SUCC_PSEAE
ID SUCC_PSEAE Reviewed; 388 AA.
AC P53593; Q9X5W1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta {ECO:0000255|HAMAP-Rule:MF_00558};
DE EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10671455};
DE AltName: Full=Succinyl-CoA synthetase subunit beta {ECO:0000255|HAMAP-Rule:MF_00558};
DE Short=SCS-beta {ECO:0000255|HAMAP-Rule:MF_00558};
GN Name=sucC {ECO:0000255|HAMAP-Rule:MF_00558}; OrderedLocusNames=PA1588;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10671455; DOI=10.1128/jb.182.5.1333-1339.2000;
RA Kapatral V., Bina X., Chakrabarty A.M.;
RT "Succinyl coenzyme A synthetase of Pseudomonas aeruginosa with a broad
RT specificity for nucleoside triphosphate (NTP) synthesis modulates
RT specificity for NTP synthesis by the 12-kilodalton form of nucleoside
RT diphosphate kinase.";
RL J. Bacteriol. 182:1333-1339(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 239-388.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=8581173; DOI=10.1099/13500872-142-1-79;
RA Liao X., Charlebois I., Ouellet C., Morency M.J., Dewar K., Lightfoot J.,
RA Foster J., Siehnel R., Schweizer H., Lam J.S., Hancock R.E., Levesque R.C.;
RT "Physical mapping of 32 genetic markers on the Pseudomonas aeruginosa PAO1
RT chromosome.";
RL Microbiology 142:79-86(1996).
CC -!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle
CC (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of
CC either ATP or GTP and thus represents the only step of substrate-level
CC phosphorylation in the TCA. The beta subunit provides nucleotide
CC specificity of the enzyme and binds the substrate succinate, while the
CC binding sites for coenzyme A and phosphate are found in the alpha
CC subunit. Can also generate UTP or CTP, although it preferentially
CC synthesizes ATP and/or GTP. {ECO:0000255|HAMAP-Rule:MF_00558,
CC ECO:0000269|PubMed:10671455}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + succinate = ADP + phosphate + succinyl-CoA;
CC Xref=Rhea:RHEA:17661, ChEBI:CHEBI:30031, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC ChEBI:CHEBI:456216; EC=6.2.1.5; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00558, ECO:0000269|PubMed:10671455};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00558};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00558};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00558}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00558}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_00558}.
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DR EMBL; AF128399; AAD21622.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04977.1; -; Genomic_DNA.
DR EMBL; X84052; CAA58870.1; -; Genomic_DNA.
DR PIR; A83446; A83446.
DR PIR; S54847; S54847.
DR RefSeq; NP_250279.1; NC_002516.2.
DR RefSeq; WP_003087425.1; NZ_QZGE01000003.1.
DR AlphaFoldDB; P53593; -.
DR SMR; P53593; -.
DR STRING; 287.DR97_301; -.
DR PaxDb; P53593; -.
DR PRIDE; P53593; -.
DR DNASU; 882016; -.
DR EnsemblBacteria; AAG04977; AAG04977; PA1588.
DR GeneID; 882016; -.
DR KEGG; pae:PA1588; -.
DR PATRIC; fig|208964.12.peg.1647; -.
DR PseudoCAP; PA1588; -.
DR HOGENOM; CLU_037430_0_2_6; -.
DR InParanoid; P53593; -.
DR OMA; ITACDEV; -.
DR PhylomeDB; P53593; -.
DR BioCyc; PAER208964:G1FZ6-1618-MON; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0042709; C:succinate-CoA ligase complex; IDA:PseudoCAP.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IDA:PseudoCAP.
DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IDA:PseudoCAP.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IDA:PseudoCAP.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:PseudoCAP.
DR GO; GO:0006104; P:succinyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.261; -; 1.
DR HAMAP; MF_00558; Succ_CoA_beta; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005811; CoA_ligase.
DR InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR InterPro; IPR005809; Succ_CoA_synthase_bsu.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR11815; PTHR11815; 1.
DR Pfam; PF08442; ATP-grasp_2; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR PIRSF; PIRSF001554; SucCS_beta; 1.
DR SUPFAM; SSF52210; SSF52210; 1.
DR TIGRFAMs; TIGR01016; sucCoAbeta; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..388
FT /note="Succinate--CoA ligase [ADP-forming] subunit beta"
FT /id="PRO_0000102844"
FT DOMAIN 9..244
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 53..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 199
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 264
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 321..323
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT CONFLICT 239..240
FT /note="DA -> LP (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 364..382
FT /note="SGLNIIAATSLTDAAQQVV -> KRPEHHRGNQPDRRCPASL (in Ref.
FT 1; AAD21622)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 388 AA; 41543 MW; B0CC74089FE6C8EF CRC64;
MNLHEYQGKQ LFAEYGLPVS KGFAVDTPEE AAEACDKIGG SEWVVKAQVH AGGRGKAGGV
KLVKSKEDAK AFAQQWLGKN LVTYQTDANG QPVSKILVES CTDIDKELYL GAVVDRSSRR
IVFMASTEGG VDIEKVAHDT PEKILKATID PLVGAQPYQG RELAFQLGLK GDQIKQFTHI
FVGLAKLFQD YDLALLEVNP LVIKKDGNLH CLDAKINIDS NALYRQPKLR AMHDPSQDDA
REAHAQKWEL NYVALEGNIG CMVNGAGLAM GTMDIVNLHG GKPANFLDVG GGATKERVTE
AFKIILSDSN VKAVLVNIFG GIVRCDMIAE GIIGAVKEVG VKVPVVVRLE GNNAELGAKV
LAESGLNIIA ATSLTDAAQQ VVKAAEGK
