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
Actinomyces sp. oral taxon 178 str. F0338
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

Lacks conserved residue(s) required for the propagation of feature annotation.UniRule annotation
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 alpha (sucD), Succinate--CoA ligase [ADP-forming] subunit beta (sucC)
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 sitei49ATPUniRule annotation1
Binding sitei98ATP; via amide nitrogenUniRule annotation1
Binding sitei103ATPUniRule annotation1
Metal bindingi195MagnesiumUniRule annotation1
Metal bindingi209MagnesiumUniRule annotation1
Binding sitei260Substrate; shared with subunit alphaUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi56 – 58ATPUniRule 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

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 annotationImported
ORF Names:HMPREF9005_1925Imported
OrganismiActinomyces sp. oral taxon 178 str. F0338Imported
Taxonomic identifieri888051 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinomycetalesActinomycetaceaeActinomyces
Proteomesi
  • UP000003389 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 – 222ATP-graspInterPro annotationAdd BLAST214

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni321 – 323Substrate binding; shared with subunit alphaUniRule annotation3

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili370 – 390Sequence 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.

E8JK78-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLYEYQARE LFRKHGVPVL DFELATTPGQ ARDAAERLLG AGASLLVVKA
60 70 80 90 100
QVKTGGRGKA GGVKLARTPD EAREKAEAIL GLDIKGHVVE RLMIASGADI
110 120 130 140 150
AAEYYFSILL DRSNRRHLAM CSREGGMDIE TLAKERPEAL ARVPLDPAVG
160 170 180 190 200
IDADVARRIV DEAGFDRAAG EAIAPVLRTL WEVYRDEDAT LVEVNPLVAS
210 220 230 240 250
PDGSIWAVDG KVTLDDNARF RHPAHADLVD AAAQDPREAA AKEAGLNYVR
260 270 280 290 300
LEGQVGVIGN GAGLVMSTLD VVAMAGEDLR MRPANFLDIG GGASAAVMAK
310 320 330 340 350
GLGIILGDEQ VRSVFVNVFG GITACDEVAR GILGALEELG GAASKPLVVR
360 370 380 390
LDGNKVAEGR AILAAAGHPL VHLEETMDGA ARRAAELAAA SE
Length:392
Mass (Da):41,231
Last modified:April 5, 2011 - v1
Checksum:iE217722602DC791C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AEUH01000223 Genomic DNA Translation: EFW09065.1
RefSeqiWP_009400326.1, NZ_GL636935.1

Genome annotation databases

EnsemblBacteriaiEFW09065; EFW09065; HMPREF9005_1925

Similar proteinsi

Entry informationi

Entry nameiE8JK78_9ACTO
AccessioniPrimary (citable) accession number: E8JK78
Entry historyiIntegrated into UniProtKB/TrEMBL: April 5, 2011
Last sequence update: April 5, 2011
Last modified: March 28, 2018
This is version 45 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health