ID A0A1H6UW80_9SPHN Unreviewed; 1069 AA.
AC A0A1H6UW80;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Acetyl/propionyl-CoA carboxylase, alpha subunit {ECO:0000313|EMBL:SEI92590.1};
GN ORFNames=SAMN05428950_101590 {ECO:0000313|EMBL:SEI92590.1};
OS Sphingomonas sp. OV641.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1881068 {ECO:0000313|EMBL:SEI92590.1, ECO:0000313|Proteomes:UP000199191};
RN [1] {ECO:0000313|Proteomes:UP000199191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV641 {ECO:0000313|Proteomes:UP000199191};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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; FNZB01000001; SEI92590.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6UW80; -.
DR STRING; 1881068.SAMN05428950_101590; -.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000199191; Unassembled WGS sequence.
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; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
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; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
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; PF01039; Carboxyl_trans; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
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; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000199191}.
FT DOMAIN 17..453
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 122..324
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 459..537
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 817..1056
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 1069 AA; 112282 MW; 0CF1A499F32F4A15 CRC64;
MRGAARLKEF DDKGRGAIES LLIANRGEIA IRIARAASAI GLRTVAVYSE DDEAAPHVAA
ADCAVALTGE GAPAYLSIEG IIAAARAEAC TAIHPGYGFL SENAGLAQAC SEAGLTFVGP
HADLLKLFGD KAAAKHHARS VGVPVLAEGK DGAGPVIVKA VAGGGGRGIR VVQDRSTLAA
QLAAAGAEAL AAFGSDAVMV ERYIPSARHI EVQLAADAHG RVLALGTRDC TLQRRHQKLI
EIAPAQALDP ALADRIQAAA VKLLDGTGYV GVATAEFLVD RDLSPDHPEA FAFLEVNPRL
QVEHTVTEEV TGLDLVALQL RLAQGKALPL AVPEPRGVAM QLRINAETIG SDGTPRGSAG
TITDLSLPGG PGIRIDGAAQ AGVAANPRFD PLLAKLIVHA PDWEGALARA RRALSEYRIM
GLGTNLPLLA RLLERPEVSD VSIDTAWFDR YVADLISPTM PAQATQDAQA IVAPLSGVVV
GIDVSVGDSI HAGMEVGTVE ALKMQHAVVA SRSGLVTAIA AVKGKVIEEG GLFLSIEPTD
DAIGEATAVQ ELDLDLVRPD LAEVHARHAL GLDEYRPDAM ARRRRTGQRS ARENLDHLFD
PDSFVEYGAL TIAAQRRRRT LDDLMRNTPA DGLVGGIGTV NAQDHGEEAA KCLGLAYDYT
VLAGTQGHNN HRKTDRLFGI AADLKLPIVF YTEGGGGRPG DVDSVGATGL DVPTFRSFAA
LSGTAPRIGI TSGYSFAGNA VLFGSCDITI ATRDAHIGVG GPAMIEGGGL GVYSPKEVGP
VEVHWQSGAV DVLAEDEADA TDLARRLLSF FQGRVSGGEV PDQRLLRHVV PENRLRVFDM
RAVIAGLFDQ GSFVELRGGY AKGMIAGLAR IDGRAIGIIA NDCKFLSGAV DAEGSDKAAR
FFQLCDAFGI PIVSLCDTPG FMVGPDAEKT APIRRGARMF IVGSALSVPV FTVVIRKAYG
LGAQAMAGGS LHAGPFTVAW PTGEFGGMGL EGAVRLGYRK ELEAITDPAQ REARYQELVA
NSYERGKAVS VAQYLEIDAV IDPADTRKWL LRGLASTPSR RSGRYVDTW
//
