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Database: UniProt
Entry: A0A1H9QNB4_9EURY
LinkDB: A0A1H9QNB4_9EURY
Original site: A0A1H9QNB4_9EURY 
ID   A0A1H9QNB4_9EURY        Unreviewed;       201 AA.
AC   A0A1H9QNB4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   08-MAY-2019, entry version 7.
DE   RecName: Full=Nicotinamide-nucleotide adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00243};
DE            EC=2.7.7.1 {ECO:0000256|HAMAP-Rule:MF_00243};
DE   AltName: Full=NAD(+) diphosphorylase {ECO:0000256|HAMAP-Rule:MF_00243};
DE   AltName: Full=NAD(+) pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00243};
DE   AltName: Full=NMN adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00243};
GN   ORFNames=SAMN04489841_4214 {ECO:0000313|EMBL:SER61233.1};
OS   Natrinema salaciae.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
OC   Natrialbales; Natrialbaceae; Natrinema.
OX   NCBI_TaxID=1186196 {ECO:0000313|EMBL:SER61233.1, ECO:0000313|Proteomes:UP000199114};
RN   [1] {ECO:0000313|Proteomes:UP000199114}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25055 {ECO:0000313|Proteomes:UP000199114};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-nicotinamide D-ribonucleotide + H(+) =
CC         diphosphate + NAD(+); Xref=Rhea:RHEA:21360, ChEBI:CHEBI:14649,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57540; EC=2.7.7.1; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00243};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC       nicotinamide D-ribonucleotide: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_00243}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00243}.
CC   -!- SIMILARITY: Belongs to the archaeal NMN adenylyltransferase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00243}.
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DR   EMBL; FOFD01000006; SER61233.1; -; Genomic_DNA.
DR   UniPathway; UPA00253; UER00600.
DR   Proteomes; UP000199114; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02166; NMNAT_Archaea; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00243; NMN_adenylyltr; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR006418; NMN_Atrans_arc.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   TIGRFAMs; TIGR01527; arch_NMN_Atrans; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00243};
KW   Complete proteome {ECO:0000313|Proteomes:UP000199114};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00243};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00243};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00243};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00243,
KW   ECO:0000313|EMBL:SER61233.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00243};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199114};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00243,
KW   ECO:0000313|EMBL:SER61233.1}.
FT   DOMAIN       34    161       CTP_transf_like. {ECO:0000259|Pfam:
FT                                PF01467}.
SQ   SEQUENCE   201 AA;  22408 MW;  964A8A01B878EB01 CRC64;
     MWESGTSDAE LADGGELATL KRRARAVSGM TRGFYIGRFQ PFHNGHRSMV ERIAEDVDEL
     VLGIGSADDS HTIRNPFTAG ERIMMITKSL VDFDLVTYAV PIEDLERNSV WVSHVQSMSP
     DFDIAYSNNP LVIQLFREAG IDIRQSPMFN RDVLEGSEVR ERMINDGDWE SLVPEAVVEV
     VDEIGGIERI QMVSGSDSNG E
//
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