SUCB_TRIVA
ID SUCB_TRIVA Reviewed; 407 AA.
AC Q03184;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta, hydrogenosomal {ECO:0000305|PubMed:1400232};
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:1400232};
DE Short=SCS-beta {ECO:0000255|HAMAP-Rule:MF_03219};
DE Flags: Precursor;
OS Trichomonas vaginalis.
OC Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae;
OC Trichomonas.
OX NCBI_TaxID=5722;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 10-21, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 30001 / NIH-C1;
RX PubMed=1400232; DOI=10.1128/jb.174.21.6822-6830.1992;
RA Lahti C.J., D'Oliveira C.E., Johnson P.J.;
RT "Beta-succinyl-coenzyme A synthetase from Trichomonas vaginalis is a
RT soluble hydrogenosomal protein with an amino-terminal sequence that
RT resembles mitochondrial presequences.";
RL J. Bacteriol. 174:6822-6830(1992).
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:1400232}.
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; M97553; AAA30326.1; -; Genomic_DNA.
DR PIR; A45242; A45242.
DR AlphaFoldDB; Q03184; -.
DR SMR; Q03184; -.
DR STRING; 5722.XP_001322061.1; -.
DR VEuPathDB; TrichDB:TVAG_259190; -.
DR eggNOG; KOG2799; Eukaryota.
DR BioCyc; MetaCyc:MON-13302; -.
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 ATP-binding; Direct protein sequencing; Hydrogenosome; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..9
FT /note="Hydrogenosome"
FT /evidence="ECO:0000269|PubMed:1400232"
FT CHAIN 10..407
FT /note="Succinate--CoA ligase [ADP-forming] subunit beta,
FT hydrogenosomal"
FT /id="PRO_0000033361"
FT DOMAIN 18..261
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT BINDING 62..64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT BINDING 124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT BINDING 281
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT BINDING 338..340
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
SQ SEQUENCE 407 AA; 43829 MW; 123C1F3D0A0E896B CRC64;
MLSSSFARNF NILEWQSKEI CAKYNVAAGI NLVARSPEEA AEAFRKMNLP AAVIKAQVYC
GGRGKGHWLE TGFKSGVHFV KSADEAAKIA KEMLGHHLVT KQTGKDGLLC QAVMLSDPVE
VKRELYFAIL LDRQTQSPVV IASTEGGVEI EEVAAHHPEK IHKFVLDGVE GITEEVAKNI
STKLGLTGKA YDNGVVEMQK LWKLFVGSDA TQVEVNPLAE TTDGRIITVD SKFNFDDSAH
YRQKQIFGYR DLKQVNPFEI RAEKYGLNYV PLDGNVACLV NGAGLAMATM DVIKLAGGDP
ANFLDLGGAA SEAAVTEGFT IISQQSHVKA ILVNIFGGIV RCDMVAAGVI AAFKKVGLKV
PLVVRLEGTN VEAGKKLIRE SGLPIISADN LTDAGEKAVK AAKGEKF
