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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: 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)
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

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

ATP-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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
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

Protein-protein interaction databases

STRINGi326423.RBAM_015920.

Structurei

3D structure databases

ProteinModelPortaliA7Z4M9.
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
Contains 1 ATP-grasp domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CMV. Bacteria.
COG0045. LUCA.
HOGENOMiHOG000007059.
KOiK01903.
OMAiYIESGCD.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.261. 1 hit.
HAMAPiMF_00558. Succ_CoA_beta. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR013650. ATP-grasp_succ-CoA_synth-type.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR005811. CoA_ligase.
IPR017866. Succ-CoA_synthase_bsu_CS.
IPR005809. Succ_CoA_synthase_bsu.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]
PANTHERiPTHR11815. PTHR11815. 1 hit.
PfamiPF08442. ATP-grasp_2. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]
PIRSFiPIRSF001554. SucCS_beta. 1 hit.
SUPFAMiSSF52210. SSF52210. 1 hit.
TIGRFAMsiTIGR01016. sucCoAbeta. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view]

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.
PATRICi18748250. VBIBacAmy31356_1601.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliA7Z4M9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi326423.RBAM_015920.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABS73955; ABS73955; RBAM_015920.
KEGGibay:RBAM_015920.
PATRICi18748250. VBIBacAmy31356_1601.

Phylogenomic databases

eggNOGiENOG4105CMV. Bacteria.
COG0045. LUCA.
HOGENOMiHOG000007059.
KOiK01903.
OMAiYIESGCD.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00999.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.261. 1 hit.
HAMAPiMF_00558. Succ_CoA_beta. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR013650. ATP-grasp_succ-CoA_synth-type.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR005811. CoA_ligase.
IPR017866. Succ-CoA_synthase_bsu_CS.
IPR005809. Succ_CoA_synthase_bsu.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]
PANTHERiPTHR11815. PTHR11815. 1 hit.
PfamiPF08442. ATP-grasp_2. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]
PIRSFiPIRSF001554. SucCS_beta. 1 hit.
SUPFAMiSSF52210. SSF52210. 1 hit.
TIGRFAMsiTIGR01016. sucCoAbeta. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSUCC_BACVZ
AccessioniPrimary (citable) accession number: A7Z4M9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 23, 2007
Last modified: November 30, 2016
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.