ID   SUCC_ANAPZ              Reviewed;         388 AA.
AC   Q2GJ42;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 29.
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=APH_1052;
OS   Anaplasma phagocytophilum (strain HZ).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma; phagocytophilum group.
OX   NCBI_TaxID=212042;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S.,
RA   Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N.,
RA   Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P.,
RA   Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H.,
RA   Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F.,
RA   Forberger H., Halpin R., Mulligan S., Robinson J., White O.,
RA   Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(2006).
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   -!- 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; CP000235; ABD44388.1; -; Genomic_DNA.
DR   RefSeq; YP_505609.1; -.
DR   GeneID; 3930725; -.
DR   GenomeReviews; CP000235_GR; APH_1052.
DR   KEGG; aph:APH_1052; -.
DR   NMPDR; fig|212042.5.peg.996; -.
DR   TIGR; APH_1052; -.
DR   HOGENOM; Q2GJ42; -.
DR   OMA; Q2GJ42; GLGTFKS.
DR   BioCyc; APHA212042:APH_1052-MON; -.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:HAMAP.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:HAMAP.
DR   HAMAP; MF_00558; -; 1.
DR   InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
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   Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1.
DR   Gene3D; G3DSA:3.40.50.261; Succinyl-CoA_synth-like; 1.
DR   PANTHER; PTHR11815; CoA_lig_beta; 1.
DR   Pfam; PF08442; ATP-grasp_2; 1.
DR   Pfam; PF00549; Ligase_CoA; 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_1000081999.
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;  41378 MW;  4B924E1E284DD8F5 CRC64;
     MNVHEFQAKG ILSGFDVRVP KGVVVRSVEE VDSALGSLAA GIVAVKAQIH AGGRGKAGGV
     KIGKAREEVA DLVKSMLGSV LVTHQTSAAG QKVHAVYLEE GVSIKKEYYL GAVVDRKAGM
     VSVIFSSEGG MDIEEVAHSR PEMVVVVNVD PVYGFLDFHG RKLCYGLGLK KEQVVQITAM
     ARKVCRALME TDASQVEINP LVETTCGEFI ALDAKMTFDD NGLFRRPEIV KLTDPHEYSE
     EELEAAKYGL SYIKLDGNIG CMVNGAGLAM ATMDIVKYYG GEPANFLDVG GGASKDTVRE
     AFKIILRSGV DGILVNIFGG IMRCDVIAAG IIESAKEIGV SVPMVVRLSG TNYKIGKEML
     DASGLSIVTA ENLDEAARFV VDLVGKRG
//