ID A0A0A5GE78_9BACI Unreviewed; 449 AA.
AC A0A0A5GE78;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Biotin carboxylase {ECO:0000313|EMBL:KGX91496.1};
GN ORFNames=N783_08045 {ECO:0000313|EMBL:KGX91496.1};
OS Pontibacillus marinus BH030004 = DSM 16465.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385511 {ECO:0000313|EMBL:KGX91496.1, ECO:0000313|Proteomes:UP000030403};
RN [1] {ECO:0000313|EMBL:KGX91496.1, ECO:0000313|Proteomes:UP000030403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH030004 {ECO:0000313|EMBL:KGX91496.1,
RC ECO:0000313|Proteomes:UP000030403};
RA Huang J., Wang G.;
RL Submitted (AUG-2013) 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:KGX91496.1}.
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DR EMBL; AVPF01000002; KGX91496.1; -; Genomic_DNA.
DR RefSeq; WP_027445695.1; NZ_AVPF01000002.1.
DR AlphaFoldDB; A0A0A5GE78; -.
DR STRING; 1385511.GCA_000425225_01347; -.
DR eggNOG; COG0439; Bacteria.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000030403; 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; 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; 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:UP000030403}.
FT DOMAIN 1..445
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 449 AA; 49967 MW; BB579FF61003B6C6 CRC64;
MFNKILIANR GEIASRIIRT CKKLGIQSVA VYSEPDADSP FVSEADESYP LGGTRVHESY
LNIDKILEIA KEAGVEAIHP GYGLLSENGD FANRIEQVGI TFIGPSPEVM SKMGSKVEAR
QTMKDAGVPV IPGTESAVAD VDEAKKAAEE IGYPVMLKAS SGGGGIGMQI VHDDEELAKA
FESNSKRAQM FFGDGTMFLE KKIVDPHHVE IQVLADQEGN TIHLFERECS IQRRHQKVVE
EAPSPFISEE TRNKMGNAAV KAAKAIGYKN AGTIEFLVDE GQNFYFLEMN TRLQVEHPVT
EEITGFDLVH EQLRIANGDS LRYKQEELTM HGHAIEVRVY AEDPKTFYPA PGQMTNLELP
QGDSIRHEVG VHKESMVSPF YDPMIAKCIT WAETRDEAIE NMIYALENYT IEGIKTNIPM
LLDVLKHDAF KQGNTNTHFI QSYLKEEAK
//
