ID A0A0F2J5A2_9BACT Unreviewed; 408 AA.
AC A0A0F2J5A2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Carbamoyl-phosphate synthase L chain ATP-binding {ECO:0000313|EMBL:KJR42565.1};
GN ORFNames=MCHI_001537 {ECO:0000313|EMBL:KJR42565.1};
OS Candidatus Magnetoovum chiemensis.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Magnetoovum.
OX NCBI_TaxID=1609970 {ECO:0000313|EMBL:KJR42565.1, ECO:0000313|Proteomes:UP000033718};
RN [1] {ECO:0000313|EMBL:KJR42565.1, ECO:0000313|Proteomes:UP000033718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS-04 {ECO:0000313|EMBL:KJR42565.1,
RC ECO:0000313|Proteomes:UP000033718};
RA Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.;
RT "Single-cell genomics of uncultivated deep-branching MTB reveals a
RT conserved set of magnetosome genes.";
RL Submitted (FEB-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:KJR42565.1}.
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DR EMBL; JZJI01000407; KJR42565.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2J5A2; -.
DR Proteomes; UP000033718; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 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; 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; 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; 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; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW ECO:0000313|EMBL:KJR42565.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000033718}.
FT DOMAIN 1..200
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 1..71
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 408 AA; 46478 MW; 6F51DD95A86BE0B4 CRC64;
MDRELRAKIG GFACSIAKEA NYKNAGTCEF IMDQDKNFYF LEMNTRLQVE HPITELVTSL
DLVELQLRIA SGEPLNLTQE EIQFKGSAIE ARICAENPYK GFLPTTGIVT RYAMPRGKNI
RVDSGICAGS MVTIHFDSLL AKVAVWGETR NEAIQTMGRA LNGYHIEGVT TNLDFANAII
NHPSFANAEL STDFINEHFI DGLEKDRASI EKLHYMVIAS ALVYHTRQQL VIDSLKPMSP
VTGGTSNPKK KYDYIAKIDN DVFEVSLNAG DIKKNWLIEV NKIDDSNTEA DKKTYDVITP
EFEYYRRRLK LSINDNSQMF RLNYHENHTR IAFCGLIRTC AIYSPREWEL YQYMVRDTKE
IQDNTLRCPM PGLITSICVK EGEQVNERQE LVRMESMKME TGIASITF
//
