ID A0A1V0GYP7_9RHOB Unreviewed; 650 AA.
AC A0A1V0GYP7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:ARC38994.1};
GN ORFNames=A6J80_22130 {ECO:0000313|EMBL:ARC38994.1};
OS Paracoccus yeei.
OG Plasmid unnamed5 {ECO:0000313|EMBL:ARC38994.1,
OG ECO:0000313|Proteomes:UP000191257}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=147645 {ECO:0000313|EMBL:ARC38994.1, ECO:0000313|Proteomes:UP000191257};
RN [1] {ECO:0000313|Proteomes:UP000191257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_252 {ECO:0000313|Proteomes:UP000191257};
RC PLASMID=Plasmid unnamed5 {ECO:0000313|Proteomes:UP000191257};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA Sadzewicz L., Sengamalay N., Ott S., Godinez A., Nagaraj S., Nadendla S.,
RA Geyer C., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (MAR-2017) 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; CP020445; ARC38994.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V0GYP7; -.
DR KEGG; pye:A6J80_22130; -.
DR eggNOG; COG4770; Bacteria.
DR Proteomes; UP000191257; 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:ARC38994.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000191257}.
FT DOMAIN 1..449
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..322
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 569..646
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 650 AA; 68356 MW; 3FF7F052444F322A CRC64;
MFTKILIANR GEIACRVIDT ARRMGIATVA VYSDADADAR HRDLADEAVH IGPASAADSY
LRGDRIIAAA LETGAQAIHP GYGFLSENPG FVQAVQDAGL VFIGPSAASI RAMGLKDAAK
ALMEAAGVPV VPGYHGENQD AAFLAEQAAR IGYPVLIKAR AGGGGKGMRR VADPADFAAA
LEGAQREGQS SFGDPAVLIE KYITTPRHIE VQVFGDSHGT IVHLYERDCS LQRRHQKVIE
EAPAPDMPPE VRTAMTQAAV QAARAVDYRN AGTVEFIADG SGPLRADGFW FMEMNTRLQV
EHPVTEAITG LDLVEWQLRV AAGEPLPLTQ DRIGLTGHAF EARIYAEDPA RDFLPAPGPL
VHVAFPEGAR IDTGVRGGDR ISPHYDPMIA KLTTHAATRQ QALSALHRAL GQTHIAGTAT
NLGFLQALCR DPDFAAGRMD TGLIGRKQKA LTHVPDPDDA AFLFAALAAL DLDPAAPQAG
FRLWGPASLQ VDLAHGKERI ARDLHLLGPG HVAVGDSAFT AVALGADGTA RARRNGRNLT
ARVARRGDAV SVLLDGRITD FARIDPLAVE RAGGAGDGRI AAPMTGLVRA VPAMAGARVA
PGDILVVIEA MKMEHSLRAA GAGTVQAIHC AVGDTVADGA LLVELEPADA
//
