKK NEMKRVPYLH
YYYSDIWFKK HGINYIRNIA INHSTWDLEF ENLSLESLIL IYSDFRVKNR QINNKNEMHI
FSLKESFDVI LSKLDNVDET KEKRYRRVYS KLRDFEKFLQ SINVETEVKD IDLKCMKKIK
EPLYSLNQGE EIVDNLKYMA INHNINLMYI LRDEHSLNTI IEEARSEKNW KSLREYIRIF
EEYSTYLTQN QKIQTINFLY ENLVHPEDDI RRHSAEIIGK LIAILDEEYR KELPEGAVDD
FFNIDSKDVL RKYIDKILFP SHKIISSHRY WIGYSLSTLI KSLFENCGEN KKEEYKEVVL
SYYETFKYKN SDNLLFLIES ANYIPIDKED KLLDKLYIFI FTMLKKRNIT LRLSTLGLCI
NLMEKLSDES VFVIHLKDYL YSVSAKSSYG AEILLRYRLS QKLSLKDLEY NLKENLQVQK
KNIQEIYLSN LKSATEWSVK KYQIELILEF VKNHKEINAL QASIHFCNLL KVSAVEEVRV
TAGCAIVEIM DLLSFSERNE VAIELLRSLE IEGHKITEYI PRYLGQVLLY IPPKEFDEII
DDLAFKVKIA KPSVKTLMLK TIGVVLEYYK CYGKRFNESE KTLDKRRNTL LSILLNGLGD
YINEVKRSSF TTIGKVIFGS KILSLKEKKN YFDLLAKKIL TLVINDEKED LFFLSNAAGL
AHIYRFIADY NFFIGEFNME IPRKIAFFPG TFDPFSLSHK EIAKTIRNLG YEVYLSVDEF
SWSKKTLPHL LRRNILNMSI ASEFGIFVYP ESEPINLSNK EDLQSLKDNF KEQEVFIVVG
ADVITNASSY KLPYNKGSIH DFSHIVIERN KNNTLSEYLM EIKGNVHIIN LPSKYTDISS
TQIRNYIDSN RDISSLVDPL AEQYIYDNGF YQREPLEKAT LNLLSLETEI IDHKDEEIIN
TLCNIANNGL REKIEELFSK PSGRIVILKD CNKNEICGFS LIHWARSSML YSDIKDMEIA
QYMREESQGR IILLDGFYIK NHEKNKNLLS ILITETLAFA CSRDYEYALY RQCEKDNLST
TIKDTLALYG FKEIFDSVHL VNMSSPCVLN FDIENLIKEP FRSNNKIKAA INESRIKLQQ
VICNLFPGNL VLSFDSNMVH QGLIKKVCKE NKVPEYETNP KSLGSAMCVP YGDILDRYII
PNTVTKSLHT EKYFNPDMKS FKIGEFPHYL SLENQIKMLK SFNRPIILVD NLLHKGYRMK
AIEPIFKKEK INIQKIIVAI LSGRGKDLLD YQGGEVDCLY FIPRLKIWFN ENALYPFIGG
DAVWRGEFPG RNLLPSINLI MPYTSPKFIR GANNKERYKL SKVCIENSIN ILKALEDEYH
YINERNLTLL SLGQVFTIPR SVDRGLDINY DLNHKPSHYL ENDLERLKRF EDMYI
//
