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Database: UniProt
Entry: P53593
LinkDB: P53593
Original site: P53593 
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   05-DEC-2018, entry version 132.
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 /
OS   JCM 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 /
RC   1C / 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 /
RC   1C / 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.,
RA   Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an
RT   opportunistic 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 /
RC   1C / 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.,
RA   Lightfoot J., Foster J., Siehnel R., Schweizer H., Lam J.S.,
RA   Hancock R.E., Levesque R.C.;
RT   "Physical mapping of 32 genetic markers on the Pseudomonas aeruginosa
RT   PAO1 chromosome.";
RL   Microbiology 142:79-86(1996).
CC   -!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid
CC       cycle (TCA), coupling the hydrolysis of succinyl-CoA to the
CC       synthesis of either ATP or GTP and thus represents the only step
CC       of substrate-level phosphorylation in the TCA. The beta subunit
CC       provides nucleotide specificity of the enzyme and binds the
CC       substrate succinate, while the binding sites for coenzyme A and
CC       phosphate are found in the alpha subunit. Can also generate UTP or
CC       CTP, although it preferentially synthesizes ATP and/or GTP.
CC       {ECO:0000255|HAMAP-Rule:MF_00558, 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-
CC       Rule:MF_00558};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       succinate from succinyl-CoA (ligase route): step 1/1.
CC       {ECO:0000255|HAMAP-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
CC       subunit family. {ECO:0000255|HAMAP-Rule:MF_00558}.
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; NC_002516.2.
DR   ProteinModelPortal; P53593; -.
DR   SMR; P53593; -.
DR   STRING; 208964.PA1588; -.
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   eggNOG; ENOG4105CMV; Bacteria.
DR   eggNOG; COG0045; LUCA.
DR   HOGENOM; HOG000007059; -.
DR   InParanoid; P53593; -.
DR   KO; K01903; -.
DR   OMA; LCMDAKF; -.
DR   PhylomeDB; P53593; -.
DR   BioCyc; PAER208964:G1FZ6-1618-MONOMER; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000002438; Chromosome.
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:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
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; Complete proteome; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN         1    388       Succinate--CoA ligase [ADP-forming]
FT                                subunit beta.
FT                                /FTId=PRO_0000102844.
FT   DOMAIN        9    244       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   NP_BIND      53     55       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   REGION      321    323       Substrate binding; shared with subunit
FT                                alpha. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   METAL       199    199       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   METAL       213    213       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   BINDING      46     46       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING      99     99       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING     102    102       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING     107    107       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING     264    264       Substrate; shared with subunit alpha.
FT                                {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   CONFLICT    239    240       DA -> LP (in Ref. 3). {ECO:0000305}.
FT   CONFLICT    364    382       SGLNIIAATSLTDAAQQVV -> KRPEHHRGNQPDRRCPAS
FT                                L (in Ref. 1; AAD21622). {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
//
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