ID H0QX74_9ACTN Unreviewed; 677 AA.
AC H0QX74;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Acyl-CoA carboxylase alpha chain {ECO:0000313|EMBL:GAB17425.1};
GN Name=accA {ECO:0000313|EMBL:GAB17425.1};
GN ORFNames=GOEFS_032_00210 {ECO:0000313|EMBL:GAB17425.1};
OS Gordonia effusa NBRC 100432.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1077974 {ECO:0000313|EMBL:GAB17425.1, ECO:0000313|Proteomes:UP000035034};
RN [1] {ECO:0000313|EMBL:GAB17425.1, ECO:0000313|Proteomes:UP000035034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100432 {ECO:0000313|EMBL:GAB17425.1,
RC ECO:0000313|Proteomes:UP000035034};
RA Yoshida I., Takarada H., Hosoyama A., Tsuchikane K., Katsumata H.,
RA Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia effusa NBRC 100432.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
CC Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC ChEBI:CHEBI:456216; EC=6.3.4.14;
CC Evidence={ECO:0000256|ARBA:ARBA00024172};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13502;
CC Evidence={ECO:0000256|ARBA:ARBA00024172};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAB17425.1}.
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DR EMBL; BAEH01000032; GAB17425.1; -; Genomic_DNA.
DR RefSeq; WP_007316763.1; NZ_BAEH01000032.1.
DR AlphaFoldDB; H0QX74; -.
DR STRING; 1077974.GOEFS_032_00210; -.
DR eggNOG; COG4770; Bacteria.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000035034; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866:SF126; BIOTIN CARBOXYLASE; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000035034}.
FT DOMAIN 14..451
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 133..324
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 590..665
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 677 AA; 71356 MW; C5D08C5114F3E275 CRC64;
MTTAIHTDGN EQTVITSVLV ANRGEIACRV FRTCEDLGIS TVAVYSDPDA DAPHVRAADA
AVRLPGSSSA QTYLRGDLVI AAALSAGADA IHPGYGFLSE NAEFAQAVVD AGLTWIGPPP
AAITAMGSKI NAKELMSAAG VPVLGDIDPE SVTASDLPLL IKASAGGGGR GMRIVRDLAD
LADQVAGAKR EAESAFGDPT IFCEPYVERG HHIEVQVMAD QHGAIWAVGE RECSIQRRHQ
KVIEEAPAPL VESLGGDLRE RLFDAARKAV AAIGYTGAGT VEFLADGKGR FYFLETNTRL
QVEHPVTEET TGLDLVEWQL RVAMGEHLDA ETPVTTGHSI EVRLYAEDPA ADWQPQSGTV
HRFEIAERSG IRVDSGITDG SEITTFYDPM LAKVIGTAPT RTRAARLLAA ALADARLHGP
VTNRDMLVNT LRSKQFLSGD TDTGFIDEIG LDVLGAPVAD DADIRLAAVA ATLSDAAKQR
TLATALADLP SGWRNLASGY STRSFLPGLV TGSPTDDAGQ IEVRYRHSRH GVELPDDATI
SVITATPSEL IAEVDGVRRT LSVSRYGASV FVDWPGKSVV LTDVPRFIDP SSVQRPGSLL
APMPGAVIRV AVAEGDQVTA GQPLLWLEAM KMEHTIAAPA DGVVATLSVV AGQQLAVGEV
LAVIVGEDTE EPAGSEN
//
