UniProtKB - P9WQD1 (ACSA_MYCTU)
Acetyl-coenzyme A synthetase
acsA
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. M.tuberculosis may use AcsA for both acetate and propionate assimilation.
UniRule annotation2 PublicationsMiscellaneous
Catalytic activityi
- EC:6.2.1.1UniRule annotation
Cofactori
Kineticsi
- KM=0.35 mM for CoA (at pH 8 and at 37 degrees Celsius)1 Publication
- KM=1.2 mM for acetate (at pH 8 and at 37 degrees Celsius)1 Publication
- KM=2.1 mM for propionate (at pH 8 and at 37 degrees Celsius)1 Publication
- KM=5.6 mM for ATP (at pH 8 and at 37 degrees Celsius)1 Publication
- KM=509 mM for butyrate (at pH 8 and at 37 degrees Celsius)1 Publication
pH dependencei
Temperature dependencei
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 311 | Coenzyme AUniRule annotation | 1 | |
Binding sitei | 508 | ATPUniRule annotation | 1 | |
Binding sitei | 523 | ATPUniRule annotation | 1 | |
Binding sitei | 531 | Coenzyme A; via carbonyl oxygenUniRule annotation | 1 | |
Binding sitei | 534 | ATPUniRule annotation | 1 | |
Metal bindingi | 545 | Magnesium; via carbonyl oxygenUniRule annotation | 1 | |
Metal bindingi | 547 | Magnesium; via carbonyl oxygenUniRule annotation | 1 | |
Metal bindingi | 550 | Magnesium; via carbonyl oxygenUniRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 387 – 389 | ATPUniRule annotation | 3 | |
Nucleotide bindingi | 411 – 416 | 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
SABIO-RKi | P9WQD1 |
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:Rv3667 ORF Names:MTV025.015 |
Organismi | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic identifieri | 83332 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › |
Proteomesi |
|
Organism-specific databases
TubercuListi | Rv3667 |
Subcellular locationi
Cell Wall
- cell wall Source: MTBBASE
Plasma Membrane
- plasma membrane Source: MTBBASE
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 617 | K → R: Complete loss of acetyl-coenzyme A synthetase activity. 2 Publications | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources | |||
ChainiPRO_0000208369 | 2 – 651 | Acetyl-coenzyme A synthetaseAdd BLAST | 650 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylserineCombined sources | 1 | |
Modified residuei | 617 | N6-acetyllysineUniRule annotation1 Publication | 1 |
Post-translational modificationi
Keywords - PTMi
AcetylationProteomic databases
PaxDbi | P9WQD1 |
PTM databases
iPTMneti | P9WQD1 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 190 – 193 | Coenzyme A bindingUniRule annotation | 4 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0365, Bacteria |
OMAi | DHWWHDL |
PhylomeDBi | P9WQD1 |
Family and domain databases
Gene3Di | 3.30.300.30, 1 hit 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 IPR045851, AMP-bd_C_sf IPR020845, AMP-binding_CS IPR000873, AMP-dep_Synth/Lig IPR042099, ANL_N_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.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MSESTPEVSS SYPPPAHFAE HANARAELYR EAEEDRLAFW AKQANRLSWT
60 70 80 90 100
TPFTEVLDWS GAPFAKWFVG GELNVAYNCV DRHVEAGHGD RVAIHWEGEP
110 120 130 140 150
VGDRRTLTYS DLLAEVSKAA NALTDLGLVA GDRVAIYLPL IPEAVIAMLA
160 170 180 190 200
CARLGIMHSV VFGGFTAAAL QARIVDAQAK LLITADGQFR RGKPSPLKAA
210 220 230 240 250
ADEALAAIPD CSVEHVLVVR RTGIEMAWSE GRDLWWHHVV GSASPAHTPE
260 270 280 290 300
PFDSEHPLFL LYTSGTTGKP KGIMHTSGGY LTQCCYTMRT IFDVKPDSDV
310 320 330 340 350
FWCTADIGWV TGHTYGVYGP LCNGVTEVLY EGTPDTPDRH RHFQIIEKYG
360 370 380 390 400
VTIYYTAPTL IRMFMKWGRE IPDSHDLSSL RLLGSVGEPI NPEAWRWYRD
410 420 430 440 450
VIGGGRTPLV DTWWQTETGS AMISPLPGIA AAKPGSAMTP LPGISAKIVD
460 470 480 490 500
DHGDPLPPHT EGAQHVTGYL VLDQPWPSML RGIWGDPARY WHSYWSKFSD
510 520 530 540 550
KGYYFAGDGA RIDPDGAIWV LGRIDDVMNV SGHRISTAEV ESALVAHSGV
560 570 580 590 600
AEAAVVGVTD ETTTQAICAF VVLRANYAPH DRTAEELRTE VARVISPIAR
610 620 630 640 650
PRDVHVVPEL PKTRSGKIMR RLLRDVAENR ELGDTSTLLD PTVFDAIRAA
K
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP46490.1 |
PIRi | D70789 |
RefSeqi | NP_218184.1, NC_000962.3 WP_003899631.1, NZ_NVQJ01000028.1 |
Genome annotation databases
GeneIDi | 885479 |
KEGGi | mtu:Rv3667 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP46490.1 |
PIRi | D70789 |
RefSeqi | NP_218184.1, NC_000962.3 WP_003899631.1, NZ_NVQJ01000028.1 |
3D structure databases
AlphaFoldDBi | P9WQD1 |
SMRi | P9WQD1 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv3667 |
PTM databases
iPTMneti | P9WQD1 |
Proteomic databases
PaxDbi | P9WQD1 |
Protocols and materials databases
DNASUi | 885479 |
Genome annotation databases
GeneIDi | 885479 |
KEGGi | mtu:Rv3667 |
Organism-specific databases
TubercuListi | Rv3667 |
Phylogenomic databases
eggNOGi | COG0365, Bacteria |
OMAi | DHWWHDL |
PhylomeDBi | P9WQD1 |
Enzyme and pathway databases
SABIO-RKi | P9WQD1 |
Family and domain databases
Gene3Di | 3.30.300.30, 1 hit 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 IPR045851, AMP-bd_C_sf IPR020845, AMP-binding_CS IPR000873, AMP-dep_Synth/Lig IPR042099, ANL_N_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 |
MobiDBi | Search... |
Entry informationi
Entry namei | ACSA_MYCTU | |
Accessioni | P9WQD1Primary (citable) accession number: P9WQD1 Secondary accession number(s): L0TGD8, O69635 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
Last sequence update: | April 16, 2014 | |
Last modified: | May 25, 2022 | |
This is version 41 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
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families