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Protein

Succinyl-CoA ligase [ADP-forming] subunit beta

Gene

sucC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

During aerobic metabolism it functions in the citric acid cycle, coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents an important site of substrate-level phosphorylation. It can also function in the other direction for anabolic purposes, and this may be particularly important for providing succinyl-CoA during anaerobic growth when the oxidative route from 2-oxoglutarate is severely repressed. The beta-subunit contains the attachment sites for succinate. The complete active site is probably located in the region of alpha-beta contact.

Catalytic activityi

ATP + succinate + CoA = ADP + phosphate + succinyl-CoA.

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 1 Mg2+ or Mn2+ ion per subunit.By similarity

Enzyme regulationi

Exhibits two interesting properties: "substrate synergism", in which the enzyme is most active for the catalysis of its partial reactions only when all the substrate-binding sites are occupied, and "catalytic cooperativity" between alternating active sites in the tetramer, whereby the interaction of substrates (particularly ATP) at one site is needed to promote catalysis at the other.

Pathwayi: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes succinate from succinyl-CoA (ligase route).
Proteins known to be involved in this subpathway in this organism are:
  1. Succinyl-CoA ligase [ADP-forming] subunit alpha (sucD), Succinyl-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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi197 – 1971Magnesium or manganeseBy similarity
Metal bindingi199 – 1991Magnesium or manganeseBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi35 – 10874ATPBy similarityAdd
BLAST

GO - Molecular functioni

  • ATP binding Source: UniProtKB-HAMAP
  • magnesium ion binding Source: UniProtKB-HAMAP
  • manganese ion binding Source: UniProtKB-HAMAP
  • succinate-CoA ligase (ADP-forming) activity Source: EcoliWiki

GO - Biological processi

  • tricarboxylic acid cycle Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:SUCCCOASYN-BETA.
ECOL316407:JW0717-MONOMER.
MetaCyc:SUCCCOASYN-BETA.
BRENDAi6.2.1.5. 2165.
UniPathwayiUPA00223; UER00999.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinyl-CoA ligase [ADP-forming] subunit beta (EC:6.2.1.5)
Alternative name(s):
Succinyl-CoA synthetase subunit beta
Short name:
SCS-beta
Gene namesi
Name:sucC
Ordered Locus Names:b0728, JW0717
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10981. sucC.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: EcoCyc
  • succinate-CoA ligase complex (ADP-forming) Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 388388Succinyl-CoA ligase [ADP-forming] subunit betaPRO_0000102832Add
BLAST

Proteomic databases

EPDiP0A836.
PaxDbiP0A836.
PRIDEiP0A836.

2D gel databases

SWISS-2DPAGEP0A836.

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta subunits.

Binary interactionsi

WithEntry#Exp.IntActNotes
sucDP0AGE93EBI-369117,EBI-369078

Protein-protein interaction databases

BioGridi4259946. 7 interactions.
DIPiDIP-31852N.
IntActiP0A836. 8 interactions.
STRINGi511145.b0728.

Structurei

Secondary structure

1
388
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1410Combined sources
Beta strandi22 – 276Combined sources
Helixi28 – 3811Combined sources
Beta strandi43 – 475Combined sources
Beta strandi50 – 523Combined sources
Turni54 – 585Combined sources
Beta strandi60 – 634Combined sources
Helixi66 – 7611Combined sources
Beta strandi79 – 813Combined sources
Beta strandi96 – 1005Combined sources
Beta strandi104 – 11512Combined sources
Turni116 – 1194Combined sources
Beta strandi120 – 1278Combined sources
Helixi133 – 1397Combined sources
Helixi141 – 1433Combined sources
Beta strandi144 – 1485Combined sources
Turni151 – 1533Combined sources
Helixi157 – 16610Combined sources
Helixi172 – 19019Combined sources
Beta strandi193 – 20412Combined sources
Beta strandi209 – 2124Combined sources
Beta strandi215 – 2184Combined sources
Helixi220 – 2256Combined sources
Helixi227 – 2326Combined sources
Helixi235 – 2373Combined sources
Helixi240 – 2478Combined sources
Beta strandi251 – 2544Combined sources
Beta strandi256 – 26510Combined sources
Helixi266 – 27813Combined sources
Beta strandi285 – 2884Combined sources
Helixi295 – 30612Combined sources
Beta strandi308 – 3103Combined sources
Beta strandi313 – 3208Combined sources
Beta strandi321 – 3233Combined sources
Helixi325 – 33915Combined sources
Beta strandi345 – 3517Combined sources
Helixi354 – 3629Combined sources
Beta strandi366 – 3705Combined sources
Helixi374 – 38411Combined sources
Turni385 – 3873Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CQIX-ray3.30B/E1-385[»]
1CQJX-ray2.90B/E1-385[»]
1JKJX-ray2.35B/E1-388[»]
1JLLX-ray2.69B/E1-388[»]
1SCUX-ray2.50B/E1-388[»]
2NU6X-ray2.55B/E1-388[»]
2NU7X-ray2.20B/E1-388[»]
2NU8X-ray2.15B/E1-388[»]
2NU9X-ray2.90B/E/G/I1-388[»]
2NUAX-ray2.95B/E1-388[»]
2SCUX-ray2.30B/E1-388[»]
ProteinModelPortaliP0A836.
SMRiP0A836. Positions 1-388.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A836.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 244236ATP-graspAdd
BLAST

Sequence similaritiesi

Contains 1 ATP-grasp domain.Curated

Phylogenomic databases

eggNOGiENOG4105CMV. Bacteria.
COG0045. LUCA.
HOGENOMiHOG000007059.
InParanoidiP0A836.
KOiK01903.
OMAiYIESGCD.
OrthoDBiEOG644ZT0.
PhylomeDBiP0A836.

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.
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.

P0A836-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLHEYQAKQ LFARYGLPAP VGYACTTPRE AEEAASKIGA GPWVVKCQVH
60 70 80 90 100
AGGRGKAGGV KVVNSKEDIR AFAENWLGKR LVTYQTDANG QPVNQILVEA
110 120 130 140 150
ATDIAKELYL GAVVDRSSRR VVFMASTEGG VEIEKVAEET PHLIHKVALD
160 170 180 190 200
PLTGPMPYQG RELAFKLGLE GKLVQQFTKI FMGLATIFLE RDLALIEINP
210 220 230 240 250
LVITKQGDLI CLDGKLGADG NALFRQPDLR EMRDQSQEDP REAQAAQWEL
260 270 280 290 300
NYVALDGNIG CMVNGAGLAM GTMDIVKLHG GEPANFLDVG GGATKERVTE
310 320 330 340 350
AFKIILSDDK VKAVLVNIFG GIVRCDLIAD GIIGAVAEVG VNVPVVVRLE
360 370 380
GNNAELGAKK LADSGLNIIA AKGLTDAAQQ VVAAVEGK
Length:388
Mass (Da):41,393
Last modified:April 1, 1988 - v1
Checksum:i09C429EC97A823CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01619 Genomic DNA. Translation: AAA23899.1.
U00096 Genomic DNA. Translation: AAC73822.1.
AP009048 Genomic DNA. Translation: BAA35394.1.
PIRiA24090. SYECSB.
RefSeqiNP_415256.1. NC_000913.3.
WP_001048602.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73822; AAC73822; b0728.
BAA35394; BAA35394; BAA35394.
GeneIDi945312.
KEGGiecj:JW0717.
eco:b0728.
PATRICi32116651. VBIEscCol129921_0758.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01619 Genomic DNA. Translation: AAA23899.1.
U00096 Genomic DNA. Translation: AAC73822.1.
AP009048 Genomic DNA. Translation: BAA35394.1.
PIRiA24090. SYECSB.
RefSeqiNP_415256.1. NC_000913.3.
WP_001048602.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CQIX-ray3.30B/E1-385[»]
1CQJX-ray2.90B/E1-385[»]
1JKJX-ray2.35B/E1-388[»]
1JLLX-ray2.69B/E1-388[»]
1SCUX-ray2.50B/E1-388[»]
2NU6X-ray2.55B/E1-388[»]
2NU7X-ray2.20B/E1-388[»]
2NU8X-ray2.15B/E1-388[»]
2NU9X-ray2.90B/E/G/I1-388[»]
2NUAX-ray2.95B/E1-388[»]
2SCUX-ray2.30B/E1-388[»]
ProteinModelPortaliP0A836.
SMRiP0A836. Positions 1-388.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259946. 7 interactions.
DIPiDIP-31852N.
IntActiP0A836. 8 interactions.
STRINGi511145.b0728.

2D gel databases

SWISS-2DPAGEP0A836.

Proteomic databases

EPDiP0A836.
PaxDbiP0A836.
PRIDEiP0A836.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73822; AAC73822; b0728.
BAA35394; BAA35394; BAA35394.
GeneIDi945312.
KEGGiecj:JW0717.
eco:b0728.
PATRICi32116651. VBIEscCol129921_0758.

Organism-specific databases

EchoBASEiEB0974.
EcoGeneiEG10981. sucC.

Phylogenomic databases

eggNOGiENOG4105CMV. Bacteria.
COG0045. LUCA.
HOGENOMiHOG000007059.
InParanoidiP0A836.
KOiK01903.
OMAiYIESGCD.
OrthoDBiEOG644ZT0.
PhylomeDBiP0A836.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00999.
BioCyciEcoCyc:SUCCCOASYN-BETA.
ECOL316407:JW0717-MONOMER.
MetaCyc:SUCCCOASYN-BETA.
BRENDAi6.2.1.5. 2165.

Miscellaneous databases

EvolutionaryTraceiP0A836.
PROiP0A836.

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.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of the succinyl-CoA synthetase of Escherichia coli."
    Buck D., Spencer M.E., Guest J.R.
    Biochemistry 24:6245-6252(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-12.
    Strain: K12 / EMG2.
  6. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  7. "The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-A resolution."
    Wolodko W.T., Fraser M.E., James M.N.G., Bridger W.A.
    J. Biol. Chem. 269:10883-10890(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  8. "A detailed structural description of Escherichia coli succinyl-CoA synthetase."
    Fraser M.E., James M.N., Bridger W.A., Wolodko W.T.
    J. Mol. Biol. 285:1633-1653(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  9. "ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by X-ray crystallography."
    Joyce M.A., Fraser M.E., James M.N., Bridger W.A., Wolodko W.T.
    Biochemistry 39:17-25(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).

Entry informationi

Entry nameiSUCC_ECOLI
AccessioniPrimary (citable) accession number: P0A836
Secondary accession number(s): P07460
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: March 16, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Succinyl-CoA synthetase (SCS) of E.coli catalyzes its reaction via three steps that involve phosphoryl enzyme and enzyme-bound succinyl phosphate as intermediates.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.