ID A5Z4G7_9FIRM Unreviewed; 396 AA.
AC A5Z4G7;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
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 ECO:0000313|EMBL:EDM52066.1};
GN ORFNames=EUBVEN_00593 {ECO:0000313|EMBL:EDM52066.1};
OS Eubacterium ventriosum ATCC 27560.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=411463 {ECO:0000313|EMBL:EDM52066.1, ECO:0000313|Proteomes:UP000006000};
RN [1] {ECO:0000313|EMBL:EDM52066.1, ECO:0000313|Proteomes:UP000006000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27560 {ECO:0000313|EMBL:EDM52066.1,
RC ECO:0000313|Proteomes:UP000006000};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDM52066.1, ECO:0000313|Proteomes:UP000006000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27560 {ECO:0000313|EMBL:EDM52066.1,
RC ECO:0000313|Proteomes:UP000006000};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Eubacterium ventriosum (ATCC 27560).";
RL Submitted (APR-2007) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2
CC H(+); Xref=Rhea:RHEA:24252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58141, ChEBI:CHEBI:456216; EC=3.6.1.41;
CC Evidence={ECO:0000256|ARBA:ARBA00001682};
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|HAMAP-
CC Rule:MF_00244}.
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:EDM52066.1}.
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DR EMBL; AAVL02000028; EDM52066.1; -; Genomic_DNA.
DR RefSeq; WP_005358455.1; NZ_DS264264.1.
DR AlphaFoldDB; A5Z4G7; -.
DR STRING; 411463.EUBVEN_00593; -.
DR eggNOG; COG1057; Bacteria.
DR eggNOG; COG1713; Bacteria.
DR HOGENOM; CLU_050191_0_0_9; -.
DR OrthoDB; 5295945at2; -.
DR UniPathway; UPA00253; UER00332.
DR Proteomes; UP000006000; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008803; F:bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity; IEA:RHEA.
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; cd00077; HDc; 1.
DR CDD; cd02165; NMNAT; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR HAMAP; MF_00244; NaMN_adenylyltr; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR006675; HDIG_dom.
DR InterPro; IPR005248; NadD/NMNAT.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR005249; YqeK.
DR NCBIfam; TIGR00488; bis(5'-nucleosyl)-tetraphosphatase (symmetrical) YqeK; 1.
DR NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR NCBIfam; TIGR00277; HDIG; 1.
DR NCBIfam; TIGR00482; nicotinate (nicotinamide) nucleotide adenylyltransferase; 1.
DR PANTHER; PTHR35795:SF1; BIS(5'-NUCLEOSYL)-TETRAPHOSPHATASE, SYMMETRICAL; 1.
DR PANTHER; PTHR35795; SLR1885 PROTEIN; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR Pfam; PF01966; HD; 1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00244};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
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:EDM52066.1};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|HAMAP-Rule:MF_00244};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00244, ECO:0000313|EMBL:EDM52066.1}.
FT DOMAIN 218..346
FT /note="HD/PDEase"
FT /evidence="ECO:0000259|SMART:SM00471"
SQ SEQUENCE 396 AA; 45724 MW; D0AD8D4EBC406202 CRC64;
MKVGILGGTF DPIHNAHIEI AKTALNQFNL DKVMIMPTPN PPHKDKNTIT SNFHRINMIK
LAILPYENIE FSDFEINMHD VTYTADTLYL LNELNPDIEY YFILGSDSIM SFLSWYRPDI
ILKYAKLLTV RRDDESFDLM DSKIKEIEKT YNTTIGIIDM KAMDISSGFI RTHSHEEIKK
AVPESVYKYI IDNDLYTDTN VNRAWSINKI TRDLEKELKP SRYTHTLNVA KTAKNMAEAF
NVNPNKAYFA GILHDCAKNF SDQKLLQICK DNNLPINVFE ERNPSLLHGK VGAFMAKNKY
GITDEEILSA ITWHTTGKDN MTDLEKIVFC ADYIEPGRTK QPHLEELRSI ALSDLDMLTF
RILEDTVEYL KAKSLDCIDD NTITAYNFYK KLIEER
//
