(data stored in SCRATCH zone)
SWISSPROT: C0ZNF2_RHOE4
ID C0ZNF2_RHOE4 Unreviewed; 643 AA.
AC C0ZNF2;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 08-MAY-2019, entry version 59.
DE SubName: Full=Acetate--CoA ligase {ECO:0000313|EMBL:BAH31204.1};
DE EC=6.2.1.1 {ECO:0000313|EMBL:BAH31204.1};
GN Name=acs {ECO:0000313|EMBL:BAH31204.1};
GN OrderedLocusNames=RER_04960 {ECO:0000313|EMBL:BAH31204.1};
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH31204.1, ECO:0000313|Proteomes:UP000002204};
RN [1] {ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus
RT erythropolis PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAH31204.1, ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT "Sequence analysis of three plasmids harboured in Rhodococcus
RT erythropolis strain PR4.";
RL Environ. Microbiol. 8:334-346(2006).
CC -!- FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA
CC (AcCoA), an essential intermediate at the junction of anabolic and
CC catabolic pathways. AcsA undergoes a two-step reaction. In the
CC first half reaction, AcsA combines acetate with ATP to form
CC acetyl-adenylate (AcAMP) intermediate. In the second half
CC reaction, it can then transfer the acetyl group from AcAMP to the
CC sulfhydryl group of CoA, forming the product AcCoA.
CC {ECO:0000256|SAAS:SAAS00711888}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|SAAS:SAAS00711884};
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DR EMBL; AP008957; BAH31204.1; -; Genomic_DNA.
DR RefSeq; WP_020905977.1; NC_012490.1.
DR STRING; 234621.RER_04960; -.
DR EnsemblBacteria; BAH31204; BAH31204; RER_04960.
DR KEGG; rer:RER_04960; -.
DR PATRIC; fig|234621.6.peg.939; -.
DR eggNOG; ENOG4108IQF; Bacteria.
DR eggNOG; COG0365; LUCA.
DR HOGENOM; HOG000229981; -.
DR KO; K01895; -.
DR OMA; DHWWHDL; -.
DR Proteomes; UP000002204; Chromosome.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR CDD; cd05966; ACS; 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; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; AMP-dep_Synthh-like_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 4: Predicted;
DR PRODOM; C0ZNF2.
DR SWISS-2DPAGE; C0ZNF2.
KW Complete proteome {ECO:0000313|Proteomes:UP000002204};
KW Ligase {ECO:0000313|EMBL:BAH31204.1};
KW Magnesium {ECO:0000256|SAAS:SAAS00711869};
KW Metal-binding {ECO:0000256|SAAS:SAAS00711886}.
FT DOMAIN 29 80 ACAS_N. {ECO:0000259|Pfam:PF16177}.
FT DOMAIN 86 522 AMP-binding. {ECO:0000259|Pfam:PF00501}.
FT DOMAIN 531 610 AMP-binding_C. {ECO:0000259|Pfam:
FT PF13193}.
SQ SEQUENCE 643 AA; 69967 MW; 8A4D79100F54D649 CRC64;
MTSAAETDVP QAYPPSAEFA AAANAGPELQ AAADTDRLAF WANQAERLHW HEKWTDVLDW
TDAPVAKWFV GGKLNVAYNC VDRHVLAGNG DRVAIHFEGE PGDSRDLTYN DLLAEVSRAA
NTFTDLGLVA GDRVAIYMPM IPEAIVTMLA CARLGLTHSV VFAGFSATAL RSRIDDAQAK
LVVTVDGQWR RGAAAPIKTA VDESVAGADS VQNVLVVNRT GIDVEWTDGR DLWWHETVAA
ASPEHEAQAF DAEHPLFILY TSGTTGKPKG IIHTSGGYLT QASYTHHNVF DHKAGQDVYW
CTADIGWVTG HSYIVYGPLS NGVTQVVYEG TPNSPNEHRH FDIIEKYGVS IYYTAPTLVR
TFMKWGREIP DAHDLSSIRL LGSVGEPINP EAWRWFRDVI GGNKAPIVDT WWQTETGAIM
ISPLPGITAT KPGSAMAPLP GISAKIVDDD AKPLGPGGNG YLVLDEPWPA MLRGIWGDMD
RYRDTYWSRY AEEGWYFAGD GAKYDDDGAL WVLGRVDDVM NVSGHRISTS EVESALVNHH
GVAEAAVVGA ADETTGQGIV AFVILREGVE NTGEVLIAEL KAQVSTDISP IAKPRQITIV
PELPKTRSGK IMRRLLRDVA EGRDLGDTST LVDPKVFDAI RGK
//
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