ACS2_CANAL
ID ACS2_CANAL Reviewed; 671 AA.
AC Q8NJN3; A0A1D8PD92; Q59VM9;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 3.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Acetyl-coenzyme A synthetase 2;
DE EC=6.2.1.1;
DE AltName: Full=Acetate--CoA ligase 2;
DE AltName: Full=Acyl-activating enzyme 2;
GN Name=ACS2; OrderedLocusNames=CAALFM_C104290CA;
GN ORFNames=CaO19.1064, CaO19.8666;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-581.
RA Jones P.M., Clarkson J.M., Wheals A.E.;
RT "Acetyl-CoA synthetase 2 of Candida albicans.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:456215; EC=6.2.1.1;
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AOW26103.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP017623; AOW26103.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF535132; AAN01233.1; -; Genomic_DNA.
DR RefSeq; XP_019330638.1; XM_019475093.1.
DR PDB; 7KDS; X-ray; 2.90 A; A=2-671.
DR PDBsum; 7KDS; -.
DR AlphaFoldDB; Q8NJN3; -.
DR SMR; Q8NJN3; -.
DR BioGRID; 1227746; 1.
DR STRING; 237561.Q8NJN3; -.
DR PRIDE; Q8NJN3; -.
DR GeneID; 3644710; -.
DR KEGG; cal:CAALFM_C104290CA; -.
DR CGD; CAL0000197968; ACS2.
DR eggNOG; KOG1175; Eukaryota.
DR HOGENOM; CLU_000022_3_6_1; -.
DR InParanoid; Q8NJN3; -.
DR OMA; SPDIWEW; -.
DR OrthoDB; 288915at2759; -.
DR PRO; PR:Q8NJN3; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IBA:GO_Central.
DR GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR011904; Ac_CoA_lig.
DR InterPro; IPR032387; ACAS_N.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..671
FT /note="Acetyl-coenzyme A synthetase 2"
FT /id="PRO_0000208406"
FT BINDING 207..210
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 402..404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 426..431
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 517
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 532
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 540
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 543
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 603
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT CONFLICT 576..581
FT /note="VIAYVA -> ALLTLP (in Ref. 4; AAN01233)"
FT /evidence="ECO:0000305"
FT TURN 11..15
FT /evidence="ECO:0007829|PDB:7KDS"
FT HELIX 23..28
FT /evidence="ECO:0007829|PDB:7KDS"
FT HELIX 38..50
FT /evidence="ECO:0007829|PDB:7KDS"
FT HELIX 52..63
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:7KDS"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:7KDS"
FT HELIX 93..97
FT /evidence="ECO:0007829|PDB:7KDS"
FT HELIX 99..104
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:7KDS"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:7KDS"
FT HELIX 126..143
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:7KDS"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:7KDS"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 197..207
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:7KDS"
FT HELIX 215..222
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:7KDS"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:7KDS"
FT HELIX 252..256
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 272..279
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:7KDS"
FT HELIX 294..306
FT /evidence="ECO:0007829|PDB:7KDS"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:7KDS"
FT HELIX 325..330
FT /evidence="ECO:0007829|PDB:7KDS"
FT HELIX 333..337
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 349..352
FT /evidence="ECO:0007829|PDB:7KDS"
FT HELIX 356..363
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:7KDS"
FT HELIX 373..382
FT /evidence="ECO:0007829|PDB:7KDS"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 397..403
FT /evidence="ECO:0007829|PDB:7KDS"
FT HELIX 407..416
FT /evidence="ECO:0007829|PDB:7KDS"
FT TURN 419..421
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 422..428
FT /evidence="ECO:0007829|PDB:7KDS"
FT TURN 431..433
FT /evidence="ECO:0007829|PDB:7KDS"
FT TURN 442..444
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 461..464
FT /evidence="ECO:0007829|PDB:7KDS"
FT TURN 466..468
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 474..485
FT /evidence="ECO:0007829|PDB:7KDS"
FT HELIX 498..505
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 512..521
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 527..539
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 542..545
FT /evidence="ECO:0007829|PDB:7KDS"
FT HELIX 546..554
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 559..567
FT /evidence="ECO:0007829|PDB:7KDS"
FT TURN 570..572
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 573..582
FT /evidence="ECO:0007829|PDB:7KDS"
FT HELIX 591..605
FT /evidence="ECO:0007829|PDB:7KDS"
FT HELIX 608..610
FT /evidence="ECO:0007829|PDB:7KDS"
FT STRAND 615..617
FT /evidence="ECO:0007829|PDB:7KDS"
FT HELIX 631..638
FT /evidence="ECO:0007829|PDB:7KDS"
FT HELIX 655..667
FT /evidence="ECO:0007829|PDB:7KDS"
SQ SEQUENCE 671 AA; 73890 MW; D4989ED9167F197D CRC64;
MPTEQTHNVV HEANGVKLRE TPKEFFERQP NKGHIHDVNQ YKQMYEQSIK DPQGFFGPLA
KELLSWDHDF HTVKSGTLKN GDAAWFLGGE LNASYNCVDR HAFANPDKPA LICEADDEKD
SHILTYGDLL REVSKVAGVL QSWGIKKGDT VAVYLPMNAQ AIIAMLAIAR LGAAHSVIFA
GFSAGSIKDR VNDASCKALI TCDEGKRGGR TTNIKKLCDE ALVDCPTVEK VLVYKRTNNP
EIHLTEGRDY YWDVETAKFP GYLPPVSVNS EDPLFLLYTS GSTGTPKGVV HSTAGYLLGA
ALSTKYIFDI HPEDILFTAG DVGWITGHTY ALYGPLLLGV PTIIFEGTPA YPDYGRFWQI
VEKHKATHFY VAPTALRLLR KAGEQEIVKY DLSSLRTLGS VGEPISPDIW EWYNEFVGKN
QCHISDTYWQ TESGSHLIAP LAGVVPNKPG SASYPFFGID AALIDPVTGV EIEGNDAEGV
LAIKDHWPSM ARTVYKNHTK YMDTYMNPYP GYYFTGDGAA RDHDGYYWIR GRVDDVVNVS
GHRLSTAEIE AALIEDKKVS EAAVVGIHDD ITGQAVIAYV ALKEGNSDED SEGLRKELVL
QVRKTIGPFA APKSVIIVQD LPKTRSGKIM RRILRKVSSN EADQLGDIST LSNPQSVEGI
ISAFGAQFGK K
