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Protein

Succinate--CoA ligase [ADP-forming] subunit beta

Gene

sucC

Organism
Agrobacterium tumefaciens str. Cherry 2E-2-2
Status
Unreviewed-Annotation score: -Protein inferred from homologyi

Functioni

Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.UniRule annotationSAAS annotation

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

Catalytic activityi

ATP + succinate + CoA = ADP + phosphate + succinyl-CoA.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Pathwayi: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes succinate from succinyl-CoA (ligase route).UniRule annotationSAAS annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Succinate--CoA ligase [ADP-forming] subunit beta (sucC), Succinate--CoA ligase [ADP-forming] subunit alpha (sucD)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes succinate from succinyl-CoA (ligase route), the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei46ATPUniRule annotation1
Binding sitei109ATPUniRule annotation1
Binding sitei112ATP; via amide nitrogenUniRule annotation1
Binding sitei117ATPUniRule annotation1
Metal bindingi209MagnesiumUniRule annotation1
Metal bindingi223MagnesiumUniRule annotation1
Binding sitei274Substrate; shared with subunit alphaUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi53 – 55ATPUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigaseUniRule annotationSAAS annotationImported
Biological processTricarboxylic acid cycleUniRule annotationSAAS annotation
LigandATP-bindingUniRule annotation, MagnesiumUniRule annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation, Nucleotide-binding

Enzyme and pathway databases

UniPathwayi
UPA00223;UER00999

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate--CoA ligase [ADP-forming] subunit betaUniRule annotation (EC:6.2.1.5UniRule annotation)
Alternative name(s):
Succinyl-CoA synthetase subunit betaUniRule annotation
Short name:
SCS-betaUniRule annotation
Gene namesi
Name:sucCUniRule annotationImported
ORF Names:H009_19669Imported
OrganismiAgrobacterium tumefaciens str. Cherry 2E-2-2Imported
Taxonomic identifieri1281779 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacteriumAgrobacterium tumefaciens complex
Proteomesi
  • UP000012074 Componenti: Unassembled WGS sequence

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta subunits.UniRule annotationSAAS annotation

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 237ATP-graspInterPro annotationAdd BLAST229

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni331 – 333Substrate binding; shared with subunit alphaUniRule annotation3

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili236 – 256Sequence analysisAdd BLAST21

Sequence similaritiesi

Belongs to the succinate/malate CoA ligase beta subunit family.UniRule annotationSAAS annotation

Keywords - Domaini

Coiled coilSequence analysis

Phylogenomic databases

OrthoDBiPOG091H050Y

Family and domain databases

Gene3Di3.30.1490.20, 1 hit
3.40.50.261, 1 hit
HAMAPiMF_00558 Succ_CoA_beta, 1 hit
InterProiView protein in InterPro
IPR011761 ATP-grasp
IPR013650 ATP-grasp_succ-CoA_synth-type
IPR013815 ATP_grasp_subdomain_1
IPR005811 CoA_ligase
IPR017866 Succ-CoA_synthase_bsu_CS
IPR005809 Succ_CoA_synthase_bsu
IPR016102 Succinyl-CoA_synth-like
PANTHERiPTHR11815 PTHR11815, 1 hit
PfamiView protein in Pfam
PF08442 ATP-grasp_2, 1 hit
PF00549 Ligase_CoA, 1 hit
PIRSFiPIRSF001554 SucCS_beta, 1 hit
SUPFAMiSSF52210 SSF52210, 1 hit
TIGRFAMsiTIGR01016 sucCoAbeta, 1 hit
PROSITEiView protein in PROSITE
PS50975 ATP_GRASP, 1 hit
PS01217 SUCCINYL_COA_LIG_3, 1 hit

Sequencei

Sequence statusi: Complete.

M8B963-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNIHEYQAKA LLKGYGAPVA EGVAILKVEE AEAAAKQLPG PLYVVKSQIH
60 70 80 90 100
AGGRGKGKFK ELGPDAKGGV RLAKSIDEVV SHAKDMLGNT LVTAQTGEVG
110 120 130 140 150
KQVNRLYIED GADIARELYC SLLVDRSVGQ VAFVVSTEGG MDIEAVAHDT
160 170 180 190 200
PEKIHTIAIN PEKGVSDADV AAISKALALD GVAAEDAKAL FPILYKAFNE
210 220 230 240 250
KDMALLEVNP LIVMENGHLR VLDAKMSFDG NALFRHDDVK ALRDETEEDA
260 270 280 290 300
KEIEASKWDL AYVALDGNIG CMVNGAGLAM ATMDIIKLYG KEPANFCDVG
310 320 330 340 350
GGAGKEKVAA AFKIITADPK VEGILVNIFG GIMKCDVIAE GVIAAVKEVG
360 370 380 390
LQVPLVVRLE GTNVELGKKL LNESGLAITA ADDLDDAAKK IVAAING
Length:397
Mass (Da):41,811
Last modified:May 29, 2013 - v1
Checksum:i75D37FB5D0DC7BAA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
APCC01000061 Genomic DNA Translation: EMS95965.1
RefSeqiWP_003523514.1, NZ_APCC01000061.1

Genome annotation databases

EnsemblBacteriaiEMS95965; EMS95965; H009_19669
PATRICifig|1281779.3.peg.4061

Similar proteinsi

Entry informationi

Entry nameiM8B963_RHIRD
AccessioniPrimary (citable) accession number: M8B963
Entry historyiIntegrated into UniProtKB/TrEMBL: May 29, 2013
Last sequence update: May 29, 2013
Last modified: March 28, 2018
This is version 37 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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