ID A0A0N1LPP0_9SPHN Unreviewed; 444 AA.
AC A0A0N1LPP0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Acetyl-CoA carboxylase biotin carboxylase subunit {ECO:0000313|EMBL:KPF90003.1};
DE EC=6.4.1.2 {ECO:0000313|EMBL:KPF90003.1};
GN ORFNames=IP83_00385 {ECO:0000313|EMBL:KPF90003.1};
OS Novosphingobium sp. AAP93.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1523427 {ECO:0000313|EMBL:KPF90003.1, ECO:0000313|Proteomes:UP000037906};
RN [1] {ECO:0000313|EMBL:KPF90003.1, ECO:0000313|Proteomes:UP000037906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP93 {ECO:0000313|EMBL:KPF90003.1,
RC ECO:0000313|Proteomes:UP000037906};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPF90003.1}.
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DR EMBL; LJHZ01000002; KPF90003.1; -; Genomic_DNA.
DR RefSeq; WP_054120223.1; NZ_LJHZ01000002.1.
DR AlphaFoldDB; A0A0N1LPP0; -.
DR STRING; 1523427.IP83_00385; -.
DR PATRIC; fig|1523427.4.peg.1547; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000037906; Unassembled WGS sequence.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KPF90003.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 1..444
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..315
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 444 AA; 46364 MW; 991F88839CF5C312 CRC64;
MIRRLFIANR GEIALRVIRT AKAMGITTVL GVSSADAASL PALMADETVL LGPGPSSQSY
LAIDKVVAAM VAAKCDAVHP GYGFLSENAA FAKAVAEAGI RFVGPDIKTL EGMGDKLAAR
ALALEAGLPV LPGGEAATRE AIHARAAETG YPLLLKAVAG GGGKGMRRVD RAEDLDSALD
MAQAEAQAAF GNNAVYVERF VAKGRHVEVQ LLGDGTHAIH LGTRDCSIQR RFQKLVEEAP
APAMPEEARA GIENAAVRLA QHIGYRGAGT AEFLVDATDF SFYFLELNAR IQVEHPVTEA
ITGVDLVEQQ LLVASGKALK LAQAMVRPVG HAIEVRINAE DPEADFRPAP GRIARAAWPA
GPGIRVDTHI AAGGEVPPFY DSLLGKLIVH GATREEAVAR LQAALARIAI EGVPTTAGLH
ARIAADPRFA AGGVDTGFLT GLAS
//
