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
//