ID SUCC_BACTN Reviewed; 376 AA.
AC Q8A9M7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 16-JAN-2019, entry version 103.
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=BT_0788;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC
OS 10582 / E50 / VPI-5482).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K.,
RA Chiang H.C., Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
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; AE015928; AAO75895.1; -; Genomic_DNA.
DR RefSeq; NP_809701.1; NC_004663.1.
DR RefSeq; WP_008765647.1; NC_004663.1.
DR ProteinModelPortal; Q8A9M7; -.
DR SMR; Q8A9M7; -.
DR STRING; 226186.BT_0788; -.
DR PaxDb; Q8A9M7; -.
DR PRIDE; Q8A9M7; -.
DR EnsemblBacteria; AAO75895; AAO75895; BT_0788.
DR GeneID; 1072236; -.
DR GeneID; 31616888; -.
DR KEGG; bth:BT_0788; -.
DR PATRIC; fig|226186.12.peg.806; -.
DR eggNOG; ENOG4105CMV; Bacteria.
DR eggNOG; COG0045; LUCA.
DR InParanoid; Q8A9M7; -.
DR KO; K01903; -.
DR OMA; LCMDAKF; -.
DR BioCyc; BTHE:G13PU-5699-MONOMER; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000001414; 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 1 376 Succinate--CoA ligase [ADP-forming]
FT subunit beta.
FT /FTId=PRO_1000082017.
FT DOMAIN 9 237 ATP-grasp. {ECO:0000255|HAMAP-
FT Rule:MF_00558}.
FT NP_BIND 53 55 ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT REGION 314 316 Substrate binding; shared with subunit
FT alpha. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT METAL 192 192 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_00558}.
FT METAL 206 206 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_00558}.
FT BINDING 46 46 ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT BINDING 95 95 ATP; via amide nitrogen.
FT {ECO:0000255|HAMAP-Rule:MF_00558}.
FT BINDING 100 100 ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT BINDING 257 257 Substrate; shared with subunit alpha.
FT {ECO:0000255|HAMAP-Rule:MF_00558}.
SQ SEQUENCE 376 AA; 41197 MW; 363CAE207893E10B CRC64;
MKIHEYQAKE IFSKYGIPVE RHTLCRTAAG AVAAYKRMGS DRVVIKAQVL TGGRGKAGGV
KLVDNTEDTY QEAKNILGMS IKGLPVNQIL VSEAVDIAAE YYVSFTIDRN TRSVILMMSA
SGGMDIEEVA RQSPEKIIRY AIDPFIGLPD YLARRFAFSL FPHIEQAGRM AAILQALYKI
FMENDASLVE VNPLALTAKG ILMAIDAKIV FDDNALYRHP DVLSLFDPTE EEKVEADAKN
KGFSYVHMDG NIGCMVNGAG LAMATMDMIK LHGGNPANFL DIGGSSNPVK VVEAMKLLLQ
DEKVKVVLIN IFGGITRCDD VAIGLIQAFD QIKSDIPVIV RLTGTNEHLG RDLLRNHSRF
QIATTMQEAA LMAIKS
//
