ID A0A0T5P6T3_9RHOB Unreviewed; 673 AA.
AC A0A0T5P6T3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Acetyl-/propionyl-coenzyme A carboxylase alpha chain {ECO:0000313|EMBL:QEW29602.1};
DE SubName: Full=Acetyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:KRS16946.1};
GN Name=accA1_4 {ECO:0000313|EMBL:QEW29602.1};
GN ORFNames=RIdsm_05448 {ECO:0000313|EMBL:QEW29602.1}, XM52_15330
GN {ECO:0000313|EMBL:KRS16946.1};
OS Roseovarius indicus.
OG Plasmid pRIdsm_01 {ECO:0000313|EMBL:QEW29602.1}, and
OG Plasmid pridsm_01 {ECO:0000313|Proteomes:UP000325785}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=540747 {ECO:0000313|EMBL:KRS16946.1, ECO:0000313|Proteomes:UP000051401};
RN [1] {ECO:0000313|EMBL:KRS16946.1, ECO:0000313|Proteomes:UP000051401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B108 {ECO:0000313|EMBL:KRS16946.1,
RC ECO:0000313|Proteomes:UP000051401};
RA Li G., Lai Q., Shao Z., Yan P.;
RT "The draft genome sequence of Roseovarius indicus B108T.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QEW29602.1, ECO:0000313|Proteomes:UP000325785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26383 {ECO:0000313|EMBL:QEW29602.1,
RC ECO:0000313|Proteomes:UP000325785};
RC PLASMID=pridsm_01 {ECO:0000313|Proteomes:UP000325785}, and pRIdsm_01
RC {ECO:0000313|EMBL:QEW29602.1};
RA Vollmers J., Petersen J.;
RT "Genetic Globetrotter - A new plasmid hitch-hiking vast phylogenetic and
RT geographic distances.";
RL Submitted (AUG-2018) 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; LAXI01000010; KRS16946.1; -; Genomic_DNA.
DR EMBL; CP031599; QEW29602.1; -; Genomic_DNA.
DR RefSeq; WP_057817043.1; NZ_LAXI01000010.1.
DR AlphaFoldDB; A0A0T5P6T3; -.
DR STRING; 540747.SAMN04488031_110134; -.
DR KEGG; rid:RIdsm_05448; -.
DR PATRIC; fig|540747.5.peg.764; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000051401; Unassembled WGS sequence.
DR Proteomes; UP000325785; Plasmid pridsm_01.
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:QEW29602.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051401}.
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..668
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 673 AA; 70958 MW; 91FCF17484F9569D CRC64;
MAGEMSFTRV LIANRGEIAQ RIHRGCRKLG LESVAVFSDA DRDAPFVAEA DHAVCIGGAA
PSDSYLNVEA ILEAARATGA GAVHPGYGFL SENAGFAAAV EAAGLVFIGP EPDAIARMGS
KIEAKAAAEA AGVPVLPGYR GEDQSAARLL EEARALGTPF LVKASAGGGG RGMRLVTDLG
EAPEAIASAR AEAQGAFGDP AVFLERYAPR ARHVEVQVLG DTHGTVLHLG DRDCSLQRNH
QKLIEEAPAA DLPETVRDDM RAAAVRLAQA IGYRSAGTVE YLYDPARGEY YFLEMNTRLQ
VEHPVTEAIT GIDLVEWQLR IARGEPLTLA QSDVQFDGHA IEIRIAAESP AEDFRPETGQ
ITLWAPPAGV RLDTGVEAGS VVSHHYDSMI AKLIVHAPDR AGAIRQAVAA MDAFAVGGVG
LNLAYQRALL LHPDFQTFRH HTSGLPEMFP DGWTHPTPDP RDMALAAIAL HLHLAPAAAG
ASPWESLGSW RLTAPAGRPG AASYWDTTND DPIRVTGSGT IFAAVPPGGQ TVTVETAALT
GDRLSGRIDG VPFARIAHVE RARDHWRVHL QTSAGMTAAD LRTLEDQHLQ RATGGSDGAD
LLSAPMPGAV AEVRVAPGDR VEAGDTLVVL EAMKLLQSLP APVAGVVTEI YCAPGDTVAG
HVPLIKLDPE ENT
//
