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Database: UniProt
Entry: A0A0A1MK85_9BACI
LinkDB: A0A0A1MK85_9BACI
Original site: A0A0A1MK85_9BACI 
ID   A0A0A1MK85_9BACI        Unreviewed;       451 AA.
AC   A0A0A1MK85;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Acetyl-/propionyl-coenzyme A carboxylase alpha chain {ECO:0000313|EMBL:CEI83513.1};
GN   Name=accA1 {ECO:0000313|EMBL:CEI83513.1};
GN   ORFNames=BN997_03428 {ECO:0000313|EMBL:CEI83513.1};
OS   Oceanobacillus oncorhynchi.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=545501 {ECO:0000313|EMBL:CEI83513.1, ECO:0000313|Proteomes:UP000040453};
RN   [1] {ECO:0000313|EMBL:CEI83513.1, ECO:0000313|Proteomes:UP000040453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Oc5 {ECO:0000313|EMBL:CEI83513.1,
RC   ECO:0000313|Proteomes:UP000040453};
RA   Urmite Genomes Urmite Genomes;
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CDGG01000001; CEI83513.1; -; Genomic_DNA.
DR   RefSeq; WP_042533820.1; NZ_JAUDBP010000004.1.
DR   AlphaFoldDB; A0A0A1MK85; -.
DR   STRING; 545501.BN997_03428; -.
DR   OrthoDB; 9807469at2; -.
DR   Proteomes; UP000040453; 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:UP000040453}.
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   451 AA;  50006 MW;  7553FE856D179531 CRC64;
     MIQKVLIANR GEIARRILRS CKESGIRTVA VYSEADENAL FKQEADEAYP IGPSQVQQSY
     LQLDKIIEVA KKTNADAIHP GYGFLSESPS FAERCKEEGI IFIGPEAAIL SLMGSKIEAR
     KAMIAAGVPV IPGTDRAVES LEEAVTFAEQ IGYPVMLKAS AGGGGIGMEV VHTSDELRKA
     FENNSKRALS FFGDGAMFLE KHITNSRHIE VQVLADCHQH TVHLFERECS IQRRNQKVLE
     EAPSPSISEA LRMKLGETAV IAAEAIDYTN AGTIEFLVDE SEQFYFLEMN TRIQVEHPVT
     EEITGIDIVK EQIRIANQQA LSFTQEEITR NGHAIEIRVY AEDPIRFFPS PGKITALELP
     EGEGVRNECA VASGDMVTPF YDPMIAKLIV FGENRAEARN KLEKALGRFK IEGIKTNIPM
     LQEIITYEAF KKGNTPTNFL DKYYQPTTGG N
//
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