Skip Header

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

D-galactarolactone cycloisomerase

Gene

gci

Organism
Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the ring opening of D-galactaro-1,4-lactone to yield 5-keto-4-deoxy-D-glucarate (KDG) via a beta-elimination reaction. This is a step in the oxidative degradation pathway of D-galacturonate, which allows A.tumefaciens to utilize D-galacturonate as a sole carbon source. To a lesser extent, can also use D-glucaro-1,4-lactone as substrate to produce KDG, but cannot use D-galactaro-1,5-lactone, D-glucaro-6,3-lactone and linear D-glucarate.2 Publications

Catalytic activityi

D-glucaro-1,4-lactone = 5-dehydro-4-deoxy-D-glucarate.2 Publications
D-galactaro-1,4-lactone = 5-dehydro-4-deoxy-D-glucarate.2 Publications

Cofactori

Mg2+1 Publication

pH dependencei

Optimum pH is 8.5.1 Publication

Pathwayi: D-galacturonate degradation via prokaryotic oxidative pathway

This protein is involved in the pathway D-galacturonate degradation via prokaryotic oxidative pathway, which is part of Carbohydrate acid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway D-galacturonate degradation via prokaryotic oxidative pathway and in Carbohydrate acid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi194 – 1941Magnesium
Metal bindingi220 – 2201Magnesium
Metal bindingi246 – 2461Magnesium
Sitei269 – 2691Increases basicity of active site HisBy similarity
Active sitei296 – 2961Proton acceptorBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciAGRO:ATU3139-MONOMER.
UniPathwayiUPA01050.

Names & Taxonomyi

Protein namesi
Recommended name:
D-galactarolactone cycloisomerase (EC:5.5.1.272 Publications)
Gene namesi
Name:gci
Ordered Locus Names:Atu3139
OrganismiAgrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Taxonomic identifieri176299 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacteriumAgrobacterium tumefaciens complex
Proteomesi
  • UP000000813 Componenti: Chromosome linear

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 378378D-galactarolactone cycloisomerasePRO_0000429433Add
BLAST

Interactioni

Subunit structurei

Homooctamer.2 Publications

Protein-protein interaction databases

STRINGi176299.Atu3139.

Structurei

Secondary structure

1
378
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 2018Combined sources
Beta strandi25 – 3814Combined sources
Beta strandi43 – 486Combined sources
Helixi52 – 6312Combined sources
Turni64 – 685Combined sources
Helixi74 – 8411Combined sources
Helixi85 – 884Combined sources
Helixi93 – 11321Combined sources
Helixi117 – 1204Combined sources
Beta strandi127 – 1348Combined sources
Helixi144 – 15714Combined sources
Beta strandi161 – 1666Combined sources
Helixi171 – 18515Combined sources
Turni186 – 1883Combined sources
Beta strandi189 – 1946Combined sources
Helixi201 – 21111Combined sources
Helixi212 – 2143Combined sources
Beta strandi217 – 2204Combined sources
Helixi228 – 23710Combined sources
Beta strandi238 – 2403Combined sources
Beta strandi242 – 2443Combined sources
Helixi250 – 25910Combined sources
Beta strandi264 – 2663Combined sources
Turni270 – 2745Combined sources
Helixi275 – 28915Combined sources
Helixi301 – 31313Combined sources
Beta strandi328 – 3314Combined sources
Helixi337 – 3404Combined sources
Beta strandi342 – 3443Combined sources
Beta strandi352 – 3543Combined sources
Beta strandi358 – 3603Combined sources
Helixi367 – 3726Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GGBX-ray2.00A1-378[»]
4HPNX-ray1.60A1-378[»]
ProteinModelPortaliA9CEQ8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CXK. Bacteria.
COG4948. LUCA.
HOGENOMiHOG000113756.
KOiK18983.
OMAiFAPHLWA.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
InterProiIPR029065. Enolase_C-like.
IPR029017. Enolase_N-like.
IPR018110. Mandel_Rmase/mucon_lact_enz_CS.
IPR013342. Mandelate_racemase_C.
IPR013341. Mandelate_racemase_N_dom.
IPR001354. MR/MLE/MAL.
[Graphical view]
PANTHERiPTHR13794. PTHR13794. 1 hit.
PfamiPF13378. MR_MLE_C. 1 hit.
PF02746. MR_MLE_N. 1 hit.
[Graphical view]
SMARTiSM00922. MR_MLE. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
PROSITEiPS00908. MR_MLE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A9CEQ8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKITAVRTHL LEHRLDTPFE SASMRFDRRA HVLVEIECDD GTVGWGECLG
60 70 80 90 100
PARPNAAVVQ AYSGWLIGQD PRQTEKIWAV LYNALRDQGQ RGLSLTALSG
110 120 130 140 150
IDIALWDIKG KHYGASISML LGGRWRESVR AYATGSFKRD NVDRVSDNAS
160 170 180 190 200
EMAERRAEGF HACKIKIGFG VEEDLRVIAA VREAIGPDMR LMIDANHGYT
210 220 230 240 250
VTEAITLGDR AAGFGIDWFE EPVVPEQLDA YARVRAGQPI PVAGGETWHG
260 270 280 290 300
RYGMWQALSA GAVDILQPDL CGCGGFSEIQ KIATLATLHG VRIVPHVWGT
310 320 330 340 350
GVQIAAALQF MAAMTPDPVR VNPIEPIMEF DRTHNPFRQA VLREPLEAVN
360 370
GVVTIPDGPG LGIEINRDAL TEFRMPDP
Length:378
Mass (Da):41,456
Last modified:January 15, 2008 - v1
Checksum:i3B4EC2C7877DDCD6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE007870 Genomic DNA. Translation: AAK90247.1.
PIRiAE2942.
E98340.
RefSeqiNP_357462.1. NC_003063.2.
WP_010972789.1. NC_003063.2.

Genome annotation databases

EnsemblBacteriaiAAK90247; AAK90247; Atu3139.
GeneIDi1134941.
KEGGiatu:Atu3139.
PATRICi20815744. VBIAgrTum91616_2984.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE007870 Genomic DNA. Translation: AAK90247.1.
PIRiAE2942.
E98340.
RefSeqiNP_357462.1. NC_003063.2.
WP_010972789.1. NC_003063.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GGBX-ray2.00A1-378[»]
4HPNX-ray1.60A1-378[»]
ProteinModelPortaliA9CEQ8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi176299.Atu3139.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK90247; AAK90247; Atu3139.
GeneIDi1134941.
KEGGiatu:Atu3139.
PATRICi20815744. VBIAgrTum91616_2984.

Phylogenomic databases

eggNOGiENOG4105CXK. Bacteria.
COG4948. LUCA.
HOGENOMiHOG000113756.
KOiK18983.
OMAiFAPHLWA.

Enzyme and pathway databases

UniPathwayiUPA01050.
BioCyciAGRO:ATU3139-MONOMER.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
InterProiIPR029065. Enolase_C-like.
IPR029017. Enolase_N-like.
IPR018110. Mandel_Rmase/mucon_lact_enz_CS.
IPR013342. Mandelate_racemase_C.
IPR013341. Mandelate_racemase_N_dom.
IPR001354. MR/MLE/MAL.
[Graphical view]
PANTHERiPTHR13794. PTHR13794. 1 hit.
PfamiPF13378. MR_MLE_C. 1 hit.
PF02746. MR_MLE_N. 1 hit.
[Graphical view]
SMARTiSM00922. MR_MLE. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
PROSITEiPS00908. MR_MLE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGCI_AGRFC
AccessioniPrimary (citable) accession number: A9CEQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 11, 2014
Last sequence update: January 15, 2008
Last modified: September 7, 2016
This is version 56 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.