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Database: UniProt
Entry: B1ZP17
LinkDB: B1ZP17
Original site: B1ZP17 
ID   SUCC_OPITP              Reviewed;         393 AA.
AC   B1ZP17;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   16-JAN-2019, entry version 70.
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=Oter_4233;
OS   Opitutus terrae (strain DSM 11246 / JCM 15787 / PB90-1).
OC   Bacteria; Verrucomicrobia; Opitutae; Opitutales; Opitutaceae;
OC   Opitutus.
OX   NCBI_TaxID=452637;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11246 / JCM 15787 / PB90-1;
RX   PubMed=21398538; DOI=10.1128/JB.00228-11;
RA   van Passel M.W., Kant R., Palva A., Copeland A., Lucas S., Lapidus A.,
RA   Glavina del Rio T., Pitluck S., Goltsman E., Clum A., Sun H.,
RA   Schmutz J., Larimer F.W., Land M.L., Hauser L., Kyrpides N.,
RA   Mikhailova N., Richardson P.P., Janssen P.H., de Vos W.M., Smidt H.;
RT   "Genome sequence of the verrucomicrobium Opitutus terrae PB90-1, an
RT   abundant inhabitant of rice paddy soil ecosystems.";
RL   J. Bacteriol. 193:2367-2368(2011).
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; CP001032; ACB77506.1; -; Genomic_DNA.
DR   RefSeq; WP_012377034.1; NC_010571.1.
DR   ProteinModelPortal; B1ZP17; -.
DR   SMR; B1ZP17; -.
DR   STRING; 452637.Oter_4233; -.
DR   PRIDE; B1ZP17; -.
DR   EnsemblBacteria; ACB77506; ACB77506; Oter_4233.
DR   KEGG; ote:Oter_4233; -.
DR   eggNOG; ENOG4105CMV; Bacteria.
DR   eggNOG; COG0045; LUCA.
DR   HOGENOM; HOG000007059; -.
DR   KO; K01903; -.
DR   OMA; LCMDAKF; -.
DR   OrthoDB; 316012at2; -.
DR   BioCyc; OTER452637:G1GBP-4312-MONOMER; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000007013; 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; 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; 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    393       Succinate--CoA ligase [ADP-forming]
FT                                subunit beta.
FT                                /FTId=PRO_1000129204.
FT   DOMAIN        9    251       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   NP_BIND      53     55       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   REGION      328    330       Substrate binding; shared with subunit
FT                                alpha. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   METAL       206    206       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   METAL       220    220       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   BINDING      46     46       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING     109    109       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING     114    114       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING     271    271       Substrate; shared with subunit alpha.
FT                                {ECO:0000255|HAMAP-Rule:MF_00558}.
SQ   SEQUENCE   393 AA;  42006 MW;  F7954E0DCFC8E5B7 CRC64;
     MNIHEYQAKA LFEKFGVLVP KGAPAKTPEE FVTALAQLPE GMIVVKSQIH AGGRGKGTFT
     DGFKGGVKVC KSKAEAREAA GKMLGNTLVT AQTGPAGRKV QTIYFNVGSQ IKKEYYLAIL
     LDRATSRPVI VASTEGGMEI EKVAHDTPDR IFKVHVDPAY GLADFQVREL VFKLGFTAAE
     GKNASKLIRA LYRCFWENDA SMVEVNPLIT TPDGQVEALD AKVAFDDNAL FRHPELVELR
     DLNEEDPKEI EASKHELNYI ALDGNIACLV NGAGLAMSTM DIIKHFGGTP ANFLDVGGGA
     SREQVVAAFK IILGDKNVRG ILVNIFGGIM DCNVIAQGIV DAVKEVGLEL PLVVRLEGNN
     VAAGKATLAT SGLKLVSGDS MADAAQKIVK LVA
//
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