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Protein

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

Gene

sucC

Organism
Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / FZB42) (Bacillus amyloliquefaciens subsp. plantarum)
Status
Reviewed-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 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 sitei99ATPUniRule annotation1
Binding sitei102ATP; via amide nitrogenUniRule annotation1
Binding sitei107ATPUniRule annotation1
Metal bindingi199MagnesiumUniRule annotation1
Metal bindingi213MagnesiumUniRule annotation1
Binding sitei264Substrate; 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:RBAM_015920
OrganismiBacillus velezensis (strain DSM 23117 / BGSC 10A6 / FZB42) (Bacillus amyloliquefaciens subsp. plantarum)
Taxonomic identifieri326423 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus amyloliquefaciens group
Proteomesi
  • UP000001120 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000820041 – 385Succinate--CoA ligase [ADP-forming] subunit betaAdd BLAST385

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta subunits.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA7Z4M9
SMRiA7Z4M9
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 244ATP-graspUniRule annotationAdd BLAST236

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni321 – 323Substrate 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

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.

A7Z4M9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNIHEYQGKE VLRKYGVSVP EGKVAFTAEE AVEKAESLSS SVYVVKAQIH
60 70 80 90 100
AGGRGKAGGV KIAKTKDEVK EYAEELLGKT LVTHQTGPDG QVIKRLLIEE
110 120 130 140 150
GCDIKKEYYV GLVLDRATSR IVLMASEEGG TEIEEVAEKT PEKIKKAVID
160 170 180 190 200
PAVGLQGYQA REIAFAINIP KELVGKAAKF MLGLYKAFVE KDCSIAEINP
210 220 230 240 250
LVVTGDGNVM ALDAKLNFDS NALYRQKDIM EYRDLDEEDP KEIEASKYDL
260 270 280 290 300
SYISLDGNIG CMVNGAGLAM STMDIIKHYG GEPANFLDVG GGATAEKVTE
310 320 330 340 350
AFKIILSDQN VKGIFVNIFG GIMKCDVIAE GVVEATRQVG LTLPLVVRLE
360 370 380
GTNVDLGKKI LNESGLNITS AESMADGAQK IVSLV
Length:385
Mass (Da):41,514
Last modified:October 23, 2007 - v1
Checksum:iA477F07640FF24E2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000560 Genomic DNA Translation: ABS73955.1
RefSeqiWP_003154283.1, NC_009725.1

Genome annotation databases

EnsemblBacteriaiABS73955; ABS73955; RBAM_015920
KEGGibay:RBAM_015920

Similar proteinsi

Entry informationi

Entry nameiSUCC_BACVZ
AccessioniPrimary (citable) accession number: A7Z4M9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 23, 2007
Last modified: April 25, 2018
This is version 77 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
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Main funding by: National Institutes of Health