ID A0A3E1F044_9FLAO Unreviewed; 486 AA.
AC A0A3E1F044;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Acetyl-CoA carboxylase biotin carboxylase subunit {ECO:0000313|EMBL:RFC55186.1};
GN ORFNames=DXU93_05025 {ECO:0000313|EMBL:RFC55186.1};
OS Brumimicrobium aurantiacum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Crocinitomicaceae; Brumimicrobium.
OX NCBI_TaxID=1737063 {ECO:0000313|EMBL:RFC55186.1, ECO:0000313|Proteomes:UP000257127};
RN [1] {ECO:0000313|EMBL:RFC55186.1, ECO:0000313|Proteomes:UP000257127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N62 {ECO:0000313|EMBL:RFC55186.1,
RC ECO:0000313|Proteomes:UP000257127};
RA Du Z.-J., Luo H.-R.;
RT "The draft genome squence of Brumimicrobium sp. N62.";
RL Submitted (AUG-2018) 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:RFC55186.1}.
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DR EMBL; QURB01000002; RFC55186.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E1F044; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000257127; 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}.
FT DOMAIN 1..445
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 486 AA; 54412 MW; C73653EC9A1CA0AE CRC64;
MKKVLIANRG EIARRVIRTL KKMNIASVAV YSEADRNAPF VHEADESVLI GPAPSAESYL
VQDKIIDAAK DLNVDGIHPG YGFLSENAEF AERLKKEGIT LIGPSAEAMQ LMGDKLSAKQ
AVKAYDVPLV PGIDKAVVDF DEAKEIAVQI GFPVLIKASA GGGGKGMRLV EKAEDMKEQM
ELAQSEARSS FGNDAVFVEK FVTKPRHIEI QIFADNHGNV IYLHERECSI QRRHQKVIEE
APSAVLTPEL RQRMGESACA VAKACNYSGA GTVEFLLDGD LNFYFLEMNT RLQVEHPVTE
EITGLDLVEM QIRVANNEML SIKQEDVQLN GHAMEVRVYA EDALSNFTPD IGTLNRYQKP
VADYIRIDDA FEEGMEIPIY YDPMIAKLVT WGENREESID RMIKAIDAYE ISGLRTTLDF
GKYVMKHEAF RSGDFDTNFI KHYFSDPNVL HTAQEEEKRA LEASLDTLWN DVIEKKNNEV
ASELIK
//
