(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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