ID SUCC_ACIAD Reviewed; 388 AA.
AC Q6F8L4;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 13-FEB-2019, entry version 96.
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};
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};
GN OrderedLocusNames=ACIAD2873;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Moraxellaceae; Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S.,
RA Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P.,
RA Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp.
RT ADP1, a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
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. {ECO:0000255|HAMAP-
CC Rule:MF_00558}.
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};
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; CR543861; CAG69601.1; -; Genomic_DNA.
DR RefSeq; WP_004929376.1; NC_005966.1.
DR ProteinModelPortal; Q6F8L4; -.
DR SMR; Q6F8L4; -.
DR STRING; 62977.ACIAD2873; -.
DR PRIDE; Q6F8L4; -.
DR EnsemblBacteria; CAG69601; CAG69601; ACIAD2873.
DR KEGG; aci:ACIAD2873; -.
DR eggNOG; ENOG4105CMV; Bacteria.
DR eggNOG; COG0045; LUCA.
DR HOGENOM; HOG000007059; -.
DR KO; K01903; -.
DR OMA; LCMDAKF; -.
DR OrthoDB; 316012at2; -.
DR BioCyc; ASP62977:ACIAD_RS12970-MONOMER; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
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_0000102814.
FT DOMAIN 9 245 ATP-grasp. {ECO:0000255|HAMAP-
FT Rule:MF_00558}.
FT NP_BIND 53 55 ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT REGION 322 324 Substrate binding; shared with subunit
FT alpha. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT METAL 200 200 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_00558}.
FT METAL 214 214 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_00558}.
FT BINDING 46 46 ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT BINDING 100 100 ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT BINDING 103 103 ATP; via amide nitrogen.
FT {ECO:0000255|HAMAP-Rule:MF_00558}.
FT BINDING 108 108 ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT BINDING 265 265 Substrate; shared with subunit alpha.
FT {ECO:0000255|HAMAP-Rule:MF_00558}.
SQ SEQUENCE 388 AA; 41375 MW; D388D64A9F487E6C CRC64;
MNLHEYQAKA LLKKYGVSVQ EGILARSAEE AVAAFEQLGG KFAVIKAQVH AGGRGKAGGV
KVVKSKEEAA DYANQLIGTN LVTYQTDANG QPVNSVLVCE DVYPVERELY LGAVVDRSSR
RVTFMASTEG GVEIEKVAEE TPEKIIKVEV DPLVGLQPFQ AREVAFALGL KDKQIGQFVK
LMAGAYQAFV ENDFALFEIN PLSVRENGDI LAVDAKIGID SNALYRLPEI AASRDKSQEN
ERELKASEFE LNYVALEGNI GCMVNGAGLA MATMDIIKLY GGQPANFLDV GGGATKERVI
EAFKLILADT SVQGVLINIF GGIVRCDMIA EAIIAAVQEV NVTVPVVVRL EGNNAELGAK
ILDESGLKLT SANGLSDAAE KIVAAVKG
//
