SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q5V3F0

- GMSS2_HALMA

UniProt

Q5V3F0 - GMSS2_HALMA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glutamate mutase sigma subunit 2

Gene
glmS2, mamA2, rrnAC0984
Organism
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate) By similarity.UniRule annotation

Catalytic activityi

L-threo-3-methylaspartate = L-glutamate.UniRule annotation

Cofactori

Adenosylcobalamin By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi14 – 141Cobalt (cobalamin axial ligand) By similarity

GO - Molecular functioni

  1. cobalamin binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. methylaspartate mutase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. anaerobic glutamate catabolic process Source: UniProtKB-HAMAP
  2. glutamate catabolic process via L-citramalate Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Cobalamin, Cobalt, Metal-binding

Enzyme and pathway databases

BioCyciHMAR272569:GJDH-879-MONOMER.
UniPathwayiUPA00561; UER00617.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate mutase sigma subunit 2 (EC:5.4.99.1)
Alternative name(s):
Glutamate mutase S chain 2
Glutamate mutase small subunit 2
Methylaspartate mutase 2
Gene namesi
Name:glmS2
Synonyms:mamA2
Ordered Locus Names:rrnAC0984
OrganismiHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Taxonomic identifieri272569 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula
ProteomesiUP000001169: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 148148Glutamate mutase sigma subunit 2UniRule annotationPRO_0000278196Add
BLAST

Interactioni

Subunit structurei

Heterotetramer composed of 2 epsilon subunits (GlmE) and 2 sigma subunits (GlmS). GlmE exists as a homodimer and GlmS as a monomer By similarity.

Protein-protein interaction databases

STRINGi272569.rrnAC0984.

Structurei

3D structure databases

ProteinModelPortaliQ5V3F0.
SMRiQ5V3F0. Positions 2-132.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 134134B12-bindingAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 155Adenosylcobalamin binding By similarity
Regioni59 – 613Adenosylcobalamin binding By similarity
Regioni90 – 945Adenosylcobalamin binding By similarity

Sequence similaritiesi

Contains 1 B12-binding domain.

Phylogenomic databases

eggNOGiCOG2185.
HOGENOMiHOG000011065.
KOiK01846.
OMAiMELLEHE.

Family and domain databases

Gene3Di3.40.50.280. 1 hit.
HAMAPiMF_00526. Me_Asp_mutase_S.
InterProiIPR006158. Cobalamin-bd.
IPR006394. Me_Asp_mutase.
[Graphical view]
PfamiPF02310. B12-binding. 1 hit.
[Graphical view]
SUPFAMiSSF52242. SSF52242. 1 hit.
TIGRFAMsiTIGR01501. MthylAspMutase. 1 hit.
PROSITEiPS51332. B12_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5V3F0-1 [UniParc]FASTAAdd to Basket

« Hide

MRTVILGVIG SDAHVVGITI LERAFEAAGF NVVNLGVQSS QSEFIDAADE    50
HDAEAILVSS LYGHAEQDCQ GFQQQINEAG LDVTTYIGGN LAVGQDSFEE 100
TRETFKALGF DRVFNSETDP EEAIEALKAD LGHRSREEAS SEKVQLGS 148
Length:148
Mass (Da):15,934
Last modified:December 7, 2004 - v1
Checksum:i75FFF20F6795D515
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY596297 Genomic DNA. Translation: AAV45952.1.
RefSeqiYP_135658.1. NC_006396.1.

Genome annotation databases

EnsemblBacteriaiAAV45952; AAV45952; rrnAC0984.
GeneIDi3130028.
KEGGihma:rrnAC0984.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY596297 Genomic DNA. Translation: AAV45952.1 .
RefSeqi YP_135658.1. NC_006396.1.

3D structure databases

ProteinModelPortali Q5V3F0.
SMRi Q5V3F0. Positions 2-132.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272569.rrnAC0984.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAV45952 ; AAV45952 ; rrnAC0984 .
GeneIDi 3130028.
KEGGi hma:rrnAC0984.

Phylogenomic databases

eggNOGi COG2185.
HOGENOMi HOG000011065.
KOi K01846.
OMAi MELLEHE.

Enzyme and pathway databases

UniPathwayi UPA00561 ; UER00617 .
BioCyci HMAR272569:GJDH-879-MONOMER.

Family and domain databases

Gene3Di 3.40.50.280. 1 hit.
HAMAPi MF_00526. Me_Asp_mutase_S.
InterProi IPR006158. Cobalamin-bd.
IPR006394. Me_Asp_mutase.
[Graphical view ]
Pfami PF02310. B12-binding. 1 hit.
[Graphical view ]
SUPFAMi SSF52242. SSF52242. 1 hit.
TIGRFAMsi TIGR01501. MthylAspMutase. 1 hit.
PROSITEi PS51332. B12_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.

Entry informationi

Entry nameiGMSS2_HALMA
AccessioniPrimary (citable) accession number: Q5V3F0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: December 7, 2004
Last modified: July 9, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi