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

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

Gene

sucC

Organism
Rhizobium loti (strain MAFF303099) (Mesorhizobium loti)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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 annotation

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 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), 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 functionLigase
Biological processTricarboxylic acid cycle
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00223; 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 annotation
Ordered Locus Names:mll4306
OrganismiRhizobium loti (strain MAFF303099) (Mesorhizobium loti)
Taxonomic identifieri266835 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium
Proteomesi
  • UP000000552 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001028461 – 397Succinate--CoA ligase [ADP-forming] subunit betaAdd BLAST397

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta subunits.UniRule annotation

Protein-protein interaction databases

STRINGi266835.mll4306.

Structurei

3D structure databases

ProteinModelPortaliQ98EC5.
SMRiQ98EC5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 254ATP-graspUniRule annotationAdd BLAST246

Region

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

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CMV. Bacteria.
COG0045. LUCA.
HOGENOMiHOG000007059.
KOiK01903.
OMAiLCMDAKF.
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.

Q98EC5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNIHEYQGKA LLKSFGAPVA EGVPVFKASE AEAAARALPG PLYVVKSQIH
60 70 80 90 100
AGGRGKGKFK ELSPDAKGGV RLAKSVADVV ANANEMLGHT LVTKQTGPAG
110 120 130 140 150
KQVNRLYIED GADIERELYL SILVDRSVGR IAFVVSTEGG MDIEAVAHDT
160 170 180 190 200
PEKVITVAID PERGVTADDV KKLNAALKLD GDAAKDGGTL FPILYKAFIE
210 220 230 240 250
KDMSLLEVNP LIVMKNGRLR VLDAKVSFDN NALFRHPDVL ELRDTTEEDE
260 270 280 290 300
KEIEASKYDL AYVALDGNIG CMVNGAGLAM ATMDIIKLYG AEPANFLDVG
310 320 330 340 350
GGASKEKVTA AFKIITKDPA VKGILINIFG GIMKCDIIAE GVIAAVKEVG
360 370 380 390
LEVPLVVRLE GTNAELGKKI INDSGLNVVS ADDLDDAAKK IVAAVKG
Length:397
Mass (Da):42,032
Last modified:October 1, 2001 - v1
Checksum:i0F3AD3AA57FFE781
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000012 Genomic DNA. Translation: BAB50995.1.
RefSeqiWP_010912337.1. NC_002678.2.

Genome annotation databases

EnsemblBacteriaiBAB50995; BAB50995; BAB50995.
KEGGimlo:mll4306.
PATRICifig|266835.9.peg.3399.

Similar proteinsi

Entry informationi

Entry nameiSUCC_RHILO
AccessioniPrimary (citable) accession number: Q98EC5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: October 1, 2001
Last modified: June 7, 2017
This is version 98 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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