SCOA_HELPY
ID SCOA_HELPY Reviewed; 232 AA.
AC P56006;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Succinyl-CoA:3-ketoacid coenzyme A transferase subunit A;
DE EC=2.8.3.5;
DE AltName: Full=Succinyl-CoA:3-oxoacid CoA-transferase;
DE Short=OXCT A;
GN Name=scoA; OrderedLocusNames=HP_0691;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC STRAIN=69A;
RX PubMed=9325289; DOI=10.1074/jbc.272.41.25659;
RA Corthesy-Theulaz I.E., Bergonzelli G.E., Henry H., Bachmann D.,
RA Schorderet D.F., Blum A.L., Ornston L.N.;
RT "Cloning and characterization of Helicobacter pylori succinyl
RT CoA:acetoacetate CoA-transferase, a novel prokaryotic member of the CoA-
RT transferase family.";
RL J. Biol. Chem. 272:25659-25667(1997).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-oxo acid + succinyl-CoA = a 3-oxoacyl-CoA + succinate;
CC Xref=Rhea:RHEA:24564, ChEBI:CHEBI:30031, ChEBI:CHEBI:35973,
CC ChEBI:CHEBI:57292, ChEBI:CHEBI:90726; EC=2.8.3.5;
CC Evidence={ECO:0000269|PubMed:9325289};
CC -!- SUBUNIT: Heterodimer of a subunit A and a subunit B.
CC -!- INTERACTION:
CC P56006; P56007: scoB; NbExp=3; IntAct=EBI-7723842, EBI-7724043;
CC -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase subunit A family.
CC {ECO:0000305}.
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DR EMBL; AE000511; AAD07743.1; -; Genomic_DNA.
DR PIR; C64606; C64606.
DR RefSeq; NP_207485.1; NC_000915.1.
DR RefSeq; WP_001045154.1; NC_018939.1.
DR PDB; 3RRL; X-ray; 2.29 A; A/C=1-232.
DR PDBsum; 3RRL; -.
DR AlphaFoldDB; P56006; -.
DR SMR; P56006; -.
DR DIP; DIP-3481N; -.
DR IntAct; P56006; 2.
DR MINT; P56006; -.
DR STRING; 85962.C694_03560; -.
DR PaxDb; P56006; -.
DR EnsemblBacteria; AAD07743; AAD07743; HP_0691.
DR KEGG; hpy:HP_0691; -.
DR PATRIC; fig|85962.47.peg.739; -.
DR eggNOG; COG1788; Bacteria.
DR OMA; FVKAWKG; -.
DR PhylomeDB; P56006; -.
DR BioCyc; MetaCyc:HP_RS03380-MON; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0008260; F:3-oxoacid CoA-transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008775; F:acetate CoA-transferase activity; IBA:GO_Central.
DR GO; GO:0008410; F:CoA-transferase activity; IBA:GO_Central.
DR InterPro; IPR012792; 3-oxoacid_CoA-transf_A.
DR InterPro; IPR004165; CoA_trans_fam_I.
DR InterPro; IPR004163; CoA_transf_BS.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR PANTHER; PTHR13707; PTHR13707; 1.
DR Pfam; PF01144; CoA_trans; 1.
DR SMART; SM00882; CoA_trans; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR02429; pcaI_scoA_fam; 1.
DR PROSITE; PS01273; COA_TRANSF_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Transferase.
FT CHAIN 1..232
FT /note="Succinyl-CoA:3-ketoacid coenzyme A transferase
FT subunit A"
FT /id="PRO_0000157909"
FT BINDING 24..30
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255"
FT CONFLICT 14
FT /note="A -> T (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 108..109
FT /note="HA -> RP (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 116..121
FT /note="AYYTPT -> LTTPQP (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 129..139
FT /note="QGKESREFNGK -> PRQGIQGSLTAR (in Ref. 2; no
FT nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="T -> A (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:3RRL"
FT HELIX 9..12
FT /evidence="ECO:0007829|PDB:3RRL"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:3RRL"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:3RRL"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:3RRL"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:3RRL"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:3RRL"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:3RRL"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:3RRL"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:3RRL"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:3RRL"
FT HELIX 100..112
FT /evidence="ECO:0007829|PDB:3RRL"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:3RRL"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:3RRL"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:3RRL"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:3RRL"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:3RRL"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:3RRL"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:3RRL"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:3RRL"
FT HELIX 175..180
FT /evidence="ECO:0007829|PDB:3RRL"
FT STRAND 182..193
FT /evidence="ECO:0007829|PDB:3RRL"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:3RRL"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:3RRL"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:3RRL"
SQ SEQUENCE 232 AA; 25362 MW; 83CFEE57C0192F3D CRC64;
MNKVITDLDK ALSALKDGDT ILVGGFGLCG IPEYAIDYIY KKGIKDLIVV SNNCGVDDFG
LGILLEKKQI KKIIASYVGE NKIFESQMLN GEIEVVLTPQ GTLAENLHAG GAGIPAYYTP
TGVGTLIAQG KESREFNGKE YILERAITGD YGLIKAYKSD TLGNLVFRKT ARNFNPLCAM
AAKICVAEVE EIVPAGELDP DEIHLPGIYV QHIYKGEKFE KRIEKITTRS TK
