ID   SUCB1_MACFA             Reviewed;         463 AA.
AC   Q4R517;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   16-JUN-2009, entry version 34.
DE   RecName: Full=Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial;
DE            EC=6.2.1.5;
DE   AltName: Full=Succinyl-CoA synthetase beta-A chain;
DE            Short=SCS-betaA;
DE   AltName: Full=ATP-specific succinyl-CoA synthetase subunit beta;
DE   Flags: Precursor;
GN   Name=SUCLA2; ORFNames=QflA-11886;
OS   Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Frontal cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + succinate + CoA = ADP + phosphate +
CC       succinyl-CoA.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By 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; AB169727; BAE01808.1; -; mRNA.
DR   HOVERGEN; Q4R517; -.
DR   BRENDA; 6.2.1.5; 3438.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:EC.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR011761; ATP-grasp.
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; 1.
DR   PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW   Phosphoprotein; Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT       1     52       Mitochondrion (By similarity).
FT   CHAIN        53    463       Succinyl-CoA ligase [ADP-forming] subunit
FT                                beta, mitochondrial.
FT                                /FTId=PRO_0000270821.
FT   DOMAIN       61    288       ATP-grasp.
FT   MOD_RES      84     84       Phosphotyrosine (By similarity).
FT   MOD_RES     279    279       Phosphoserine (By similarity).
SQ   SEQUENCE   463 AA;  49960 MW;  C960AA81E3F78E2D CRC64;
     MAASVFYGRL LAVATLRNHR PRTALGAAAQ VLGSSGLFNN HGLQVQQQQQ RNLSLHEYMS
     MELLQEAGVS IPKGCVAKSP DEAYAVAKKL GSKDVVIKAQ VLAGGRGKGT FESGLKGGVK
     IVFSPEEAKA VSSQMIGKKL FTKQTGEKGR ICNQVLVCER KYPRREYYFA ITMERSFQGP
     VLIGSSQGGV NIEDVAAETP EAIITEPIDI EEGIKKEQAL QLAQKMGFPP NIVESAAENM
     VKLYSLFLKY DATMIEINPM VEDSDGAVLC MDAKINFDSN SAYRQKKIFD LQDWTQEDER
     DKDAAQANLN YIGLDGNIGC LVNGAGLAMA TMDIIKLHGG TPANFLDVGG GATVHQVTEA
     FKLITSDKKV LAILVNIFGG IMSCDVIAQG IVTALKDLEI KIPVVVRLQG TRVDDAKALI
     AGSGLKILAC DDLDEAARMV VKLSEIVTLA KQAHVDVKFQ LPI
//