ID X5K723_9FLAO Unreviewed; 397 AA.
AC X5K723; A0A085CCX0; A0A117VAH2; A0A1T3ECN7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta {ECO:0000256|HAMAP-Rule:MF_00558};
DE EC=6.2.1.5 {ECO:0000256|HAMAP-Rule:MF_00558};
DE AltName: Full=Succinyl-CoA synthetase subunit beta {ECO:0000256|HAMAP-Rule:MF_00558};
DE Short=SCS-beta {ECO:0000256|HAMAP-Rule:MF_00558};
GN Name=sucC {ECO:0000256|HAMAP-Rule:MF_00558,
GN ECO:0000313|EMBL:AQX50460.1};
GN ORFNames=AYC66_07155 {ECO:0000313|EMBL:AQX50460.1}, BAY09_05425
GN {ECO:0000313|EMBL:OPB48398.1}, BBD32_10535
GN {ECO:0000313|EMBL:AQX01868.1}, NCTC10588_02660
GN {ECO:0000313|EMBL:STD07565.1};
OS Elizabethkingia anophelis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Elizabethkingia.
OX NCBI_TaxID=1117645 {ECO:0000313|EMBL:AQX01868.1, ECO:0000313|Proteomes:UP000190848};
RN [1] {ECO:0000313|EMBL:AQX50460.1, ECO:0000313|Proteomes:UP000189738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E6809 {ECO:0000313|EMBL:AQX50460.1,
RC ECO:0000313|Proteomes:UP000189738};
RA Nicholson A.C., Humrighouse B.W., Loparev V., Emery B., Graziano J.,
RA McQuiston J.R.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OPB48398.1, ECO:0000313|Proteomes:UP000189738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E6809 {ECO:0000313|EMBL:OPB48398.1,
RC ECO:0000313|Proteomes:UP000189738};
RA Nicholson A.C.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AQX01868.1, ECO:0000313|Proteomes:UP000190848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F3201 {ECO:0000313|EMBL:AQX01868.1,
RC ECO:0000313|Proteomes:UP000190848};
RA Nicholson A.C.;
RT "Revisiting the taxonomy of the Elizabethkingia Genus using Whole-Genome
RT Sequencing, Optical Mapping, and MALDI-TOF, along with proposal of three
RT novel Elizabethkingia species: Elizabethkingia bruuniana sp. nov.,
RT Elizabethkingia ursingii sp. nov., and Elizabethkingia occulta sp. nov.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:STD07565.1, ECO:0000313|Proteomes:UP000254876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10588 {ECO:0000313|EMBL:STD07565.1,
RC ECO:0000313|Proteomes:UP000254876};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle
CC (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of
CC either ATP or 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:0000256|HAMAP-Rule:MF_00558}.
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:0000256|HAMAP-
CC Rule:MF_00558};
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; Evidence={ECO:0000256|HAMAP-Rule:MF_00558};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00558};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00558};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1. {ECO:0000256|HAMAP-
CC Rule:MF_00558}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00558}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC family. {ECO:0000256|HAMAP-Rule:MF_00558}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00558}.
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DR EMBL; CP016374; AQX01868.1; -; Genomic_DNA.
DR EMBL; CP014339; AQX50460.1; -; Genomic_DNA.
DR EMBL; MAHS01000011; OPB48398.1; -; Genomic_DNA.
DR EMBL; UFYD01000001; STD07565.1; -; Genomic_DNA.
DR RefSeq; WP_009085002.1; NZ_VTFI01000007.1.
DR GeneID; 78267704; -.
DR OrthoDB; 9802602at2; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000189738; Chromosome.
DR Proteomes; UP000190848; Chromosome.
DR Proteomes; UP000254876; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR HAMAP; MF_00558; Succ_CoA_beta; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR InterPro; IPR005811; SUCC_ACL_C.
DR InterPro; IPR005809; Succ_CoA_ligase-like_bsu.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR NCBIfam; TIGR01016; sucCoAbeta; 1.
DR PANTHER; PTHR11815:SF10; SUCCINATE--COA LIGASE [ADP-FORMING] SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11815; SUCCINYL-COA SYNTHETASE BETA CHAIN; 1.
DR Pfam; PF08442; ATP-grasp_2; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR PIRSF; PIRSF001554; SucCS_beta; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00558, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00558};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00558};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00558};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00558}; Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00558}.
FT DOMAIN 9..236
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT BINDING 57..59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT BINDING 106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT BINDING 116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT BINDING 208
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT BINDING 273
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT BINDING 330..332
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
SQ SEQUENCE 397 AA; 42474 MW; 280C9860E0C27F58 CRC64;
MNLHEYQSKE ILAKYGVAIQ RGFVANNVDE AVAAAEKLTA ETGAQGWVVK AQIHAGGRGK
GGGVKFSPNM DKLKENAGNI IGMQLITPQT SAEGKKVNSV LVAEDVYYPG ETETKEFYVS
ILLDRALGKN TVVYSTEGGM DIEHVAEVTP HLIHKEVIDA AYGLQGFQAR KIAFNLGLEG
NAFKEFVKFI GSLYNAYVGI DASLFEINPV LKTSDNKIIA VDAKVTLDDN ALYRHKDLAE
LRDTREEDPM DVEAGEAGLN FVKLDGNVAC MVNGAGLAMA TMDIIKLSGG NPANFLDVGG
TADAQRVQTA FGIILRDPNV KAILINIFGG IVRCDRVAQG VVDAYKAMGS LPVPLIVRLQ
GTNAVEAKQL IDDSGLPVHS AITLEEAANK VKEVLAS
//
