Gene Details


gene name: guaA


locus tag k12ECK2503 Crenarchaeota Euryarchaeota Nanoarcheota Alphaproteobacteria Betaproteobacteria Gammaproteobacteria Deltaproteobacteria Epsilonproteobacteria Cyanobacteria Actinobacteridae Firmicutes Spirochaetes others Protist Microsporidia Fungi Metazoa Plantae
information on phylogenetic profile
locus tag mg1655b2507
locus tag w3110JW2491
gene name k12guaA
locus nameguaA
synonyms of locus name

scop id52317; 52402
superfamilyClass I glutamine amidotransferase-like; Adenine nucleotide alpha hydrolases
pfam idPF00117; PF00958
pfam domainGlutamine amidotransferase class-I; GMP synthase C terminal domain
tigrfam idTIGR00888; TIGR00884
nameguaA_Nterm; guaA_Cterm
functionGMP synthase, N-terminal domai; GMP synthase, C-terminal domai

swissprot nameGUAA_ECOLI
descriptionGMP synthase [glutamine-hydrolyzing] (EC 6.3.5.2) (Glutamine|amidotransferase) (GMP synthetase) (GMPS).
seq length525
fastaseq

go idGO:0005737; GO:0015949; GO:0006164; GO:0006164; GO:0015949; GO:0006164
go termcytoplasm; nucleobase, nucleoside and nucleotide interconversion; purine nucleotide biosynthesis; purine nucleotide biosynthesis; nucleobase, nucleoside and nucleotide interconversion; purine nucleotide biosynth

gene product descriptionGMP synthetase (glutamine aminotransferase)
comment gene product description
evidenceE
context
gene product descEnzyme
cell locationCytoplasmic
featuresCDS

functional category codeF
functional categoryNucleotide transport and metabolism

reference #1Nucleotide sequence of the guaA gene encoding GMP synthetase of Escherichia coli K12.

Tiedeman A., Smith J., Zalkin H. (J Biol Chem. 1985 Jul 25; 260(15):8676-9)
reference #2Identification of a trpG-related glutamine amide transfer domain in Escherichia coli GMP synthetase.

Zalkin H., Argos P., Narayana S., Tiedeman A., Smith J. (J Biol Chem. 1985 Mar 25; 260(6):3350-4)
reference #3Nucleotide sequence of the guaA gene encoding GMP synthetase of Escherichia coli K12.

Tiedeman A., Smith J., Zalkin H. (J Biol Chem. 1985 Jul 25; 260(15):8676-9)
reference #4The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families.

Tesmer J., Klem T., Deras M., Davisson V., Smith J. (Nat Struct Biol. 1996 Jan; 3(1):74-86)

phylogenetic profile
 
400 419 176 169 268 240 283 320 281 296 259 265 248 298 305 302 266 272 1 484
453 461 463 469 468 447 468 468 466 481 498 493 545 429 427 572 574 575 584 499
586 568 579 573 1 1 1 586 452 671 668 668 674 671 694 691 692 695 665 530
528 529 527 528 538 537 538 497 559 551 652 537 357 491 496 537 552 553 553 554
553 536 527 549 549 544 544 538 545 543 538 541 538 540 86 1 50 1 1 454
1 1 554 1 533 533 533 533 533 543 543 518 533 533 525 525 525 521 521 552
1 715 588 54 1 1 687 965 1060 1051 1060 839 741 742 830 770 839 934 768 763
776 1053 1047 1053 895 1059 1059 869 870 862 540 759 760 729 737 944 944 946 560 544
534 272 272 272 519 1 523 537 513 573 1 579 546 509 483 489 295 511 1 219
515 504 515 511 444 513 484 514 282 273 279 278 283 280 1 463 523 242 445