ID H2IWJ8_RAHAC Unreviewed; 388 AA.
AC H2IWJ8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
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 OrderedLocusNames=Rahaq2_3178 {ECO:0000313|EMBL:AEX52993.1};
OS Rahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 /
OS NCIMB 13365 / CIP 78.65).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Rahnella.
OX NCBI_TaxID=745277 {ECO:0000313|EMBL:AEX52993.1, ECO:0000313|Proteomes:UP000009010};
RN [1] {ECO:0000313|EMBL:AEX52993.1, ECO:0000313|Proteomes:UP000009010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 /
RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010};
RX PubMed=22582378; DOI=10.1128/JB.00380-12;
RA Martinez R.J., Bruce D., Detter C., Goodwin L.A., Han J., Han C.S.,
RA Held B., Land M.L., Mikhailova N., Nolan M., Pennacchio L., Pitluck S.,
RA Tapia R., Woyke T., Sobecky P.A.;
RT "Complete Genome Sequence of Rahnella aquatilis CIP 78.65.";
RL J. Bacteriol. 194:3020-3021(2012).
RN [2] {ECO:0000313|Proteomes:UP000009010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 /
RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Held B., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sobecky P.,
RA Martinez R., Woyke T.;
RT "Complete sequence of chromosome of Rahnella aquatilis CIP 78.65.";
RL Submitted (JAN-2012) 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}.
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DR EMBL; CP003244; AEX52993.1; -; Genomic_DNA.
DR RefSeq; WP_013576437.1; NZ_JMPO01000114.1.
DR AlphaFoldDB; H2IWJ8; -.
DR STRING; 745277.Rahaq2_3178; -.
DR GeneID; 61513187; -.
DR KEGG; raq:Rahaq2_3178; -.
DR PATRIC; fig|745277.3.peg.3048; -.
DR eggNOG; COG0045; Bacteria.
DR HOGENOM; CLU_037430_0_2_6; -.
DR OrthoDB; 9802602at2; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000009010; Chromosome.
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:0004776; F:succinate-CoA ligase (GDP-forming) activity; IEA:RHEA.
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}; Reference proteome {ECO:0000313|Proteomes:UP000009010};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW Rule:MF_00558}.
FT DOMAIN 9..229
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT BINDING 53..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT BINDING 102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT BINDING 199
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT BINDING 264
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT BINDING 321..323
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
SQ SEQUENCE 388 AA; 41464 MW; DDDB820DB0C1AFA6 CRC64;
MNLHEYQAKQ LFLRYGLPAP TGFACSTPRE AEEAASKIGA GPWVVKCQVH AGGRGKAGGV
KVVKSKEEIR AFAEHWLGKR LVTYQTDASG QPVNQILVEA ATDIDQELYL GAVVDRSSRR
VVFMASTEGG VEIEKVAEET PHLIHKVALD PLAGPQPYQG RELAFKLGLT GKQVQQFTKI
FMGLANIFLE RDLALIEINP LVVTTAGDLI CLDGKLGADG NALFRQPELR EMRDYSQEDA
RESQAAQWEL NYVALDGNIG CMVNGAGLAM GTMDIVKLHG GEPANFLDVG GGATKERVTE
AFKIILSDEK VKAVFVNIFG GIVRCDLIAD GIIGAVEEVG VSVPVVVRLE GNNAELGAKK
LADSGLNIIA ATSLTNAAQQ VVAAVEGK
//