SUCB_BLAHN
ID SUCB_BLAHN Reviewed; 416 AA.
AC B3FHP0;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta {ECO:0000305|PubMed:18452512};
DE EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_03219, ECO:0000269|PubMed:18452512};
DE AltName: Full=Succinyl-CoA synthetase beta chain {ECO:0000255|HAMAP-Rule:MF_03219, ECO:0000303|PubMed:18452512};
DE Short=SCS-beta {ECO:0000255|HAMAP-Rule:MF_03219};
DE Flags: Precursor;
GN Name=SCSb;
OS Blastocystis sp. subtype 1 (strain ATCC 50177 / NandII).
OC Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Opalinata; Blastocystidae;
OC Blastocystis.
OX NCBI_TaxID=478820;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=ATCC 50177 / NandII;
RX PubMed=18452512; DOI=10.1111/j.1365-2958.2008.06228.x;
RA Hamblin K., Standley D.M., Rogers M.B., Stechmann A., Roger A.J.,
RA Maytum R., van der Giezen M.;
RT "Localization and nucleotide specificity of Blastocystis succinyl-CoA
RT synthetase.";
RL Mol. Microbiol. 68:1395-1405(2008).
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, ECO:0000269|PubMed:18452512}.
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, ECO:0000269|PubMed:18452512};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=68 uM for ATP {ECO:0000269|PubMed:18452512};
CC Note=kcat is 133 min(-1) with ATP as substrate.
CC {ECO:0000269|PubMed:18452512};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_03219, ECO:0000305|PubMed:18452512}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC {ECO:0000255|HAMAP-Rule:MF_03219}.
CC -!- SUBCELLULAR LOCATION: Hydrogenosome {ECO:0000269|PubMed:18452512}.
CC Note=Found in the matrix of the mitochondrion-like organelles (MLO) of
CC Blastocystis. {ECO:0000269|PubMed:18452512}.
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; EU076379; ABY62724.1; -; mRNA.
DR EMBL; EU076380; ABY62725.1; -; Genomic_DNA.
DR PDB; 6NO0; X-ray; 2.21 A; A/B=15-253.
DR PDB; 6NO1; X-ray; 2.44 A; A/B=15-253.
DR PDB; 6NO2; X-ray; 2.16 A; A/B=15-253.
DR PDB; 6NO3; X-ray; 1.94 A; A/B=15-253.
DR PDB; 6NO4; X-ray; 2.24 A; A/B=15-253.
DR PDB; 6NO5; X-ray; 2.07 A; A/B/C/D=15-253.
DR PDB; 6NO6; X-ray; 1.91 A; A/B=15-253.
DR PDBsum; 6NO0; -.
DR PDBsum; 6NO1; -.
DR PDBsum; 6NO2; -.
DR PDBsum; 6NO3; -.
DR PDBsum; 6NO4; -.
DR PDBsum; 6NO5; -.
DR PDBsum; 6NO6; -.
DR AlphaFoldDB; B3FHP0; -.
DR SMR; B3FHP0; -.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Hydrogenosome; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..14
FT /note="Hydrogenosome"
FT /evidence="ECO:0000255"
FT CHAIN 15..416
FT /note="Succinate--CoA ligase [ADP-forming] subunit beta"
FT /id="PRO_0000438595"
FT BINDING 64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT BINDING 71..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT BINDING 132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT BINDING 293
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT BINDING 350..352
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT SITE 60
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000305|PubMed:18452512"
FT SITE 128
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000305|PubMed:18452512"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:6NO6"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:6NO6"
FT HELIX 42..52
FT /evidence="ECO:0007829|PDB:6NO6"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:6NO6"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:6NO6"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:6NO3"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:6NO6"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:6NO6"
FT HELIX 91..101
FT /evidence="ECO:0007829|PDB:6NO6"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:6NO6"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:6NO6"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:6NO3"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:6NO6"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:6NO6"
FT STRAND 129..138
FT /evidence="ECO:0007829|PDB:6NO6"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:6NO3"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:6NO6"
FT HELIX 158..164
FT /evidence="ECO:0007829|PDB:6NO6"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:6NO6"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:6NO6"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:6NO6"
FT HELIX 182..191
FT /evidence="ECO:0007829|PDB:6NO6"
FT HELIX 197..215
FT /evidence="ECO:0007829|PDB:6NO6"
FT STRAND 219..230
FT /evidence="ECO:0007829|PDB:6NO6"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:6NO6"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:6NO6"
SQ SEQUENCE 416 AA; 45145 MW; C5DCDC95BC87C43A CRC64;
MLRMAPKTVG AVRNLNIHEW QSKQLIQKYG GRAQSGEVAF SPERSRDIAK KLWNQFPGCK
FVVKAQVLAG GRGKGHWEHG MQGGVKLAKT PEEVYEIANE MIGHKLITKQ TGAKGINCNK
VMVCGAVKIL KEFYLSILLD RAMGCPVIIA TSQGGMGIEE VAQKCPECLF KVPISVKNGP
TNEQLVKLAK DLGLEGDLVQ DCVDNVKALY QVFDKCDSTM VEINPLGVIE TPTDEKVICC
LDAKIAFDKD AAFRQKEIFA LRDKSREDPR DVRASLADLN YVGLDGDIGC MVNGAGLAMA
TMDTINYFGG SAANFLDVGG NAKKEQITEA LRILNSDKHV KSILINIFGG IMRCDVVAQG
IMDAVREMKL DLPLVVRLEG TNVAKGKEIL KSSGLNIIPA NDLGDAAKKA VASLKH
