Q03638 (NADE_RHOCA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamine-dependent NAD(+) synthetase
EC=6.3.5.1

Alternative name(s):
NAD(+) synthase [glutamine-hydrolyzing]

Gene names

Name:	nadE
Synonyms:	adgA

Organism

Rhodobacter capsulatus (Rhodopseudomonas capsulata)

Taxonomic identifier

1061 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length	552 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	It is not known if this NAD synthase uses NH3 or glutamine as the N donor. HAMAP-Rule MF_00193
Catalytic activity	ATP + deamido-NAD+ + L-glutamine + H2O = AMP + diphosphate + NAD+ + L-glutamate. HAMAP-Rule MF_00193
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (L-Gln route): step 1/1. HAMAP-Rule MF_00193
Sequence similarities	In the C-terminal section; belongs to the NAD synthetase family. Contains 1 CN hydrolase domain.

Ontologies

Keywords
Ligand	ATP-binding NAD Nucleotide-binding
Molecular function	Ligase
Gene Ontology (GO)
Biological_process	NAD biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW NAD+ synthase (glutamine-hydrolyzing) activity Inferred from electronic annotation. Source: EC hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 552	552	Glutamine-dependent NAD(+) synthetase HAMAP-Rule MF_00193		PRO_0000152243
Regions
	Domain	5 – 274	270	CN hydrolase
	Nucleotide binding	290 – 297	8	ATP By similarity
	Region	275 – 552	278	Ligase HAMAP-Rule MF_00193
Sites
	Active site	292	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q03638 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 5791E11F29DB0308	FASTA	552	59,706
	10 20 30 40 50 60 MTDRFRITLA QLNPTVGALA ANAEKAMAAW QAGRAAGADL VALPEMFLTG YQTQDLVLKP 70 80 90 100 110 120 AFLRDAMAAM AALAAQVVDG PALGIGGPYV DETGSYNAWW VLKDGRVIAR ALKHHLPHDD 130 140 150 160 170 180 VFDEMRLFDQ GPVSDPLRLG PVALGVPVCE DAWHPDVAGA LAAAGAEVLM VPNGSPYRRG 190 200 210 220 230 240 KLDLRRQVTG ARVAETGLPL LYLNMVGGQD DQLFDGASFV LNPDGSVAVQ LPAFEEAVVH 250 260 270 280 290 300 VDLERGAADW RAVPADIVAP PGDIEQDYRA MVLGLQDYLR KSGFSRVVLG LSGGIDSALV 310 320 330 340 350 360 AVIAADALGA GNVHCVMLPS RYTSQGSLDD AADLARRLGA RLDTVEIEGP RAAVEGALAH 370 380 390 400 410 420 VLAGTAPDVT EENIQSRLRG VILMAISNKF GAMLLTTGNK SEVAVGYCTI YGDMAGGYNP 430 440 450 460 470 480 LKDLYKTRVF ETCRWRNATH RPWMQAPAGE IIPVAIIDKP PSAELRENQT DQDSLPPYEV 490 500 510 520 530 540 LDAILERLVE GDQSVDQIVA AGFDRATVKR IEHLLYISEW KRFQSAPGPR LTTRAFWLDR 550 RYPMVNRWRD QS

References

[1]	"Biochemical genetics revisited: the use of mutants to study carbon and nitrogen metabolism in the photosynthetic bacteria." Willison J.C. FEMS Microbiol. Rev. 10:1-38(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 33303 / B10.
[2]	"The Escherichia coli efg gene and the Rhodobacter capsulatus adgA gene code for NH3-dependent NAD synthetase." Willison J.C., Tissot G. J. Bacteriol. 176:3400-3402(1994) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X59399 Genomic DNA. Translation: CAA42042.1.
PIR	S15555.
3D structure databases
ProteinModelPortal	Q03638.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOGENOM	HOG000226694.
Enzyme and pathway databases
UniPathway	UPA00253; UER00334.
Family and domain databases
Gene3D	3.40.50.620. 1 hit. 3.60.110.10. 1 hit.
HAMAP	MF_00193. NadE. Fused.
InterPro	IPR003010. C-N_Hydrolase. IPR014445. Gln-dep_NAD_synthase. IPR022310. NAD/GMP_synthase. IPR003694. NAD_synthase. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Pfam	PF00795. CN_hydrolase. 1 hit. PF02540. NAD_synthase. 1 hit. [Graphical view]
PIRSF	PIRSF006630. NADS_GAT. 1 hit.
SUPFAM	SSF56317. Ntlse/CNhydtse. 1 hit.
TIGRFAMs	TIGR00552. nadE. 1 hit.
PROSITE	PS50263. CN_HYDROLASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NADE_RHOCA

Accession

Primary (citable) accession number: Q03638

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	April 3, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program