P31002 (IMDH_ACICA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inosine-5'-monophosphate dehydrogenase
Short name=IMP dehydrogenase
Short name=IMPD
Short name=IMPDH
EC=1.1.1.205

Gene names

Name:

guaB

Organism

Acinetobacter calcoaceticus

Taxonomic identifier

471 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter › Acinetobacter calcoaceticus/baumannii complex

Protein attributes

Sequence length	488 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth By similarity. HAMAP-Rule MF_01964
Catalytic activity	Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH. HAMAP-Rule MF_01964
Cofactor	Potassium By similarity.
Enzyme regulation	Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH By similarity. HAMAP-Rule MF_01964
Pathway	Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. HAMAP-Rule MF_01964
Subunit structure	Homotetramer By similarity.
Sequence similarities	Belongs to the IMPDH/GMPR family. Contains 2 CBS domains.

Ontologies

Keywords
Biological process	GMP biosynthesis Purine biosynthesis
Domain	CBS domain Repeat
Ligand	Metal-binding NAD Potassium
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological_process	GMP biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	IMP dehydrogenase activity Inferred from electronic annotation. Source: HAMAP metal ion binding Inferred from electronic annotation. Source: HAMAP nucleotide binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 488	488	Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964		PRO_0000093688
Regions
	Domain	93 – 148	56	CBS 1
	Domain	152 – 210	59	CBS 2
	Nucleotide binding	297 – 299	3	NAD By similarity
	Region	336 – 338	3	IMP binding By similarity
	Region	359 – 360	2	IMP binding By similarity
	Region	383 – 387	5	IMP binding By similarity
Sites
	Active site	304	1	Thioimidate intermediate By similarity
	Metal binding	299	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	301	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	304	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	470	1	Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
	Metal binding	471	1	Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
	Metal binding	472	1	Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
	Binding site	247	1	NAD By similarity
	Binding site	302	1	IMP By similarity
	Binding site	416	1	IMP By similarity

Sequences

	Sequence		Length	Mass (Da)
	P31002 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 3DE0F8F9B5157A03	FASTA	488	51,530
	10 20 30 40 50 60 MLTIVQEALT FDDVLLLPAY STVLPKDVSL KTRLTRGIYL NIPLVSAAMD TVTESRMAIA 70 80 90 100 110 120 MAQNGGIGIL HKNMDIAAQA AEVRRVKKFE AGMVKDPITV SPETTVRELI AITSANNISG 130 140 150 160 170 180 VPVVKDSKVV GIVTGRDTRF ETNLEQPVSN IMTGQDRLVT VREGESKENI QALLQKHRIE 190 200 210 220 230 240 KVLVVGESNE LKGLITVTDF RKAESYPNSC KDDLGRLRVG AAVGTGADTP SRVEALVEAG 250 260 270 280 290 300 VDVIVVDTAH GHSAGVIERV RWVKQNFPQV QVIGGNIATG DAALALLDAG ADAVKVGIGP 310 320 330 340 350 360 GSICTTRIVA GIGMPQISAI DSVASALKDQ IPLIADGGIP FSGDMAKAIG AGASTIMVGS 370 380 390 400 410 420 LLAGTEEAPG EVEFFQGRYY KAYRGMGSLG AMAGRTGSAD RYFQDSKAGA EKLVPEGIEG 430 440 450 460 470 480 RVPYKGPMGN IVHQMMGGLR SSMGYTGSAV IEDLRQNAKF VKITSAGMSE SHVHDVTITK EAPNYRVG

References

[1]	Anderegg U., Schnuck W.H., Asperger O., Kleber H.-P. Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: EB 104.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X66859 Genomic DNA. Translation: CAA47328.1.
PIR	S23226.
3D structure databases
ProteinModelPortal	P31002.
SMR	P31002. Positions 4-486.
ModBase	Search...
Proteomic databases
PRIDE	P31002.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00601; UER00295.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_01964. IMPDH.
InterPro	IPR013785. Aldolase_TIM. IPR000644. Cysta_beta_synth_core. IPR005990. IMP_DH. IPR015875. IMP_DH/GMP_Rdtase_CS. IPR001093. IMP_DH_GMPRt. [Graphical view]
PANTHER	PTHR11911:SF6. PTHR11911:SF6. 1 hit.
Pfam	PF00571. CBS. 2 hits. PF00478. IMPDH. 1 hit. [Graphical view]
PIRSF	PIRSF000130. IMPDH. 1 hit.
SMART	SM00116. CBS. 2 hits. [Graphical view]
TIGRFAMs	TIGR01302. IMP_dehydrog. 1 hit.
PROSITE	PS51371. CBS. 2 hits. PS00487. IMP_DH_GMP_RED. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

IMDH_ACICA

Accession

Primary (citable) accession number: P31002

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	April 3, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program