ID A0A1J0WPE5_9RHOB Unreviewed; 671 AA.
AC A0A1J0WPE5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Acetyl/propionyl-CoA carboxylase subuit alpha {ECO:0000313|EMBL:APE46186.1};
GN ORFNames=BOO69_21810 {ECO:0000313|EMBL:APE46186.1};
OS Sulfitobacter alexandrii.
OG Plasmid unnamed5 {ECO:0000313|EMBL:APE46186.1,
OG ECO:0000313|Proteomes:UP000181897}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=1917485 {ECO:0000313|EMBL:APE46186.1, ECO:0000313|Proteomes:UP000181897};
RN [1] {ECO:0000313|EMBL:APE46186.1, ECO:0000313|Proteomes:UP000181897}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM1-D1 {ECO:0000313|EMBL:APE46186.1,
RC ECO:0000313|Proteomes:UP000181897};
RC PLASMID=unnamed5 {ECO:0000313|EMBL:APE46186.1,
RC ECO:0000313|Proteomes:UP000181897};
RA Yang Q., Zhang X., Tian X.;
RT "Complete genome sequence of Sulfitobacter sp. AM1-D1, a toxic bacteria
RT associated with marine dinoflagellate Alexandrium minutum in East China
RT Sea.";
RL Submitted (NOV-2016) 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; CP018081; APE46186.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J0WPE5; -.
DR KEGG; suam:BOO69_21810; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000181897; Plasmid unnamed5.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 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}; Plasmid {ECO:0000313|EMBL:APE46186.1}.
FT DOMAIN 6..450
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 125..323
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 591..666
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 671 AA; 70826 MW; 164F8B5EF3D3B8AF CRC64;
MAGEMSFTRV LIANRGEIAR RIQRGCRKLG LESVAVFSDA DRDAPFVAEA DHAVCIGGAA
PSDSYLNVAA ILEAARATGA DAVHPGYGFL SENAGFAAAV EAAGLVFIGP EPDAIARMGS
KIEAKAAAEA AGVPVLPGYR GEDQSDARLL QEAEALGTPF LVKASAGGGG RGMRLVSDLG
DAPDAIASAR AEAQSAFDDP AVFLERYAPR ARHVEVQVLG DTHGTVLHLG DRDCSLQRNH
QKLIEEAPAA DLPEAVRDRM RAAAVRLAQA IGYRSAGTVE YLYDPGRGEY YFLEMNTRLQ
VEHPVTEAIT GIDLVEWQLR IARGEPLALT QGDVQFDGHA IEIRIAAENP AENFRPETGE
ISLWAPPAGV RLDTGVEAGS VVSHHYDSMI AKLIVHAPDR AGAIRQAVVA MDAFAVGGVG
LNLAYQRALL THPDFAAFRH HTSGLPEMFP GGWSEPSADP RDMALAAMAL YLHLAPAGAS
PWESLGSWRL TAPAGWPGAA SYWETTKDDP IRVNGSGSVL TAVQPDGQTI TVESAALTEC
RLSGRIDGVP FSRITYVVRA PGHWRVHLQT PAGMTATDLR TLEDQHLQRA TGGSGGADLL
SAPMPGAVAE VRVALGDRVK AGDTLVVLEA MKLLQSLPAP VAGVVTEIYC APADTVAGHA
PLIKLDPEEN T
//
