Q9CMW1

PR
Gene name
acsA
Protein name
Acetyl-coenzyme A synthetase
Names
AcCoA synthetase, Acs, Acetate--CoA ligase, Acyl-activating enzyme
Species
Pasteurella multocida (strain Pm70)
KEGG Pathway
pmu:PM0692
EC number
6.2.1.1: Acid--thiol ligases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-46 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q9CMW1

Entry ID Method Resolution Chain Position Source
AF-Q9CMW1-F1 Predicted AlphaFoldDB

No variants for Q9CMW1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9CMW1

No associated diseases with Q9CMW1

5 regional properties for Q9CMW1

Type Name Position InterPro Accession
domain AMP-dependent synthetase/ligase domain 93 - 527 IPR000873
conserved_site Peptidase S26A, signal peptidase I, conserved site 500 - 513 IPR019758
conserved_site AMP-binding, conserved site 264 - 275 IPR020845
domain AMP-binding enzyme, C-terminal domain 536 - 617 IPR025110
domain Acetyl-coenzyme A synthetase, N-terminal domain 31 - 86 IPR032387

Functions

Description
EC Number 6.2.1.1 Acid--thiol ligases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.

5 GO annotations of molecular function

Name Definition
acetate-CoA ligase activity Catalysis of the reaction: ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.
AMP binding Binding to AMP, adenosine monophosphate.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
metal ion binding Binding to a metal ion.
serine-type endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).

1 GO annotations of biological process

Name Definition
acetyl-CoA biosynthetic process from acetate The chemical reactions and pathways resulting in the formation of acetyl-CoA from acetate, either directly or via acetylphosphate.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPHNSMLKEN RLFKPTDEFR RQANISGLET YQALWEFADK DYLTYWSDLA RELITWKKPF
70 80 90 100 110 120
MHIFDDSEAP FYKWFSDGTL NVSYNCLDRH LPDKADKTAL IFESDFGQVQ LYTYAKLHNR
130 140 150 160 170 180
VCRFANALRE LGIKKGDRVI IYLPMLVEAV IAMQACARIG AVHSVVFGGF SASALRDRIE
190 200 210 220 230 240
DAEAKLVITA NAGLRGGKII PLKETVDEAL EMGCKTIENV IVFHRVNIDT PWKKGRDLWW
250 260 270 280 290 300
NELTANQPAF CEPEWMNAED PLFILYTSGS TGKPKGIVHS TGGYLLGALN SFRNVFDNKP
310 320 330 340 350 360
NDIFWCTADV GWITGHSYVC YGPLANGATQ VIFEGVPTYP DPGRIWRMIQ RHKINVFYTS
370 380 390 400 410 420
PTLIRSLTRL GDHIPNKYDL SSLRLLGSVG EPINPSAWMW FYEVVGKSRC PIVDTWWQTE
430 440 450 460 470 480
TGSIMLAPIP GVTATKPGSC TLPLPGIMAE VLDENGQKCA VEQGGALAIK RPFPSMLRTI
490 500 510 520 530 540
WNDPERYKST YFPAEYGGKY YIAGDNAHRD KDGYFWILGR TDDVLNVSGH RLGTMEIESA
550 560 570 580 590 600
LVASPKVAEA AVVGKPDEIK GEAIVAFVVL NDFRPEGEEA RQLAEELKAW VSNEIGKIAR
610 620 630 640 650
PEDIRFADNL PKTRSGKIMR RLLRSIAKNE MITQDISTLE NPQIIGQLQQ QWL