ID SUCC_RHOS1 Reviewed; 397 AA.
AC A3PN13;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 01-MAY-2013, entry version 47.
DE RecName: Full=Succinyl-CoA ligase [ADP-forming] subunit beta;
DE EC=6.2.1.5;
DE AltName: Full=Succinyl-CoA synthetase subunit beta;
DE Short=SCS-beta;
GN Name=sucC; OrderedLocusNames=Rsph17029_2627;
OS Rhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=349101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17029 / ATH 2.4.9;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Richardson P., Mackenzie C., Choudhary M.,
RA Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides ATCC
RT 17029.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY: ATP + succinate + CoA = ADP + phosphate +
CC succinyl-CoA.
CC -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By
CC similarity).
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC succinate from succinyl-CoA (ligase route): step 1/1.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits (By
CC similarity).
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta
CC subunit family.
CC -!- SIMILARITY: Contains 1 ATP-grasp domain.
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DR EMBL; CP000577; ABN77729.1; -; Genomic_DNA.
DR RefSeq; YP_001044501.1; NC_009049.1.
DR ProteinModelPortal; A3PN13; -.
DR SMR; A3PN13; 1-395.
DR STRING; 349101.Rsph17029_2627; -.
DR PRIDE; A3PN13; -.
DR EnsemblBacteria; ABN77729; ABN77729; Rsph17029_2627.
DR GeneID; 4897491; -.
DR KEGG; rsh:Rsph17029_2627; -.
DR PATRIC; 23173155; VBIRhoSph114483_2867.
DR eggNOG; COG0045; -.
DR HOGENOM; HOG000007059; -.
DR KO; K01903; -.
DR OMA; QPVTKIL; -.
DR ProtClustDB; PRK00696; -.
DR BioCyc; RSPH349101:GHC8-3770-MONOMER; -.
DR UniPathway; UPA00223; UER00999.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:HAMAP.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:HAMAP.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.30.470.20; -; 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; IPR013816; ATP_grasp_subdomain_2.
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; CoA_ligase; 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; Manganese;
KW Metal-binding; Nucleotide-binding; Tricarboxylic acid cycle.
FT CHAIN 1 397 Succinyl-CoA ligase [ADP-forming] subunit
FT beta.
FT /FTId=PRO_1000082195.
FT DOMAIN 9 254 ATP-grasp.
FT NP_BIND 35 118 ATP (By similarity).
FT METAL 207 207 Magnesium or manganese (By similarity).
FT METAL 209 209 Magnesium or manganese (By similarity).
SQ SEQUENCE 397 AA; 42228 MW; A4D16F1C201AC264 CRC64;
MNIHEYQAKA LLRSYGAPVS DGRVVLKADE AKSAAGELGG PLWVVKAQIH AGGRGKGKFK
EPEAGEKGGV RLAKSVGEAA ELAKQMLGRT LVTHQTGPAG KQVNRIYIEE GSDIARELYL
ALLVDRGTSR ISFVVSTEGG MDIEEVAAST PEKIVSFSVD PASGLSDFHG RRVAFALGLE
GAQVKQCVQL VKNLYRAFVE KDMEMLEINP LIVMTDGNLK VLDAKVGFDN NALYRQSDVM
ALRDETEEDP KELAASKFDL NYIALDGEIG CMVNGAGLAM ATMDIIKLYG AEPANFLDVG
GGATKEKVTE AFKIITSDPN VKGILVNIFG GIMRCDIIAE GIIAAVKEVG LQVPLVVRLE
GTNVEKGKEI IANSGLNVIA GDNLSDAAQK IVKAVKG
//
