SUCB2_COLLI
ID SUCB2_COLLI Reviewed; 391 AA.
AC Q9YI36;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03221};
DE EC=6.2.1.4 {ECO:0000255|HAMAP-Rule:MF_03221, ECO:0000269|PubMed:9765290};
DE AltName: Full=GTP-specific succinyl-CoA synthetase subunit beta {ECO:0000255|HAMAP-Rule:MF_03221};
DE Short=G-SCS {ECO:0000255|HAMAP-Rule:MF_03221};
DE Short=GTPSCS {ECO:0000255|HAMAP-Rule:MF_03221};
DE AltName: Full=Succinyl-CoA synthetase beta-G chain {ECO:0000255|HAMAP-Rule:MF_03221};
DE Short=SCS-betaG {ECO:0000255|HAMAP-Rule:MF_03221};
DE Flags: Fragment;
GN Name=SUCLG2 {ECO:0000255|HAMAP-Rule:MF_03221};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 110-119, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=9765291; DOI=10.1074/jbc.273.42.27580;
RA Johnson J.D., Mehus J.G., Tews K., Milavetz B.I., Lambeth D.O.;
RT "Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA
RT synthetases in multicellular eucaryotes.";
RL J. Biol. Chem. 273:27580-27586(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9765290; DOI=10.1074/jbc.273.42.27573;
RA Johnson J.D., Muhonen W.W., Lambeth D.O.;
RT "Characterization of the ATP- and GTP-specific succinyl-CoA synthetases in
RT pigeon. The enzymes incorporate the same alpha-subunit.";
RL J. Biol. Chem. 273:27573-27579(1998).
CC -!- FUNCTION: GTP-specific succinyl-CoA synthetase functions in the citric
CC acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the
CC synthesis of GTP and thus represents the only step of substrate-level
CC phosphorylation in the TCA. The beta subunit provides nucleotide
CC specificity of the enzyme and binds the substrate succinate, while the
CC binding sites for coenzyme A and phosphate are found in the alpha
CC subunit. {ECO:0000255|HAMAP-Rule:MF_03221, ECO:0000269|PubMed:9765290}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CoA + GTP + succinate = GDP + phosphate + succinyl-CoA;
CC Xref=Rhea:RHEA:22120, ChEBI:CHEBI:30031, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC ChEBI:CHEBI:58189; EC=6.2.1.4; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03221, ECO:0000269|PubMed:9765290};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03221};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03221};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.036 mM for GTP {ECO:0000269|PubMed:9765290};
CC KM=0.007 mM for GDP {ECO:0000269|PubMed:9765290};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_03221, ECO:0000305|PubMed:9765290}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta subunit
CC determines specificity for GTP. {ECO:0000255|HAMAP-Rule:MF_03221,
CC ECO:0000269|PubMed:9765290}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03221,
CC ECO:0000269|PubMed:9765290}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Not present in breast muscle.
CC {ECO:0000269|PubMed:9765291}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC family. GTP-specific subunit beta subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_03221}.
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DR EMBL; AF043541; AAC69706.1; -; mRNA.
DR AlphaFoldDB; Q9YI36; -.
DR SMR; Q9YI36; -.
DR STRING; 8932.XP_005505679.1; -.
DR eggNOG; KOG1447; Eukaryota.
DR SABIO-RK; Q9YI36; -.
DR UniPathway; UPA00223; UER00999.
DR GO; GO:0005739; C:mitochondrion; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0006104; P:succinyl-CoA metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.261; -; 1.
DR HAMAP; MF_00558; Succ_CoA_beta; 1.
DR HAMAP; MF_03221; Succ_CoA_betaG_euk; 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; IPR034722; Succ_CoA_betaG_euk.
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 Direct protein sequencing; GTP-binding; Ligase; Magnesium; Metal-binding;
KW Mitochondrion; Nucleotide-binding; Tricarboxylic acid cycle.
FT CHAIN <1..391
FT /note="Succinate--CoA ligase [GDP-forming] subunit beta,
FT mitochondrial"
FT /id="PRO_0000413702"
FT DOMAIN 5..233
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT BINDING 16
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT BINDING 49..51
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT BINDING 105
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT BINDING 202
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT BINDING 267
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT BINDING 324..326
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT SITE 38
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT SITE 106
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT NON_TER 1
SQ SEQUENCE 391 AA; 42343 MW; C019F16B1DD3123A CRC64;
EYQSKKIMAD HGVTVQRFFV ADSANDALEA AQRLKAKEIV LKAQILAGGR GKGVFNSGLK
GGVHLTKDPK IVEQLAKQMI GYNLSTKQTP KDGVTVKKVM VAEALNISRE TYFAILMDRA
CNGPVMVGSP QGGVDIEEVA VTSPELIFKE EIDIFEGIKD HQALQMAKNL GFKGPLQQQA
ADQIKKLYNL FLKIDATQVE VNPFGETPEG QVVCFDAKIN FDDNAEFRQK EIFAMDDKSE
NEPIENEAAK YDLKYIGLDG NIACFVNGAG LAMATCDIIS LNGGKPANFL DLGGGVKEAQ
VYQAFKLLTA DPKVEAILVN IFGGIVNCAI IANGITRACR ELELKVPLVV RLEGTNVHEA
QRILNESGLP IMSANDLEDA AKKAVASVAK K
