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Database: UniProt
Entry: A0A0G3UP11_9ACTN
LinkDB: A0A0G3UP11_9ACTN
Original site: A0A0G3UP11_9ACTN 
ID   A0A0G3UP11_9ACTN        Unreviewed;       648 AA.
AC   A0A0G3UP11;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Acetyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:AKL66645.1};
GN   ORFNames=M444_15950 {ECO:0000313|EMBL:AKL66645.1};
OS   Streptomyces sp. Mg1.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=465541 {ECO:0000313|EMBL:AKL66645.1, ECO:0000313|Proteomes:UP000035653};
RN   [1] {ECO:0000313|EMBL:AKL66645.1, ECO:0000313|Proteomes:UP000035653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mg1 {ECO:0000313|EMBL:AKL66645.1,
RC   ECO:0000313|Proteomes:UP000035653};
RX   PubMed=23908282;
RA   Hoefler B.C., Konganti K., Straight P.D.;
RT   "De Novo Assembly of the Streptomyces sp. Strain Mg1 Genome Using PacBio
RT   Single-Molecule Sequencing.";
RL   Genome Announc. 1:e00535-13(2013).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; CP011664; AKL66645.1; -; Genomic_DNA.
DR   RefSeq; WP_037797794.1; NZ_CP011664.1.
DR   AlphaFoldDB; A0A0G3UP11; -.
DR   KEGG; strm:M444_15950; -.
DR   PATRIC; fig|465541.12.peg.3440; -.
DR   OrthoDB; 9760256at2; -.
DR   Proteomes; UP000035653; 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; 3.30.470.20; 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 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000035653}.
FT   DOMAIN          3..435
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          99..310
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          566..643
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   COILED          160..187
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   648 AA;  68282 MW;  752E579F454FD777 CRC64;
     MTNLTSLLVA NRGEIAVRIF RTARALGLAT VAVHSDPDAD ALHVRDADAA VRLPGAAPAD
     TYLRGDLIIA AALAAGADAV HPGYGFLSEN AGFARAVEDA GLAWIGPPPE AIEAMASKTR
     AKELVRAAGV PLLDPVDPAT ATAADLPLLL KAAAGGGGRG MRVVRDLDAL KEELEAASAE
     ARSAFGDGEV FAEPYVERGR HVEVQILADA HGTVWALGTR DCSLQRRHQK VIEEAPAPCL
     PDALRESLHQ AATAAARAVS YRGAGTVEFL VTADGRPYFL EMNTRLQVEH PVTEAVFGLD
     LVALQLRVAE GAALPPAPPE PGGHAVEARL YAEDPARDWR PQTGVLRTLA VPGRVRVDTG
     FADGDTVGIH YDPMLAKVIA HAPTRAEAVR ALARALAEAR IHGLTTNREL LVRSLRHPEF
     AAARLDTGFY DRHLAALTED TPDTARALAL AALAAALAAA APAPDAPLAT RLGGWRNVPS
     QPQTRSYRSG ETTYEIRYHP ARSGPPVPVD QPGVRVLATG PALVTLEVDG IRRMFHVKHE
     SNSPEVHVDS ALGAHTLTRL PRFADPQDRT APGSLLAPMP GTVVRVAEGL APGSPVTAGQ
     PLLWLEAMKM EHRIVSPASG TLTALHAATG RQVEFGALLA VVQEETPA
//
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