SUCC_CAMJR
ID SUCC_CAMJR Reviewed; 387 AA.
AC Q5HVN3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta {ECO:0000255|HAMAP-Rule:MF_00558};
DE EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_00558};
DE AltName: Full=Succinyl-CoA synthetase subunit beta {ECO:0000255|HAMAP-Rule:MF_00558};
DE Short=SCS-beta {ECO:0000255|HAMAP-Rule:MF_00558};
GN Name=sucC {ECO:0000255|HAMAP-Rule:MF_00558}; OrderedLocusNames=CJE0637;
OS Campylobacter jejuni (strain RM1221).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=195099;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM1221;
RX PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
RA Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
RA Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
RA Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
RA Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
RA Nelson K.E.;
RT "Major structural differences and novel potential virulence mechanisms from
RT the genomes of multiple Campylobacter species.";
RL PLoS Biol. 3:72-85(2005).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_00558};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00558};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00558};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00558}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00558}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_00558}.
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DR EMBL; CP000025; AAW35850.1; -; Genomic_DNA.
DR RefSeq; WP_002858590.1; NC_003912.7.
DR PDB; 6MEL; X-ray; 2.06 A; B=1-387.
DR PDBsum; 6MEL; -.
DR AlphaFoldDB; Q5HVN3; -.
DR SMR; Q5HVN3; -.
DR KEGG; cjr:CJE0637; -.
DR HOGENOM; CLU_037430_0_2_7; -.
DR OMA; ITACDEV; -.
DR UniPathway; UPA00223; UER00999.
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; -; 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 3D-structure; ATP-binding; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Tricarboxylic acid cycle.
FT CHAIN 1..387
FT /note="Succinate--CoA ligase [ADP-forming] subunit beta"
FT /id="PRO_1000082056"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 53..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 199
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 264
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 321..323
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:6MEL"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:6MEL"
FT HELIX 28..38
FT /evidence="ECO:0007829|PDB:6MEL"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:6MEL"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:6MEL"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:6MEL"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:6MEL"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:6MEL"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:6MEL"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:6MEL"
FT STRAND 104..115
FT /evidence="ECO:0007829|PDB:6MEL"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:6MEL"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:6MEL"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:6MEL"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:6MEL"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:6MEL"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:6MEL"
FT HELIX 157..166
FT /evidence="ECO:0007829|PDB:6MEL"
FT HELIX 171..190
FT /evidence="ECO:0007829|PDB:6MEL"
FT STRAND 193..204
FT /evidence="ECO:0007829|PDB:6MEL"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:6MEL"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:6MEL"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:6MEL"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:6MEL"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:6MEL"
FT HELIX 240..247
FT /evidence="ECO:0007829|PDB:6MEL"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:6MEL"
FT STRAND 256..265
FT /evidence="ECO:0007829|PDB:6MEL"
FT HELIX 266..278
FT /evidence="ECO:0007829|PDB:6MEL"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:6MEL"
FT HELIX 295..305
FT /evidence="ECO:0007829|PDB:6MEL"
FT STRAND 313..323
FT /evidence="ECO:0007829|PDB:6MEL"
FT HELIX 325..335
FT /evidence="ECO:0007829|PDB:6MEL"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:6MEL"
FT STRAND 345..351
FT /evidence="ECO:0007829|PDB:6MEL"
FT HELIX 354..363
FT /evidence="ECO:0007829|PDB:6MEL"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:6MEL"
FT HELIX 375..385
FT /evidence="ECO:0007829|PDB:6MEL"
SQ SEQUENCE 387 AA; 41752 MW; 4E56113D35E937E9 CRC64;
MNIHEYQAKA IFVDNGIPTL KGKVAFSVDE AVANAKELGG SVWAVKAQIH AGGRGLGGGV
KIAKNLDEVK DYASKILGMN LVTHQTGPEG KLVQKLYIES GANIVKEYYL AILFNRMAEQ
ITIIASSEGG MDIEKVAKES PEKIAKVGID PQIGFKMFHG LEVARVLGLD KDEGKKLISM
IAKLYKLYMD KDMNMLEINP LIKTAEGDFY ALDAKCSFDD SALYRHPEIA ELRDTTEENP
AEREAAEFGL SYVKLDGDVA CMVNGAGLAM ATMDIINYSG AKPANFLDVG GGASPETVAK
AFEIILRDKN VKVIFINIFG GIVRCDRIAN GILEATKNVE VNIPIVVRLD GTNAAEAKTI
LDNSNLKNIK AATNLKNGAE LVKSLVG
