ID SUCC_ACTPJ Reviewed; 388 AA.
AC B0BTV5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 01-MAY-2013, entry version 42.
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=APJL_0479;
OS Actinobacillus pleuropneumoniae serotype 3 (strain JL03).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=434271;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JL03;
RX PubMed=18197260; DOI=10.1371/journal.pone.0001450;
RA Xu Z., Zhou Y., Li L., Zhou R., Xiao S., Wan Y., Zhang S., Wang K.,
RA Li W., Li L., Jin H., Kang M., Dalai B., Li T., Liu L., Cheng Y.,
RA Zhang L., Xu T., Zheng H., Pu S., Wang B., Gu W., Zhang X.L.,
RA Zhu G.-F., Wang S., Zhao G.-P., Chen H.;
RT "Genome biology of Actinobacillus pleuropneumoniae JL03, an isolate of
RT serotype 3 prevalent in China.";
RL PLoS ONE 3:E1450-E1450(2008).
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP000687; ABY69060.1; -; Genomic_DNA.
DR RefSeq; YP_001651504.1; NC_010278.1.
DR ProteinModelPortal; B0BTV5; -.
DR SMR; B0BTV5; 1-388.
DR STRING; 434271.APJL_0479; -.
DR PRIDE; B0BTV5; -.
DR EnsemblBacteria; ABY69060; ABY69060; APJL_0479.
DR GeneID; 5851617; -.
DR KEGG; apj:APJL_0479; -.
DR PATRIC; 20750192; VBIActPle136345_0483.
DR eggNOG; COG0045; -.
DR HOGENOM; HOG000007059; -.
DR KO; K01903; -.
DR OMA; NTIYLEE; -.
DR ProtClustDB; PRK00696; -.
DR BioCyc; APLE434271:GIX7-479-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; 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; FALSE_NEG.
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 1 388 Succinyl-CoA ligase [ADP-forming] subunit
FT beta.
FT /FTId=PRO_1000129154.
FT DOMAIN 9 244 ATP-grasp.
FT NP_BIND 35 108 ATP (By similarity).
FT METAL 197 197 Magnesium or manganese (By similarity).
FT METAL 199 199 Magnesium or manganese (By similarity).
SQ SEQUENCE 388 AA; 41871 MW; 157CD52A0ADE5C1B CRC64;
MNLHEYQAKQ IFAQYRLPVS KGIVCHSLDD AVSAIHTLAG DTWAAKCQVH AGGRGKAGGV
KLVRSEAEIR EFCHQWLGQR LVTFQTDKNG QLVNTIYLEE TCLIERELYL GAVIDRSSQK
IVFMASNAGG MNIEDVAAQT PELIHKATID PLTGAQAFQG RELAFKLGLS GDQIKQFAHL
FVQLAKLFIE KDLALLEVNP LVLTKQGQLL CLDAKMVIDS NALYRHPELK ALQDPSQEDA
READAAKWDL NYVALDGNIG CMVNGAGLAM GTMDIVKLHG GRPANFLDVG GGATKERVSE
AFKLILSDQN VKAVLVNIFG GIVRCDLIAE GIIAAVNEVG INIPVIVRLE GTNAELGREI
LANSGLRLIA ANTLTQAAQL AVKAAEGK
//