SUCB_NEOFR
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 03-AUG-2022, entry version 108.
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 Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Neocallimastix.
OX NCBI_TaxID=4757;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=MCH3;
RX PubMed=9003318; DOI=10.1007/pl00008598;
RA Brondijk T.H.C., van der Giezen M., Gottschal J.C., Prins R.A., 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 cycle
CC (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP
CC and thus represents the only step of substrate-level phosphorylation in
CC the TCA. The beta subunit provides nucleotide specificity of the enzyme
CC and binds the substrate succinate, while the binding sites for coenzyme
CC A and phosphate are found in the alpha subunit. {ECO:0000255|HAMAP-
CC 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-Rule:MF_03219};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC 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 subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_03219}.
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DR EMBL; X84222; CAB41451.1; -; mRNA.
DR PIR; S52384; S52384.
DR AlphaFoldDB; P53587; -.
DR SMR; 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
FT /note="Hydrogenosome"
FT CHAIN 28..437
FT /note="Succinate--CoA ligase [ADP-forming] subunit beta,
FT hydrogenosomal"
FT /id="PRO_0000033360"
FT DOMAIN 36..278
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT BINDING 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT BINDING 80..82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT BINDING 141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT BINDING 299
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT BINDING 356..358
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="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
