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Database: UniProt
Entry: P53587
LinkDB: P53587
Original site: P53587 
ID   SUCB_NEOFR              Reviewed;         437 AA.
AC   P53587;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   05-DEC-2018, entry version 101.
DE   RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta, hydrogenosomal {ECO:0000305|PubMed:9003318};
DE            EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_03219};
DE   AltName: Full=Succinyl-CoA synthetase beta chain {ECO:0000255|HAMAP-Rule:MF_03219, ECO:0000303|PubMed:9003318};
DE            Short=SCS-beta {ECO:0000255|HAMAP-Rule:MF_03219};
DE   Flags: Precursor;
GN   Name=SCSB {ECO:0000303|PubMed:9003318};
OS   Neocallimastix frontalis (Rumen fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Neocallimastigomycetes; Neocallimastigales; Neocallimastigaceae;
OC   Neocallimastix.
OX   NCBI_TaxID=4757;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC   STRAIN=MCH3;
RX   PubMed=9003318; DOI=10.1007/s004380050327;
RA   Brondijk T.H.C., van der Giezen M., Gottschal J.C., Prins R.A.,
RA   Fevre M.;
RT   "scsB, a cDNA encoding the hydrogenosomal beta subunit of succinyl-CoA
RT   synthetase fom the anerobic fungus Neocallimastix frontalis.";
RL   Mol. Gen. Genet. 253:315-323(1996).
CC   -!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid
CC       cycle (TCA), coupling the hydrolysis of succinyl-CoA to the
CC       synthesis of ATP and thus represents the only step of substrate-
CC       level phosphorylation in the TCA. The beta subunit provides
CC       nucleotide specificity of the enzyme and binds the substrate
CC       succinate, while the binding sites for coenzyme A and phosphate
CC       are found in the alpha subunit. {ECO:0000255|HAMAP-Rule:MF_03219}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + succinate = ADP + phosphate + succinyl-CoA;
CC         Xref=Rhea:RHEA:17661, ChEBI:CHEBI:30031, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC         ChEBI:CHEBI:456216; EC=6.2.1.5; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03219};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03219};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_03219};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       succinate from succinyl-CoA (ligase route): step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_03219}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_03219}.
CC   -!- SUBCELLULAR LOCATION: Hydrogenosome {ECO:0000269|PubMed:9003318}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta
CC       subunit family. {ECO:0000255|HAMAP-Rule:MF_03219}.
DR   EMBL; X84222; CAB41451.1; -; mRNA.
DR   PIR; S52384; S52384.
DR   ProteinModelPortal; P53587; -.
DR   SMR; P53587; -.
DR   PRIDE; P53587; -.
DR   UniPathway; UPA00223; UER00999.
DR   GO; GO:0042566; C:hydrogenosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1490.20; -; 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; 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; SSF52210; 1.
DR   TIGRFAMs; TIGR01016; sucCoAbeta; 1.
DR   PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Hydrogenosome; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT       1     27       Hydrogenosome.
FT   CHAIN        28    437       Succinate--CoA ligase [ADP-forming]
FT                                subunit beta, hydrogenosomal.
FT                                /FTId=PRO_0000033360.
FT   DOMAIN       36    278       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_03219}.
FT   NP_BIND      80     82       ATP. {ECO:0000255|HAMAP-Rule:MF_03219}.
FT   REGION      356    358       Substrate binding; shared with subunit
FT                                alpha. {ECO:0000255|HAMAP-Rule:MF_03219}.
FT   METAL       233    233       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_03219}.
FT   METAL       247    247       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_03219}.
FT   BINDING      73     73       ATP. {ECO:0000255|HAMAP-Rule:MF_03219}.
FT   BINDING     141    141       ATP. {ECO:0000255|HAMAP-Rule:MF_03219}.
FT   BINDING     299    299       Substrate; shared with subunit alpha.
FT                                {ECO:0000255|HAMAP-Rule:MF_03219}.
SQ   SEQUENCE   437 AA;  47153 MW;  556737C83A27F71D CRC64;
     MLANVTRSTS KAAPALASIA QTAQKRFLSV HEYCSMNLLH EYNVNAPKGI VAKTPEEAYQ
     AAKKLNTEDL VIKAQVLAGG RGKGHFDSGL QGGVKLCYTP EQVKDYASKM LGHKLITKQT
     GAAGRDCNAV YVVERQYAAR EYYFAILLDR ATRGPVLVAS SEGGVEIEEV AKTNPDAILT
     VPFSIKTGLT REVALDTAKK MGFTEKCVPQ AADTFMKLYK IFIEKDATMV EINPMAENNR
     GEVVCMDAKF GFDDNASYKP KGIFALRDTT QEDPREVAGH AKWNLNYVGM EGNIGCLVNG
     AGLAMATMDI IKLNGGVPAN FLDVGGSATA KQVKEAFKII SSDKAVSAIL VNIFGGIMRC
     DIVAEGVIQA VKELGLDIPL VVRLQGTKVE EARELIKNSN LSLYAIDDLD KAAKKVVQLA
     NVVGLAKENG IKIKIEN
//
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