Reviewed, UniProtKB/Swiss-Prot Q27549 (ACSA_CRYPV)

Names and origin

Protein names

Recommended name:
    Acetyl-coenzyme A synthetase
    EC=6.2.1.1
Alternative name(s):
    Acetate--CoA ligase
    Acyl-activating enzyme

Gene names

Name:

ACS

Organism

Cryptosporidium parvum

Taxonomic identifier

5807 [NCBI]

Taxonomic lineage

Eukaryota › Alveolata › Apicomplexa › Coccidia › Eucoccidiorida › Eimeriorina › Cryptosporidiidae › Cryptosporidium

Protein attributes

Sequence length	694 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	AMP binding Inferred from electronic annotation. Source: InterPro ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetate-CoA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 694	694	Acetyl-coenzyme A synthetase		PRO_0000208410

Sequences

	Sequence		Length	Mass (Da)
	Q27549-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 5BA42E16E9AEE63C	FASTA	694	77,971
	10 20 30 40 50 60 MSDKRPRSPC SNNNDELNDS SVLTENMDTV ATRSKNLPFH ETYKSKPTPA DKPYRVDGID 70 80 90 100 110 120 KYKELYEQSI RDPEGFWSQM ARKELRWLRD FTKVRSSGTC LQDRLAWFLN GKLNVCDNCV 130 140 150 160 170 180 DRWAEIQPNT TALIWEGDDP SSIRHISYIE LFRNVCKMAN VLKRFGIKKG DSVGIYMPMI 190 200 210 220 230 240 PETIYTMLAC ARIGAVHMVV FAGFAAQNLL ERLVNARCKI VVTADQGSRG KKIINLKDVV 250 260 270 280 290 300 DKALEKIPEI KTCIVFRHLN GPIEFVKGRD FDGETLMRSE KPYCPLEDMD SEDPLFYLYT 310 320 330 340 350 360 SGSTGTPKGV QHSTAGYLLY AAVTQKYLFN IHPGDIFGCA GDIGWITGHS YLVYAPLCNG 370 380 390 400 410 420 ITTLIFEGVP TYPNAGRYWE MVERHRITHF YAAPTAIRTL KRLGDDFVKK HDRSSLRVLG 430 440 450 460 470 480 SVGEPINPSA WRWYHSVVGE ERCSIVDTYW QTETGGIVIA PIPGCFDTKP GSATFPFFGI 490 500 510 520 530 540 EPAILDPDTG KEIDGPGSGV LCIKNSWPGM FRGIFGAHYL HEIYTKPFPK YYFTGDGVLR 550 560 570 580 590 600 DQDGYLWITG RIDDTINVSG HRLSSKEIED ALTNHFGIAE AAAVAIDHDV KGNALVCFVV 610 620 630 640 650 660 LKDSGNRTFD LNNSSPHPFE YELRMCVRTQ IGPVATPDHI IVVENIPKTR SGKVVRRLLR 670 680 690 KIATGCNDYG DISTVANPEC IKSIESSWAQ YLKR

References

[1]

"The putative acetyl-CoA synthetase gene of Cryptosporidium parvum and a new conserved protein motif in acetyl-CoA synthetases." Khramtsov N.V., Blunt D.S., Montelone B.A., Upton S.J. J. Parasitol. 82:423-427(1996) [PubMed: 8636846] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: KSU-1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U24082 Genomic DNA. Translation: AAC47128.1.
3D structure databases
HSSP	HSSP built from PDB template 1PG4 based on UniProtKB Q8ZKF6.
ModBase	Search...
Enzyme and pathway databases
BRENDA	6.2.1.1. 284.
Family and domain databases
InterPro	IPR011904. Ac_CoA_lig_AcsA. IPR000873. AMP-dep_Synth/Lig. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
TIGRFAMs	TIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACSA_CRYPV

Accession

Primary (citable) accession number: Q27549

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)