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-APR-2013, entry version 89.
DE RecName: Full=Succinyl-CoA ligase [GDP-forming] subunit beta, hydrogenosomal;
DE EC=6.2.1.4;
DE AltName: Full=Succinyl-CoA synthetase beta chain;
DE Short=SCS-beta;
DE Flags: Precursor;
OS Trichomonas vaginalis.
OC Eukaryota; Parabasalia; Trichomonadida; Trichomonadidae; Trichomonas.
OX NCBI_TaxID=5722;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 30001 / NIH-C1;
RX PubMed=1400232;
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 -!- CATALYTIC ACTIVITY: GTP + succinate + CoA = GDP + phosphate +
CC succinyl-CoA.
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC -!- SUBCELLULAR LOCATION: Hydrogenosome.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta
CC subunit family.
CC -!- SIMILARITY: Contains 1 ATP-grasp domain.
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DR EMBL; M97553; AAA30326.1; -; Genomic_DNA.
DR PIR; A45242; A45242.
DR ProteinModelPortal; Q03184; -.
DR STRING; 5722.Q03184; -.
DR eggNOG; COG0045; -.
DR BioCyc; MetaCyc:MONOMER-13302; -.
DR GO; GO:0042566; C:hydrogenosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IEA:EC.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.30.470.20; -; 1.
DR Gene3D; 3.40.50.261; -; 1.
DR InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR013816; ATP_grasp_subdomain_2.
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; CoA_ligase; 1.
DR TIGRFAMs; TIGR01016; sucCoAbeta; 1.
DR PROSITE; PS50975; ATP_GRASP; FALSE_NEG.
DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; GTP-binding; Hydrogenosome; Ligase;
KW Nucleotide-binding; Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1 9 Hydrogenosome.
FT CHAIN 10 407 Succinyl-CoA ligase [GDP-forming] subunit
FT beta, hydrogenosomal.
FT /FTId=PRO_0000033361.
FT DOMAIN 18 247 ATP-grasp.
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
//
