ID G7H3S8_9ACTN Unreviewed; 735 AA.
AC G7H3S8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Acyl-CoA carboxylase alpha chain {ECO:0000313|EMBL:GAB10503.1};
GN Name=accA {ECO:0000313|EMBL:GAB10503.1};
GN ORFNames=GOARA_057_00270 {ECO:0000313|EMBL:GAB10503.1};
OS Gordonia araii NBRC 100433.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1073574 {ECO:0000313|EMBL:GAB10503.1, ECO:0000313|Proteomes:UP000035088};
RN [1] {ECO:0000313|EMBL:GAB10503.1, ECO:0000313|Proteomes:UP000035088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100433 {ECO:0000313|EMBL:GAB10503.1,
RC ECO:0000313|Proteomes:UP000035088};
RA Yoshida Y., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Gordonia araii NBRC 100433.";
RL Submitted (NOV-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:GAB10503.1}.
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DR EMBL; BAEE01000057; GAB10503.1; -; Genomic_DNA.
DR RefSeq; WP_007322578.1; NZ_JABELY010000022.1.
DR AlphaFoldDB; G7H3S8; -.
DR STRING; 1073574.GOARA_057_00270; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000035088; 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}.
FT DOMAIN 14..455
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 128..324
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 651..726
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 735 AA; 76847 MW; D1B64E82D61759EB CRC64;
MTTKTKNKTA ATRAITSVLV ANRGEIACRV FRTCRDMGIA TVAVYSDPDA DAPHVRQADS
AVRLPGSTSA ETYLRGELII DAARAAGADA IHPGYGFLSE NAEFAQSVID AGLIWIGPPP
SAITAMGSKV NAKELMDAAG VPVLGDLDPA KVTADDLPLL IKASAGGGGR GMRIVRDLAD
LDENVAAAKR EAESAFGDPT VFCEPYVERG HHIEVQVMAD NHGAVWAVGE RECSIQRRHQ
KVIEEAPAPL VESLGGDLRE RLYDAARKAV AAIGYSGAGT VEFLADGNGR FYFLETNTRL
QVEHPVTEET TGLDLVEWQL RVAMGEPLTG DEPVAVGHSI EARLYAENPA AEWAPQSGTV
HRFAVDERAS AASRIRVDTG IADGSEISTF YDPMIAKVIS WAPTRRRAAA TLAAALAGAT
LHGPVTNRDM LVNTLRSEQF LSGDTDTAFI DEVGLDVLAA PLADEADARL AAIAAALADA
EWNRAGAQAL PAIPSGFRNI ASGFQEKKFG AGDDEVTVRY RFERRAGAAV SARAPGYGVV
LPDDEGVEVV AVGIASAPAS PDGGRVVAGF ATGPAFPHGG RVAAGVATGP VFPHGGRVPG
SAATRCIETL VTLNANGVTR DLIVARYGDT VFVDSPGKSV TLGVVPRYID PSTVQRPGSL
LAPMPGSVIR VAVAEGDKVT AGQPLLWLEA MKMEHTIAAP SDGIVATLAV EVGRQLAVGD
VLAIIEAESE ESDES
//
