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Protein

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

Gene

sucC

Organism
Halovivax ruber (strain DSM 18193 / JCM 13892 / XH-70)
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 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 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 sitei54ATPUniRule annotation1
Binding sitei100ATPUniRule annotation1
Binding sitei103ATP; via amide nitrogenUniRule annotation1
Binding sitei108ATPUniRule annotation1
Metal bindingi200MagnesiumUniRule annotation1
Metal bindingi214MagnesiumUniRule annotation1
Binding sitei266Substrate; shared with subunit alphaUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi61 – 63ATPUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigaseUniRule annotation
Biological processTricarboxylic acid cycleUniRule annotation
LigandATP-bindingUniRule annotation, MagnesiumUniRule annotation, Metal-bindingUniRule 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 annotation
Ordered Locus Names:Halru_1436Imported
OrganismiHalovivax ruber (strain DSM 18193 / JCM 13892 / XH-70)Imported
Taxonomic identifieri797302 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaNatrialbalesNatrialbaceaeHalovivax
Proteomesi
  • UP000010846 Componenti: Chromosome

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta subunits.UniRule annotation

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini18 – 230ATP-graspInterPro annotationAdd BLAST213

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni323 – 325Substrate binding; shared with subunit alphaUniRule annotation3

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili361 – 381Sequence analysisAdd BLAST21

Sequence similaritiesi

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

Keywords - Domaini

Coiled coilSequence analysis

Phylogenomic databases

KOiK01903
OMAiLCMDAKF
OrthoDBiPOG093Z04J4

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.

L0IDJ6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEVSDEFTM KLHEYQAKQV FADAGIPTPD SALASDVDGV LEAAADIGYP
60 70 80 90 100
VAIKAQVQVG GRGKAGGIEL VESDEEAREA AERIIGMDLK GIRVERVLVE
110 120 130 140 150
EAVDFTNELY VGVTMDRGEG KPVAMVSTKG GVNIEEVAEE DPDAIAREHI
160 170 180 190 200
DPSFGMQPYQ ARKVVFDAGV DRAVATDVAG VLSTLYDLWT SKDGSDAEIN
210 220 230 240 250
PLMVTADDEV VAADAVMNID EDALFRQPEI AEMGEEAAGG DELEQKADEY
260 270 280 290 300
GFDYVRLDGS VGIIGNGAGL VMTTLDLVDY YGGSPANFLD VGGGAKAERI
310 320 330 340 350
TNALDMVFSD DNVDSVVFNI FGGITRGDEV AKGINEALEA FDEIPKPVVV
360 370 380 390
RLAGTNWEEG MEILNEDLVT VEQTLEDAVQ RSVEYAEEGE A
Length:391
Mass (Da):41,773
Last modified:March 6, 2013 - v1
Checksum:i254F35746E99FFFD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003050 Genomic DNA Translation: AGB16047.1

Genome annotation databases

EnsemblBacteriaiAGB16047; AGB16047; Halru_1436
KEGGihru:Halru_1436

Similar proteinsi

Entry informationi

Entry nameiL0IDJ6_HALRX
AccessioniPrimary (citable) accession number: L0IDJ6
Entry historyiIntegrated into UniProtKB/TrEMBL: March 6, 2013
Last sequence update: March 6, 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 proteome, Reference proteomeImported

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