ID A0A1Q5KXJ3_9ACTN Unreviewed; 617 AA.
AC A0A1Q5KXJ3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Acetyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:OKJ86261.1};
GN ORFNames=AMK32_02875 {ECO:0000313|EMBL:OKJ86261.1};
OS Streptomyces sp. CB01883.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703943 {ECO:0000313|EMBL:OKJ86261.1, ECO:0000313|Proteomes:UP000186398};
RN [1] {ECO:0000313|EMBL:OKJ86261.1, ECO:0000313|Proteomes:UP000186398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01883 {ECO:0000313|EMBL:OKJ86261.1,
RC ECO:0000313|Proteomes:UP000186398};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKJ86261.1}.
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DR EMBL; LIWA01000001; OKJ86261.1; -; Genomic_DNA.
DR RefSeq; WP_073888184.1; NZ_LIWA01000001.1.
DR AlphaFoldDB; A0A1Q5KXJ3; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000186398; 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; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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.
DR PROSITE; PS00867; CPSASE_2; 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:UP000186398}.
FT DOMAIN 1..426
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 97..301
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 536..613
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 617 AA; 65851 MW; 16BE1CEA60722A81 CRC64;
MITSVLVANR GEIACRIFRT CAELGIRTVA VHSDADADAL HTRTADTAVR LPGAAPADTY
LRGDLVVKAA LAAGADAVHP GYGFLSENAD FARAVTDAGL TWIGPPPRAI EAMASKTRAK
ELMGLAPLAA ADVTEDDLPL LVKAAAGGGG RGMRIVRRLD ELPDALDGAR AEAASAFGDG
EVFVEPYIEH GRHVEVQILA DTHGTVRPLG TRDCSLQRRH QKVVEEAPAP GLPDALTEEL
YALAVRAARA VSYVGAGTVE FLVADGRAHF LEMNTRLQVE HPVTEAVFGL DLVAEQIRVA
EGHPLPADPP AAHGHAVEAR LYAEDPARDW APQTGTLHHL AVPAGVRLDT GYTDGDEIGV
HYDPMLAKIV AHAPTRAEAI RKLAGALERT ALHGPVTNRD LLVRSLRHDE FITARMDTGF
YDRHLAELTG SAPDPLAPLA AALADAHGRS RFGGWRNVPA QPQTKRYELA GEEIEVSYRH
TRHGLAADGV RVVHADAHTA VLEADGVRHR FEIARYGDQV YVNTTRLTAL PRFPDPTAQL
TPGSLLAPMP GTVVRIAEDL REGATVQAGQ PLIWLEAMKM QHRITAPVTG TLSALHAKAG
QQVEPGTLLA VVQETSS
//
