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Database: UniProt
Entry: Q03184
LinkDB: Q03184
Original site: Q03184 
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
//
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