ID A0A0F7N6J6_9ACTN Unreviewed; 700 AA.
AC A0A0F7N6J6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Acetyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:AKH83018.1};
GN ORFNames=AA958_13140 {ECO:0000313|EMBL:AKH83018.1};
OS Streptomyces sp. CNQ-509.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=444103 {ECO:0000313|EMBL:AKH83018.1, ECO:0000313|Proteomes:UP000034283};
RN [1] {ECO:0000313|EMBL:AKH83018.1, ECO:0000313|Proteomes:UP000034283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNQ-509 {ECO:0000313|EMBL:AKH83018.1,
RC ECO:0000313|Proteomes:UP000034283};
RA Ruckert C., Albersmeier A., Leipoldt F., Winkler A., Zeyhle P.,
RA Kalinowski J., Heide L., Kaysser L.;
RT "Complete Genome Sequence of Streptomyces sp. CNQ-509, a Prolific Producer
RT of Meroterpenoid Chemistry.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CP011492; AKH83018.1; -; Genomic_DNA.
DR RefSeq; WP_047016350.1; NZ_CP011492.1.
DR AlphaFoldDB; A0A0F7N6J6; -.
DR STRING; 444103.AA958_13140; -.
DR KEGG; strc:AA958_13140; -.
DR PATRIC; fig|444103.5.peg.2765; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000034283; Chromosome.
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:UP000034283}.
FT DOMAIN 1..459
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 101..306
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 597..680
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 346..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 700 AA; 72188 MW; F73464018DCFE72C CRC64;
MIRTLLVANR GEIACRVFRT CAELGITPVA VHSDADAGAL HVRAALDAGG SAVRLPGRAA
SDTYLRADLL VAAALAAGAD AVHPGYGFLS ESAEFARAVT AAGLTWVGPP PEAIEAMASK
TRAKELMGLA PFDPSKAVES DLPLLVKAAA GGGGRGMRVV RELAALDAGL ASASAEAAAA
FGDGEVFVEP YVEGGRHVEV QVLADAHGAV WALGTRDCSL QRRHQKVVEE APAPGLAPGA
AAELAETAVR AARAIGYVGA GTVEFLLAPD GRAQFLEMNT RLQVEHPVTE AVHGVDLVAA
QVRIAEGAHL PPSAPQPRGH AVEARLYAED PASDFAPQTG RVHRLEVGGA AGGPGRSPEG
NRGGAPVPGR GGIGEPPTLR LDTGYTAGDT VTPYYDALLA KVIVHAPTRA EAVRHLTAAL
RRARIHGPVT NRDLLVRSLE HEEFTGGRMT TSFYDAHLPA LTRPADEAGE PDAHLRLAAL
AAALADAAAR QQAGDAALPA RFGGWRNVPS QPQAKGYRAE PGGAEVEVRY RLTRDGIRAD
GLPDVRVLAA APGRVVLEVA GVARAFDVAV YDAPAGGRPA PATYVDTPHG SYALSPLSRF
PDPRADTPPG SLLAPMPGTV VRLADGIAPG QTVRQGQPLL WLEAMKMEHK VAAPASGVLT
ALHAVPGGQV EVGALLAVVE AAEDAAAHAA LSRDQEGRQP
//
