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 05-DEC-2018, entry version 105.
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; Parabasalia; Trichomonadida; Trichomonadidae; 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
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:1400232}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta
CC subunit family. {ECO:0000255|HAMAP-Rule:MF_03219}.
DR EMBL; M97553; AAA30326.1; -; Genomic_DNA.
DR PIR; A45242; A45242.
DR ProteinModelPortal; Q03184; -.
DR SMR; Q03184; -.
DR PRIDE; Q03184; -.
DR eggNOG; KOG2799; Eukaryota.
DR eggNOG; COG0045; LUCA.
DR BioCyc; MetaCyc:MONOMER-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;
KW Magnesium; Metal-binding; Nucleotide-binding; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1 9 Hydrogenosome.
FT {ECO:0000269|PubMed:1400232}.
FT CHAIN 10 407 Succinate--CoA ligase [ADP-forming]
FT subunit beta, hydrogenosomal.
FT /FTId=PRO_0000033361.
FT DOMAIN 18 261 ATP-grasp. {ECO:0000255|HAMAP-
FT Rule:MF_03219}.
FT NP_BIND 62 64 ATP. {ECO:0000255|HAMAP-Rule:MF_03219}.
FT REGION 338 340 Substrate binding; shared with subunit
FT alpha. {ECO:0000255|HAMAP-Rule:MF_03219}.
FT METAL 216 216 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_03219}.
FT METAL 230 230 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_03219}.
FT BINDING 55 55 ATP. {ECO:0000255|HAMAP-Rule:MF_03219}.
FT BINDING 124 124 ATP. {ECO:0000255|HAMAP-Rule:MF_03219}.
FT BINDING 281 281 Substrate; shared with subunit alpha.
FT {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
//
