ID A0A159Z9L7_9RHOB Unreviewed; 668 AA.
AC A0A159Z9L7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Putative biotin carboxylase subunit of propionyl-CoA carboxylase {ECO:0000313|EMBL:AMY71548.1};
GN ORFNames=AKL17_4336 {ECO:0000313|EMBL:AMY71548.1};
OS Frigidibacter mobilis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Frigidibacter.
OX NCBI_TaxID=1335048 {ECO:0000313|EMBL:AMY71548.1, ECO:0000313|Proteomes:UP000076128};
RN [1] {ECO:0000313|EMBL:AMY71548.1, ECO:0000313|Proteomes:UP000076128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cai42 {ECO:0000313|Proteomes:UP000076128};
RA Geng S., Pan X., Wu X.;
RT "Complete genome sequence of Defluviimonas alba cai42t isolated from an
RT oilfield in Xinjiang.";
RL Submitted (SEP-2015) 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; CP012661; AMY71548.1; -; Genomic_DNA.
DR RefSeq; WP_066817116.1; NZ_CP012661.1.
DR AlphaFoldDB; A0A159Z9L7; -.
DR STRING; 1335048.AKL17_4336; -.
DR KEGG; daa:AKL17_4336; -.
DR PATRIC; fig|1335048.3.peg.4501; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000076128; Chromosome.
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; 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; 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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 2..444
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 588..664
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 668 AA; 71262 MW; A184B0A19D6B6471 CRC64;
MKIKTLLIAN RGEIACRIAR TARAKGITPV GIHSQADANA LHVREIGKSV CIGAGPASES
YLKIDAVIVA AQSVGADAIH PGYGFLAENP DFARAVEAAG MIFMGPTPAT LERFGDKASA
KEAAVAASVP VISGAEGARS DPRQIADEVR QMGLPVLLKA VGGGGGRGQR LVTDETTLVE
DIEGALREAK STFGSEGLLL ERFLPDARHV EVQIAGDGKG HVVHLFERDC TLQRRHQKVI
EEAPAWGLPR TLLEDIARDA VRLGETLDYR GLGTVEFLVA GDEYFFLEVN PRIQVEHPVT
EAITGLDLVA LHLRIAEGAG LGLVQDDLKI NGHAVEARLY AEDPAMQFAP STGTLTTLSL
PSGLRIDSGV EEGDAVTPYY DPMIAKLIVH APDRETALAR LATALDHVAV EGVETNRAFL
TALARNPEFE RMQVHTRWID GRLAELTQAS PLVRPDLWKA AAAILFVTQS RSDINANPWT
NRDAFTGWRL GLGGDATEAG QRVTLTDSNE VSEELRVGPV KPGARYTVYS ENGEALTLSA
REITPGRWRL SEGDTVHLIE ARLHAGVIEL DTPEGRLVFR PAAPLAFAGG DAVADRAVTS
PLTGMIVEIK VSDGQTVAEG DVVAVMESMK LEISIRAAAA GIASNISVSN GDMVDRGQVI
AEILPSEE
//
