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P08633

- NODM_RHILV

UniProt

P08633 - NODM_RHILV

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Protein

Glutamine--fructose-6-phosphate aminotransferase [isomerizing]

Gene

nodM

Organism
Rhizobium leguminosarum bv. viciae
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Involved in the production of the root hair deformation (HAD) factor specifically on medicago.

Catalytic activityi

L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21Nucleophile; for GATase activityBy similarity
Active sitei603 – 6031For Fru-6P isomerization activityBy similarity

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. glutamine-fructose-6-phosphate transaminase (isomerizing) activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. carbohydrate biosynthetic process Source: InterPro
  2. glutamine metabolic process Source: UniProtKB-HAMAP
  3. nodulation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Nodulation

Protein family/group databases

MEROPSiC44.971.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] (EC:2.6.1.16)
Short name:
GFAT
Alternative name(s):
Nodulation protein M
Gene namesi
Name:nodM
Encoded oniPlasmid sym pRL1JI0 Publication
OrganismiRhizobium leguminosarum bv. viciae
Taxonomic identifieri387 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 608607Glutamine--fructose-6-phosphate aminotransferase [isomerizing]PRO_0000135436Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP08633.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 217216Glutamine amidotransferase type-2Add
BLAST
Domaini283 – 422140SIS 1Add
BLAST
Domaini456 – 598143SIS 2Add
BLAST

Sequence similaritiesi

Contains 2 SIS domains.Curated

Keywords - Domaini

Glutamine amidotransferase, Repeat

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_00164. GlmS.
InterProiIPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR005855. GlmS_trans.
IPR029055. Ntn_hydrolases_N.
IPR001347. SIS.
[Graphical view]
PANTHERiPTHR10937:SF0. PTHR10937:SF0. 1 hit.
PfamiPF00310. GATase_2. 1 hit.
PF01380. SIS. 2 hits.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR01135. glmS. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
PS51464. SIS. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08633-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MCGIVGIVGH KPVSERLIEA LGRLEYRGYD SSGVATIFEG ELHRRRAEGK
60 70 80 90 100
LGNLKTRLKE APLSGTVGIA HTRWATHGAP TECNAHPHFT DGVAVVHNGI
110 120 130 140 150
IENFSKLKDA LAEVGTKFQT DTDTEVIAHL LTKFRRDGMG CLEAMHAMLK
160 170 180 190 200
CVEGAFALAI LFEDDPATIM VARNGPPLVI GHGDGEMFLG SDAIALAPFT
210 220 230 240 250
NDITYLNDGD WAVVGKTSVQ VFDIEGNVVT RPRHISLATA DLVGKGNHPH
260 270 280 290 300
FMEKEIYEQP EVIARALGHY INVNDSHVTT TSTDIDFAGV ESLAISACGT
310 320 330 340 350
AYLAGLIGKY WFERYARLIV EIDVASEFRY REIPLSPRSA ALFISQSGET
360 370 380 390 400
ADTLASLRYC KAHGLRIGAV VNTRESTMAR EADAIFPILA GPEIGVASTK
410 420 430 440 450
AFTCQLAVLA ALRIGAGKAR GTITDDEEQV LVQSLATLPG VMRQVLNDIT
460 470 480 490 500
PEIELLSREL SHYRDVLYLG RGTSFPLAME GALKLKEVSY IHAEGYAAGE
510 520 530 540 550
LKHGPIALID ENMPVIVIAP HDRFFDKTVS NMQEVAARGG RIILITDETG
560 570 580 590 600
ASMSKLPTMH TIVLPDVAEI IAPMIFSLPL QLLAYHTAVV MGADVDQPRN

LAKSVTVE
Length:608
Mass (Da):65,794
Last modified:January 23, 2007 - v3
Checksum:i8D2DEF05E0A70E70
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00548 Genomic DNA. Translation: CAA68626.1.
PIRiS01040.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00548 Genomic DNA. Translation: CAA68626.1 .
PIRi S01040.

3D structure databases

ProteinModelPortali P08633.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C44.971.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
HAMAPi MF_00164. GlmS.
InterProi IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR005855. GlmS_trans.
IPR029055. Ntn_hydrolases_N.
IPR001347. SIS.
[Graphical view ]
PANTHERi PTHR10937:SF0. PTHR10937:SF0. 1 hit.
Pfami PF00310. GATase_2. 1 hit.
PF01380. SIS. 2 hits.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
TIGRFAMsi TIGR01135. glmS. 1 hit.
PROSITEi PS51278. GATASE_TYPE_2. 1 hit.
PS51464. SIS. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Characterization of the Rhizobium leguminosarum genes nodLMN involved in efficient host-specific nodulation."
    Surin B.P., Downie J.A.
    Mol. Microbiol. 2:173-183(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 248.

Entry informationi

Entry nameiNODM_RHILV
AccessioniPrimary (citable) accession number: P08633
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 85 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Plasmid

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3