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A1KW75

- A1KW75_NEIMF

UniProt

A1KW75 - A1KW75_NEIMF

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Protein

Phosphoribosylformylglycinamidine synthase

Gene

purL

Organism
Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate.UniRule annotationSAAS annotation

Catalytic activityi

ATP + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O = ADP + phosphate + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate.UniRule annotationSAAS annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei683 – 6831ATP; via carbonyl oxygenUniRule annotation
Metal bindingi684 – 6841MagnesiumUniRule annotation
Metal bindingi723 – 7231MagnesiumUniRule annotation
Metal bindingi727 – 7271MagnesiumUniRule annotation
Metal bindingi889 – 8891MagnesiumUniRule annotation
Binding sitei891 – 8911ATPUniRule annotation
Active sitei1167 – 11671NucleophileUniRule annotation
Active sitei1290 – 12901UniRule annotation
Active sitei1292 – 12921UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi316 – 32712ATPUniRule annotationAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. metal ion binding Source: UniProtKB-KW
  3. phosphoribosylformylglycinamidine synthase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: UniProtKB-HAMAP
  2. glutamine metabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotationSAAS annotation

Keywords - Biological processi

Purine biosynthesisUniRule annotationSAAS annotation

Keywords - Ligandi

ATP-bindingUniRule annotationSAAS annotation, MagnesiumUniRule annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation, Nucleotide-binding

Enzyme and pathway databases

BioCyciNMEN272831:GJDX-1866-MONOMER.
UniPathwayiUPA00074; UER00128.

Protein family/group databases

MEROPSiC56.972.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoribosylformylglycinamidine synthaseUniRule annotationSAAS annotation (EC:6.3.5.3UniRule annotationSAAS annotation)
Short name:
FGAM synthaseUniRule annotation
Short name:
FGAMSUniRule annotation
Alternative name(s):
Formylglycinamide ribonucleotide amidotransferaseUniRule annotation
Gene namesi
Name:purLUniRule annotationImported
Ordered Locus Names:NMC1972Imported
OrganismiNeisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18)Imported
Taxonomic identifieri272831 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
ProteomesiUP000002286: Chromosome

Subcellular locationi

Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

Interactioni

Subunit structurei

Monomer.UniRule annotationSAAS annotation

Protein-protein interaction databases

STRINGi272831.NMC1972.

Structurei

3D structure databases

ProteinModelPortaliA1KW75.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Contains 1 glutamine amidotransferase type-1 domain.UniRule annotation
Contains glutamine amidotransferase type-1 domain.SAAS annotation
Contains glutamine amidotransferase type-domain.SAAS annotation
In the N-terminal section; belongs to the FGAMS family.UniRule annotation

Keywords - Domaini

Glutamine amidotransferaseUniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiCOG0046.
HOGENOMiHOG000261359.
KOiK01952.
OMAiGEGHAEF.
OrthoDBiEOG6FNHHR.

Family and domain databases

Gene3Di3.30.1330.10. 2 hits.
3.40.50.880. 1 hit.
HAMAPiMF_00419. PurL_1.
InterProiIPR010918. AIR_synth_C_dom.
IPR000728. AIR_synth_N_dom.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR010073. PRibForGlyAmidine_synth.
IPR022940. PRibForGlyAmidine_synth_bac.
IPR016188. PurM_N-like.
[Graphical view]
PfamiPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 2 hits.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
SSF55326. SSF55326. 2 hits.
SSF56042. SSF56042. 3 hits.
TIGRFAMsiTIGR01735. FGAM_synt. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A1KW75-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRAESMSVVL PLRGVTALSD FRVEKLLQKA AALGLPEVKL SSEFWYFAGS
60 70 80 90 100
EKALDAATVE KLQALLAAQS VEQTPKAREG LHLFLVTPRL GTISPWASKA
110 120 130 140 150
TNIAENCGLA GIERIERGMA VWLEGALTDE QKQQWAALLH DRMTESVLPD
160 170 180 190 200
FQTASKLFHH LESETFSTVD VLGGGKEALV KANTEMGLAL SADEIDYLVE
210 220 230 240 250
NYQALQRNPS DVELMMFAQA NSEHCRHKIF NADFILNGEK QPKSLFGMIR
260 270 280 290 300
DTHNAHPEGT VVAYKDNSSV IEGAKIERFY PNAAENQGYR FHEEDTHIIM
310 320 330 340 350
KVETHNHPTA IAPFAGAATG AGGEIRDEGA TGKGSRPKAG LTGFTVSNLN
360 370 380 390 400
IPGLKQPWEQ DYGKPEHISS PLDIMIEGPI GGAAFNNEFG RPNLLGYFRT
410 420 430 440 450
FEEKFDGQVR GYHKPIMIAG GLGSIQAQQT HKDEIPEGAL LIQLGGPGML
460 470 480 490 500
IGLGGGAASS MDTGTNDASL DFNSVQRGNP EIERRAQEVI DRCWQLGDKN
510 520 530 540 550
PIISIHDVGA GGLSNAFPEL VNDAGRGAVF ELREVPLEEH GLTPLQIWCN
560 570 580 590 600
ESQERYVLSI LEKDLDTFRA ICERERCPFA VVGTATDDGH LKVRDDLFAN
610 620 630 640 650
NPIDLPLNVL LGKPPKTTRT DKTVTPSKKP FHADDIDITE AAYRVLHLPA
660 670 680 690 700
VAAKNFLITI GDRSVGGMTH RDQMVGKYQT PVADCAVTMM GFNTYRGEAM
710 720 730 740 750
SMGEKPTVAL FDAPASGRMC VGEAITNIAA VNIGDIGNIK LSANWMAACG
760 770 780 790 800
NEGEDEKLYR TVEAVSKACQ ALDLSIPVGK DSLSMKTVWQ DGEEKKSVVS
810 820 830 840 850
PLSLIISAFA PVQDVRKTVT PELKNVEDSV LLFVDLGFGK ARMGGSAFGQ
860 870 880 890 900
VYNNMSGDAP DLDDTGRLKA FYNVIQQLVA EDKLLAYHDR SDGGLFAVLV
910 920 930 940 950
EMAFAGRCGL DIDLNLLLAQ TFITNHTALS QSLRTEEVKA LAEWQETIAR
960 970 980 990 1000
TLFNEELGAV IQVRKQDVAD IINLFYQQQL HHNVFEIGTL TDENTLIIRD
1010 1020 1030 1040 1050
GQTHLISDNL IKLQQTWQET SHQIQRLRDN PACADSEFAL IGDNDRSALF
1060 1070 1080 1090 1100
ANLKFDVNED IAAPFINSGA KPKIAILREQ GVNGQIEMAA AFTRAGFDAY
1110 1120 1130 1140 1150
DVHMSDLMAG RFRLADFKML AACGGFSYGD VLGAGEGWAK SILFHPALRD
1160 1170 1180 1190 1200
QFAAFFADPD TLTLGVCNGC QMVSNLAEII PGAEAWPKFK RNLSEQFEAR
1210 1220 1230 1240 1250
LSMVHVPKSA SLILNEMQGS SLPVVVSHGE GRADFALHGG NISADLGIAL
1260 1270 1280 1290 1300
QYVDGQNQVT QTYPLNPNGS PQGIAGVTNA DGRVTIMMPH PERVYRAAQM
1310 1320
SWKPEDWTEL SGWYRLFAGA RKALG
Length:1,325
Mass (Da):144,502
Last modified:February 6, 2007 - v1
Checksum:iC2C446817EF39BDA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM421808 Genomic DNA. Translation: CAM11131.1.
RefSeqiYP_975899.1. NC_008767.1.

Genome annotation databases

EnsemblBacteriaiCAM11131; CAM11131; NMC1972.
GeneIDi4676582.
KEGGinmc:NMC1972.
PATRICi20354458. VBINeiMen17609_2457.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM421808 Genomic DNA. Translation: CAM11131.1 .
RefSeqi YP_975899.1. NC_008767.1.

3D structure databases

ProteinModelPortali A1KW75.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272831.NMC1972.

Protein family/group databases

MEROPSi C56.972.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAM11131 ; CAM11131 ; NMC1972 .
GeneIDi 4676582.
KEGGi nmc:NMC1972.
PATRICi 20354458. VBINeiMen17609_2457.

Phylogenomic databases

eggNOGi COG0046.
HOGENOMi HOG000261359.
KOi K01952.
OMAi GEGHAEF.
OrthoDBi EOG6FNHHR.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00128 .
BioCyci NMEN272831:GJDX-1866-MONOMER.

Family and domain databases

Gene3Di 3.30.1330.10. 2 hits.
3.40.50.880. 1 hit.
HAMAPi MF_00419. PurL_1.
InterProi IPR010918. AIR_synth_C_dom.
IPR000728. AIR_synth_N_dom.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR010073. PRibForGlyAmidine_synth.
IPR022940. PRibForGlyAmidine_synth_bac.
IPR016188. PurM_N-like.
[Graphical view ]
Pfami PF00586. AIRS. 1 hit.
PF02769. AIRS_C. 2 hits.
[Graphical view ]
SUPFAMi SSF52317. SSF52317. 1 hit.
SSF55326. SSF55326. 2 hits.
SSF56042. SSF56042. 3 hits.
TIGRFAMsi TIGR01735. FGAM_synt. 1 hit.
PROSITEi PS51273. GATASE_TYPE_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700532 / DSM 15464 / FAM18Imported.

Entry informationi

Entry nameiA1KW75_NEIMF
AccessioniPrimary (citable) accession number: A1KW75
Entry historyi
Integrated into UniProtKB/TrEMBL: February 6, 2007
Last sequence update: February 6, 2007
Last modified: November 26, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Miscellaneous

In Gram-negative bacteria and most eukaryotes, FGAM synthase is only formed by PurL, a single polypeptide of 140 kDa (large PurL). However in Gram-positive bacteria and archaebacteria, phosphoribosylformylglycinamidine synthase is composed of three separate proteins: PurL (small PurL), PurQ and PurS.UniRule annotation

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3