ID A0A1I0UZR4_9RHOB Unreviewed; 458 AA.
AC A0A1I0UZR4;
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-CoA carboxylase, biotin carboxylase subunit {ECO:0000313|EMBL:SFA68776.1};
GN ORFNames=SAMN05421688_0035 {ECO:0000313|EMBL:SFA68776.1};
OS Poseidonocella pacifica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Poseidonocella.
OX NCBI_TaxID=871651 {ECO:0000313|EMBL:SFA68776.1, ECO:0000313|Proteomes:UP000198796};
RN [1] {ECO:0000313|EMBL:SFA68776.1, ECO:0000313|Proteomes:UP000198796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29316 {ECO:0000313|EMBL:SFA68776.1,
RC ECO:0000313|Proteomes:UP000198796};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FOJU01000001; SFA68776.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0UZR4; -.
DR STRING; 871651.SAMN05421688_0035; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000198796; 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 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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR48095:SF2; BIOTIN CARBOXYLASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 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 PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00866; CPSASE_1; 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:UP000198796}.
FT DOMAIN 2..447
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..318
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 458 AA; 48711 MW; 5B2D11AECBBE93E7 CRC64;
MAIERLFIAN RGEIAVRIVR AAKSLGIHTI QAHSEADVEM LSVKLADEAV CIGPAPSKDS
YLNIQAILDA AKATGADAIH PGYGFLSENA GFARAVEEAG LIFVGPSADT IERMGDKVAA
RQAALAAGVP VVPGSDGRVD GVEATLAVAE QVGFPVMIKA AAGGGGRGIR IANTAGELAA
LAPQAKAEAE AAFGDGSLYV ERAIVAPRHI EVQILGDGDR AVHCFERECS LQRRRQKVWE
EAGADCLDAP TRDALCASAV ALAEAVGYRG AGTLEYLYDE STKEFFFIEM NTRIQVEHPV
TEMLTGIDLV AEMIRVCGGA PLSMTQEQIL RSGHAIEVRI CAEDPFNNFM PWPGRIKTLV
EPTGPGVRFD HFLSEGYQIP PFYDSLVGKV IVHAETRDAA IDKLTTALTE MVIDGTKHTG
PLHLALAADP EVRAGRFHTQ WLEPWLDAGA LSAKGDAA
//
