P0A836 (SUCC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Succinyl-CoA ligase [ADP-forming] subunit beta
EC=6.2.1.5

Alternative name(s):
Succinyl-CoA synthetase subunit beta
Short name=SCS-beta

Gene names

Name:	sucC
Ordered Locus Names:	b0728, JW0717

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	388 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + succinate + CoA = ADP + phosphate + succinyl-CoA. HAMAP MF_00558
Cofactor	Binds 1 magnesium or manganese ion per subunit By similarity.
Enzyme regulation	Exhibits two interesting properties: "substrate synergism", in which the enzyme is most active for the catalysis of its partial reactions only when all the substrate binding sites are occupied, and "catalytic cooperativity" between alternating active sites in the tetramer, whereby the interaction of substrates (particularly ATP) at one site is needed to promote catalysis at the other. HAMAP MF_00558
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1. HAMAP MF_00558
Subunit structure	Heterotetramer of two alpha and two beta subunits.
Miscellaneous	Succinyl-CoA synthetase (SCS) of E.coli catalyzes its reaction via three steps that involve phosphoryl enzyme and enzyme-bound succinyl phosphate as intermediates. HAMAP MF_00558 During aerobic metabolism it functions in the citric acid cycle, coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents an important site of substrate-level phosphorylation. It can also function in the other direction for anabolic purposes, and this may be particularly important for providing succinyl-CoA during anaerobic growth when the oxidative route from 2-oxoglutarate is severely repressed. HAMAP MF_00558 The beta-subunit contains the attachment sites for succinate. The complete active site is probably located in the region of alpha- beta contact. HAMAP MF_00558
Sequence similarities	Belongs to the succinate/malate CoA ligase beta subunit family. Contains 1 ATP-grasp domain.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	tricarboxylic acid cycle Inferred from direct assay. Source: EcoliWiki
Cellular component	cytoplasm Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct succinate-CoA ligase (ADP-forming) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
sucD	P0AGE9	3	EBI-369117,EBI-369078

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 388

388

Succinyl-CoA ligase [ADP-forming] subunit beta HAMAP MF_00558

PRO_0000102832

Regions

Domain

9 – 244

236

ATP-grasp

Nucleotide binding

35 – 108

74

ATP By similarity

Sites

Metal binding

197

1

Magnesium or manganese By similarity

Metal binding

199

1

Magnesium or manganese By similarity

Secondary structure

1

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388

Helix Strand Turn

Details...

Helix

5 – 14

10

Beta strand

22 – 27

6

Helix

28 – 38

11

Beta strand

43 – 47

5

Beta strand

50 – 52

3

Turn

54 – 58

5

Beta strand

60 – 63

4

Helix

66 – 76

11

Beta strand

79 – 81

3

Beta strand

96 – 100

5

Beta strand

104 – 115

12

Turn

116 – 119

4

Beta strand

120 – 127

8

Helix

133 – 139

7

Helix

141 – 143

3

Beta strand

144 – 148

5

Turn

151 – 153

3

Helix

157 – 166

10

Helix

172 – 190

19

Beta strand

193 – 204

12

Beta strand

209 – 211

3

Beta strand

215 – 218

4

Helix

220 – 225

6

Helix

227 – 231

5

Helix

235 – 237

3

Helix

240 – 247

8

Beta strand

251 – 254

4

Beta strand

256 – 265

10

Helix

266 – 278

13

Beta strand

285 – 288

4

Helix

295 – 306

12

Beta strand

313 – 320

8

Helix

325 – 338

14

Beta strand

345 – 351

7

Helix

354 – 362

9

Beta strand

366 – 370

5

Helix

374 – 383

10

Turn

384 – 387

4

Sequences

	Sequence		Length	Mass (Da)
	P0A836 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: 09C429EC97A823CF	FASTA	388	41,393
	10 20 30 40 50 60 MNLHEYQAKQ LFARYGLPAP VGYACTTPRE AEEAASKIGA GPWVVKCQVH AGGRGKAGGV 70 80 90 100 110 120 KVVNSKEDIR AFAENWLGKR LVTYQTDANG QPVNQILVEA ATDIAKELYL GAVVDRSSRR 130 140 150 160 170 180 VVFMASTEGG VEIEKVAEET PHLIHKVALD PLTGPMPYQG RELAFKLGLE GKLVQQFTKI 190 200 210 220 230 240 FMGLATIFLE RDLALIEINP LVITKQGDLI CLDGKLGADG NALFRQPDLR EMRDQSQEDP 250 260 270 280 290 300 REAQAAQWEL NYVALDGNIG CMVNGAGLAM GTMDIVKLHG GEPANFLDVG GGATKERVTE 310 320 330 340 350 360 AFKIILSDDK VKAVLVNIFG GIVRCDLIAD GIIGAVAEVG VNVPVVVRLE GNNAELGAKK 370 380 LADSGLNIIA AKGLTDAAQQ VVAAVEGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of the succinyl-CoA synthetase of Escherichia coli." Buck D., Spencer M.E., Guest J.R. Biochemistry 24:6245-6252(1985) [PubMed: 3002435] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-12. Strain: K12 / EMG2.
[6]	"The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-A resolution." Wolodko W.T., Fraser M.E., James M.N.G., Bridger W.A. J. Biol. Chem. 269:10883-10890(1994) [PubMed: 8144675] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[7]	"A detailed structural description of Escherichia coli succinyl-CoA synthetase." Fraser M.E., James M.N., Bridger W.A., Wolodko W.T. J. Mol. Biol. 285:1633-1653(1999) [PubMed: 9917402] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[8]	"ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by X-ray crystallography." Joyce M.A., Fraser M.E., James M.N., Bridger W.A., Wolodko W.T. Biochemistry 39:17-25(2000) [PubMed: 10625475] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J01619 Genomic DNA. Translation: AAA23899.1.
U00096 Genomic DNA. Translation: AAC73822.1.
AP009048 Genomic DNA. Translation: BAA35394.1.

PIR

SYECSB. A24090.

RefSeq

NP_415256.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CQI	X-ray	3.30	B/E	1-385	[»]
1CQJ	X-ray	2.90	B/E	1-385	[»]
1JKJ	X-ray	2.35	B/E	1-388	[»]
1JLL	X-ray	2.69	B/E	1-388	[»]
1SCU	X-ray	2.50	B/E	1-388	[»]
2NU6	X-ray	2.55	B/E	1-388	[»]
2NU7	X-ray	2.20	B/E	1-388	[»]
2NU8	X-ray	2.15	B/E	1-388	[»]
2NU9	X-ray	2.90	B/E/G/I	1-388	[»]
2NUA	X-ray	2.95	B/E	1-388	[»]
2SCU	X-ray	2.30	B/E	1-388	[»]

ProteinModelPortal

P0A836.

SMR

P0A836. Positions 1-388.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31852N.

IntAct

P0A836. 8 interactions.

2D gel databases

SWISS-2DPAGE

P0A836.

ECO2DBASE

E039.8. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000000466; EBESCP00000000466; EBESCG00000000387.
EBESCT00000000467; EBESCP00000000467; EBESCG00000000387.
EBESCT00000016898; EBESCP00000016189; EBESCG00000015957.

GeneID

945312.

GenomeReviews

Gene locus JW0717 in contig AP009048_GR.
Gene locus b0728 in contig U00096_GR.

KEGG

ecj:JW0717.
eco:b0728.

PATRIC

32116651. VBIEscCol129921_0758.

Organism-specific databases

EchoBASE

EB0974.

EcoGene

EG10981. sucC.

Phylogenomic databases

eggNOG

COG0045.

GeneTree

EBGT00050000010497.

HOGENOM

HBG315432.

OMA

IGGDMWV.

PhylomeDB

P0A836.

ProtClustDB

PRK00696.

Enzyme and pathway databases

BioCyc

EcoCyc:SUCCCOASYN-BETA.
MetaCyc:SUCCCOASYN-BETA.

Gene expression databases

Genevestigator

P0A836.

Family and domain databases

HAMAP

MF_00558. Succ_CoA_beta.
[Tree]

InterPro

IPR011761. ATP-grasp.
IPR013650. ATP-grasp_succ-CoA_synth-type.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR005811. CoA_ligase.
IPR017866. Succ-CoA_synthase_bsu_CS.
IPR005809. Succ_CoA_synthase_bsu.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]

Gene3D

G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit.
G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit.
G3DSA:3.40.50.261. Succinyl-CoA_synth-like. 1 hit.

KO

K01903.

PANTHER

PTHR11815. CoA_lig_beta. 1 hit.

Pfam

PF08442. ATP-grasp_2. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]

PIRSF

PIRSF001554. SucCS_beta. 1 hit.

SUPFAM

SSF52210. CoA_ligase. 1 hit.

TIGRFAMs

TIGR01016. SucCoAbeta. 1 hit.

PROSITE

PS50975. ATP_GRASP. 1 hit.
PS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SUCC_ECOLI

Accession

Primary (citable) accession number: P0A836
Secondary accession number(s): P07460

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 1, 1988
Last modified:	January 25, 2012
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program