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Protein

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

Gene

sucD

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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 alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit. Can also generate UTP or CTP, although it preferentially synthesizes ATP and/or GTP.1 Publication

Catalytic activityi

ATP + succinate + CoA = ADP + phosphate + succinyl-CoA.1 Publication

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. 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 sitei43Coenzyme A1
Binding sitei159Substrate; shared with subunit beta1
Active sitei247Tele-phosphohistidine intermediate1

GO - Molecular functioni

  • cofactor binding Source: InterPro
  • nucleoside diphosphate kinase activity Source: PseudoCAP
  • nucleotide binding Source: UniProtKB-KW
  • succinate-CoA ligase (ADP-forming) activity Source: PseudoCAP

GO - Biological processi

  • nucleoside triphosphate biosynthetic process Source: PseudoCAP
  • tricarboxylic acid cycle Source: UniProtKB-UniPathway

Keywordsi

Molecular functionLigase
Biological processTricarboxylic acid cycle
LigandNucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00223; UER00999.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate--CoA ligase [ADP-forming] subunit alpha (EC:6.2.1.51 Publication)
Alternative name(s):
Succinyl-CoA synthetase subunit alpha
Short name:
SCS-alpha
Gene namesi
Name:sucD
Ordered Locus Names:PA1589
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA1589.

Subcellular locationi

GO - Cellular componenti

  • succinate-CoA ligase complex Source: PseudoCAP

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001027971 – 295Succinate--CoA ligase [ADP-forming] subunit alphaAdd BLAST295

Proteomic databases

PaxDbiQ51567.
PRIDEiQ51567.

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta subunits.

Protein-protein interaction databases

STRINGi208964.PA1589.

Structurei

3D structure databases

ProteinModelPortaliQ51567.
SMRiQ51567.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni17 – 20Coenzyme A binding4
Regioni96 – 98Coenzyme A binding3

Sequence similaritiesi

Belongs to the succinate/malate CoA ligase alpha subunit family.

Phylogenomic databases

eggNOGiENOG4105CH8. Bacteria.
COG0074. LUCA.
HOGENOMiHOG000239685.
InParanoidiQ51567.
KOiK01902.
OMAiIIFVPPA.
PhylomeDBiQ51567.

Family and domain databases

Gene3Di3.40.50.261. 1 hit.
HAMAPiMF_01988. Succ_CoA_alpha. 1 hit.
InterProiView protein in InterPro
IPR017440. Cit_synth/succinyl-CoA_lig_AS.
IPR033847. Citrt_syn/SCS-alpha_CS.
IPR003781. CoA-bd.
IPR005810. CoA_lig_alpha.
IPR005811. CoA_ligase.
IPR036291. NAD(P)-bd_dom_sf.
IPR016102. Succinyl-CoA_synth-like.
PfamiView protein in Pfam
PF02629. CoA_binding. 1 hit.
PF00549. Ligase_CoA. 1 hit.
PIRSFiPIRSF001553. SucCS_alpha. 1 hit.
SMARTiView protein in SMART
SM00881. CoA_binding. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF52210. SSF52210. 1 hit.
TIGRFAMsiTIGR01019. sucCoAalpha. 1 hit.
PROSITEiView protein in PROSITE
PS01216. SUCCINYL_COA_LIG_1. 1 hit.
PS00399. SUCCINYL_COA_LIG_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Q51567-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVLINKDTK VICQGFTGSQ GTFHSEQAIA YGTKMVGGVT PGKGGTTHLG
60 70 80 90 100
LPVFNTVKEA VEATGAEASV IYVPAPFCKD SILEAAFGGI KLIVCITEGI
110 120 130 140 150
PTLDMLDAKV KCDELGVRLI GPNCPGVITP GECKIGIMPG HIHLPGKVGI
160 170 180 190 200
VSRSGTLTYE AVKQTTDAGF GQSTCVGIGG DPIPGSNFID ILKLFQEDPQ
210 220 230 240 250
TEAIVMIGEI GGSAEEEAAA FIKANVTKPV VSYIAGVTAP PGKRMGHAGA
260 270 280 290
IISGGKGTAD EKFAALQDAG VKTVRSLADI GKALAELTGW EVKKA
Length:295
Mass (Da):30,266
Last modified:December 8, 2000 - v2
Checksum:iD1BE36033FEA716F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti18 – 20GSQ → VEP in CAA58871 (PubMed:8581173).Curated3
Sequence conflicti194L → R in AAD21623 (PubMed:10671455).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF128399 Genomic DNA. Translation: AAD21623.1.
AE004091 Genomic DNA. Translation: AAG04978.1.
X84052 Genomic DNA. Translation: CAA58871.1.
PIRiB83446.
RefSeqiNP_250280.1. NC_002516.2.
WP_003087428.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG04978; AAG04978; PA1589.
GeneIDi882039.
KEGGipae:PA1589.
PATRICifig|208964.12.peg.1648.

Similar proteinsi

Entry informationi

Entry nameiSUCD_PSEAE
AccessioniPrimary (citable) accession number: Q51567
Secondary accession number(s): Q9X5W2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 8, 2000
Last modified: October 25, 2017
This is version 121 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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