ID Q9K3W3_STRCO Unreviewed; 614 AA.
AC Q9K3W3;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 24-JAN-2024, entry version 133.
DE SubName: Full=Acetyl/propionyl CoA carboxylase, alpha subunit {ECO:0000313|EMBL:CAB95892.1};
GN OrderedLocusNames=SCO4381 {ECO:0000313|EMBL:CAB95892.1};
GN ORFNames=SCD10.13 {ECO:0000313|EMBL:CAB95892.1};
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226 {ECO:0000313|EMBL:CAB95892.1, ECO:0000313|Proteomes:UP000001973};
RN [1] {ECO:0000313|EMBL:CAB95892.1, ECO:0000313|Proteomes:UP000001973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145
RC {ECO:0000313|Proteomes:UP000001973};
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.H.,
RA Kieser T., Larke L., Murphy L., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; AL939119; CAB95892.1; -; Genomic_DNA.
DR RefSeq; NP_628550.1; NC_003888.3.
DR RefSeq; WP_011029618.1; NZ_VNID01000017.1.
DR AlphaFoldDB; Q9K3W3; -.
DR STRING; 100226.gene:17762026; -.
DR PaxDb; 100226-SCO4381; -.
DR PATRIC; fig|100226.15.peg.4449; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_3_11; -.
DR InParanoid; Q9K3W3; -.
DR OMA; MYYDSMI; -.
DR OrthoDB; 9760256at2; -.
DR PhylomeDB; Q9K3W3; -.
DR Proteomes; UP000001973; 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 CARBOXYL CARRIER PROTEIN; 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:UP000001973}.
FT DOMAIN 1..424
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 97..299
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 535..612
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 614 AA; 65184 MW; 1BB4E78F69533D33 CRC64;
MITSVLVANR GEIACRVFST CRESGIRTVA VHSDADANAL HARVADAAVR LPGAAPADTY
LRGDLIVKAA VAAGADAVHP GYGFLSENAD FARAVRDAGL VWIGPPPEAI EAMASKTRAK
ELMGIAPLTD VTEADLPVLV KAAAGGGGRG MRVVRRLADL DAELTAARAE AASAFGDGEV
FVEPYVVDGR HVEVQILADT HGTVWVLGTR DCSLQRRHQK VIEEAPAPGL TPGLTAELHD
LAVRAARAVD YVGAGTVEFL VADGTAHFLE MNTRLQVEHP VTEAVFGIDL VALQLRIAEG
HALDDDPPRA RGHAVEARLY AEDPANGWAP QTGRLHRLAV PDGIRLDTGY TGGDDIGVHY
DPMLAKAVAH APTRAEAVRR LAGALERAAI HGPVTNRDLL VRSLRHEEFT SGRMDTGFYD
RHLAALTEPA PDPLAPLAAA LADASTRAGR FGGWRNLPSQ PQVKRYAVAG EEHEVRYGHT
RTGLTAEGVR VVHAGPDRVV LEADGVQRPF DIARYGDHVH VNTTRLTALP RFPDPTTQHA
PGSLLAPMPG TVVRVAEGLT EGTTVQAGQP LLWLEAMKME HRITAPVTGR LTALPAGLGR
QVEMGALLAV VESD
//