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 01-MAY-2013, entry version 68.
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=ACIAD2873;
OS Acinetobacter sp. (strain ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Moraxellaceae; Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=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 -!- 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; CR543861; CAG69601.1; -; Genomic_DNA.
DR RefSeq; YP_047423.1; NC_005966.1.
DR ProteinModelPortal; Q6F8L4; -.
DR STRING; 62977.ACIAD2873; -.
DR PRIDE; Q6F8L4; -.
DR EnsemblBacteria; CAG69601; CAG69601; ACIAD2873.
DR GeneID; 2879236; -.
DR KEGG; aci:ACIAD2873; -.
DR PATRIC; 20743267; VBIAciSp98416_2570.
DR eggNOG; COG0045; -.
DR HOGENOM; HOG000007059; -.
DR KO; K01903; -.
DR OMA; QPVTKIL; -.
DR ProtClustDB; PRK00696; -.
DR BioCyc; ASP62977:GJVV-2664-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 1 388 Succinyl-CoA ligase [ADP-forming] subunit
FT beta.
FT /FTId=PRO_0000102814.
FT DOMAIN 9 245 ATP-grasp.
FT NP_BIND 35 109 ATP (By similarity).
FT METAL 198 198 Magnesium or manganese (By similarity).
FT METAL 200 200 Magnesium or manganese (By similarity).
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
//
