UniProtKB - P59872 (ACSA_RHOBA)
Protein
Acetyl-coenzyme A synthetase
Gene
acsA
Organism
Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1)
Status
Functioni
Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.UniRule annotation
Catalytic activityi
- EC:6.2.1.1UniRule annotation
Cofactori
Mg2+UniRule annotation
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 339 | Coenzyme AUniRule annotation | 1 | |
Binding sitei | 363 | Coenzyme AUniRule annotation | 1 | |
Binding sitei | 528 | ATPUniRule annotation | 1 | |
Binding sitei | 543 | ATPUniRule annotation | 1 | |
Binding sitei | 551 | Coenzyme A; via carbonyl oxygenUniRule annotation | 1 | |
Binding sitei | 554 | ATPUniRule annotation | 1 | |
Metal bindingi | 565 | Magnesium; via carbonyl oxygenUniRule annotation | 1 | |
Metal bindingi | 567 | Magnesium; via carbonyl oxygenUniRule annotation | 1 | |
Metal bindingi | 570 | Magnesium; via carbonyl oxygenUniRule annotation | 1 | |
Binding sitei | 611 | Coenzyme AUniRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 415 – 417 | ATPUniRule annotation | 3 | |
Nucleotide bindingi | 439 – 444 | ATPUniRule annotation | 6 |
GO - Molecular functioni
- acetate-CoA ligase activity Source: UniProtKB-UniRule
- AMP binding Source: InterPro
- ATP binding Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
GO - Biological processi
- acetyl-CoA biosynthetic process from acetate Source: InterPro
Keywordsi
Molecular function | Ligase |
Ligand | ATP-binding, Magnesium, Metal-binding, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | RBAL243090:RB13264-MONOMER |
Names & Taxonomyi
Protein namesi | Recommended name: Acetyl-coenzyme A synthetaseUniRule annotation (EC:6.2.1.1UniRule annotation)Short name: AcCoA synthetaseUniRule annotation Short name: AcsUniRule annotation Alternative name(s): Acetate--CoA ligaseUniRule annotation Acyl-activating enzymeUniRule annotation |
Gene namesi | Name:acsAUniRule annotation Synonyms:acs Ordered Locus Names:RB13264 |
Organismi | Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1) |
Taxonomic identifieri | 243090 [NCBI] |
Taxonomic lineagei | Bacteria › Planctomycetes › Planctomycetia › Planctomycetales › Planctomycetaceae › Rhodopirellula › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000208383 | 1 – 671 | Acetyl-coenzyme A synthetaseAdd BLAST | 671 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 636 | N6-acetyllysineUniRule annotation | 1 |
Post-translational modificationi
Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme.UniRule annotation
Keywords - PTMi
AcetylationFamily & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 221 – 224 | Coenzyme A bindingUniRule annotation | 4 |
Sequence similaritiesi
Belongs to the ATP-dependent AMP-binding enzyme family.UniRule annotation
Phylogenomic databases
eggNOGi | ENOG4108IQF Bacteria COG0365 LUCA |
HOGENOMi | HOG000229981 |
InParanoidi | P59872 |
KOi | K01895 |
OMAi | DHWWHDL |
OrthoDBi | 141801at2 |
Family and domain databases
Gene3Di | 3.40.50.12780, 1 hit |
HAMAPi | MF_01123 Ac_CoA_synth, 1 hit |
InterProi | View protein in InterPro IPR011904 Ac_CoA_lig IPR032387 ACAS_N IPR025110 AMP-bd_C IPR020845 AMP-binding_CS IPR000873 AMP-dep_Synth/Lig IPR042099 AMP-dep_Synthh-like_sf |
Pfami | View protein in Pfam PF16177 ACAS_N, 1 hit PF00501 AMP-binding, 1 hit PF13193 AMP-binding_C, 1 hit |
TIGRFAMsi | TIGR02188 Ac_CoA_lig_AcsA, 1 hit |
PROSITEi | View protein in PROSITE PS00455 AMP_BINDING, 1 hit |
i Sequence
Sequence statusi: Complete.
P59872-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MPTASASESS SNQPESSNAS GSIDHVLVED RLFHPSAEFT SKAVISTEEQ
60 70 80 90 100
YEKLATAARE NPDEFWRAEA LEHLHWFEPF GTVCDWQPPH AKWFVNGKTN
110 120 130 140 150
ACYNSVDAHV AAGRGDRTAI IWEGEPVEDG QPRDQRTLTY AELQTEVAKC
160 170 180 190 200
AEGLTQLGIG VGDVVSIYMP MTPELAVAML ACARIGAIHS VIFAGFSAES
210 220 230 240 250
IAERNNDASA KLVITSDGLY RRGKVLPLKA TVDEALEKSP TVEKCLVLRR
260 270 280 290 300
TGDDAPMQEG RDVWWHDVVE NQPGEMAAKP LDSETPLFIL YTSGSTGKPK
310 320 330 340 350
GILHTTAGYN LWAKRTFEWV FDHREGDVYW CTADCGWITG HSYVVYGPLS
360 370 380 390 400
AGATCLMYEG APNFPAEDRF WDIVERHKVS ILYTAPTAVR AFIKWGDEHV
410 420 430 440 450
DKHDLSSLRL LGSVGEGINP EAWMWYHKKI GGEKCPIVDT WWQTETGGIM
460 470 480 490 500
MSPLPGITPT KPGSCTRPLP GVVPSIVDEL GNSVDSEHGG KLCISQPWPG
510 520 530 540 550
MLRGIYGDEE RFVEQYWSDV PDKYLTGDNA RCDTDGYYWI MGRIDDVINV
560 570 580 590 600
SGHRLSTIEV ESALVSHPDV CEAAVVGRPH DLKGQAIAAF VTSNDRGHDD
610 620 630 640 650
EFRNELKQHV RKQIGALAQP DDIRFTAALP KTRSGKIMRR LLRDVAAGRE
660 670
LVGDTSTLED LSSLAKLREE D
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BX294156 Genomic DNA Translation: CAD78032.1 |
RefSeqi | NP_870954.1, NC_005027.1 WP_011124127.1, NC_005027.1 |
Genome annotation databases
EnsemblBacteriai | CAD78032; CAD78032; RB13264 |
GeneIDi | 1792396 |
KEGGi | rba:RB13264 |
PATRICi | fig|243090.15.peg.6426 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BX294156 Genomic DNA Translation: CAD78032.1 |
RefSeqi | NP_870954.1, NC_005027.1 WP_011124127.1, NC_005027.1 |
3D structure databases
SMRi | P59872 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 243090.RB13264 |
Genome annotation databases
EnsemblBacteriai | CAD78032; CAD78032; RB13264 |
GeneIDi | 1792396 |
KEGGi | rba:RB13264 |
PATRICi | fig|243090.15.peg.6426 |
Phylogenomic databases
eggNOGi | ENOG4108IQF Bacteria COG0365 LUCA |
HOGENOMi | HOG000229981 |
InParanoidi | P59872 |
KOi | K01895 |
OMAi | DHWWHDL |
OrthoDBi | 141801at2 |
Enzyme and pathway databases
BioCyci | RBAL243090:RB13264-MONOMER |
Family and domain databases
Gene3Di | 3.40.50.12780, 1 hit |
HAMAPi | MF_01123 Ac_CoA_synth, 1 hit |
InterProi | View protein in InterPro IPR011904 Ac_CoA_lig IPR032387 ACAS_N IPR025110 AMP-bd_C IPR020845 AMP-binding_CS IPR000873 AMP-dep_Synth/Lig IPR042099 AMP-dep_Synthh-like_sf |
Pfami | View protein in Pfam PF16177 ACAS_N, 1 hit PF00501 AMP-binding, 1 hit PF13193 AMP-binding_C, 1 hit |
TIGRFAMsi | TIGR02188 Ac_CoA_lig_AcsA, 1 hit |
PROSITEi | View protein in PROSITE PS00455 AMP_BINDING, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ACSA_RHOBA | |
Accessioni | P59872Primary (citable) accession number: P59872 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | September 26, 2003 |
Last sequence update: | September 26, 2003 | |
Last modified: | July 31, 2019 | |
This is version 91 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Complete proteome, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families