ID H5U2E0_9ACTN Unreviewed; 1851 AA.
AC H5U2E0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=GOSPT_085_00160 {ECO:0000313|EMBL:GAB39898.1};
OS Gordonia sputi NBRC 100414.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1089453 {ECO:0000313|EMBL:GAB39898.1, ECO:0000313|Proteomes:UP000005845};
RN [1] {ECO:0000313|EMBL:GAB39898.1, ECO:0000313|Proteomes:UP000005845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100414 {ECO:0000313|EMBL:GAB39898.1,
RC ECO:0000313|Proteomes:UP000005845};
RA Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Gordonia sputi NBRC 100414.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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:GAB39898.1}.
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DR EMBL; BAFC01000083; GAB39898.1; -; Genomic_DNA.
DR RefSeq; WP_005206775.1; NZ_BAFC01000083.1.
DR eggNOG; COG4770; Bacteria.
DR eggNOG; COG4799; Bacteria.
DR Proteomes; UP000005845; Unassembled WGS sequence.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
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; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR013537; AcCoA_COase_cen.
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; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
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; PF08326; ACC_central; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
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 SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50989; COA_CT_CTER; 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}; Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 1..452
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 125..323
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 579..655
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1540..1818
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 1824..1851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1837..1851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1851 AA; 201295 MW; 94AB52AD3FF799B5 CRC64;
MFTRIAIVNR GEAAMRLIHA VRGLSAETGQ PIEVVALHTD VDRNATFVRE ADIAYNLGAA
ADRPYLNLKV LEHALLETGA DAAWVGWGFV AEDPLFAELC DRIGVTFIGP SAEAMRKLGD
KIGAKLIAEE VGVPVAPWSR GSVDTIDDAL EAAASIGYPL MLKATAGGGG RGIRVITSDD
ELRDAFDRTR DEAARAFGSG VVFLERLVTG ARHVEVQVIA DGQGTAWALG VRDCSVQRRN
QKIIEESASP VLAPEQVTDL KTSAERLAVA VGYRGAATVE FLYHPGEHLF AFLEVNTRLQ
VEHPITECTT GIDLVRAQLH VASGGRLDGE PPAERGHAIE ARLNAEDPDR DFAPAPGRIS
RLELPAGPGI RVDTGVSEGD TIPADFDSMI AKIIAYGANR NEALGRLRRA MSETRVVIEG
GATNKSFVLE LLGQPAVIDG SADTGWIDRV RAENGLIVNR HSAIALIAAA IDSYEEEEAV
ERQRLLSTAS GGRPQVQHES GRPLDLKLRG AAYRVRVARI GASRFRVSIE SGTDTYTADV
DIERFDEHAA QMVLNGVRYR LVTDTHGPTH LIDVDGVAHR VSRDEGGVVR SPAPALVVAT
PLAVGDEVEA GAPVLVLESM KMETVLRAPV RSRLKECSVS VGSQVETGAT LMRLEPIADA
EDDDEAAQAP VESVELELPA APDNIDPDVR TTRTQEDLRS QLLGYDVDPH DRSRLLDDYL
TVRREVRASG RRPIGDELEL LTVFADLAEL SQKRPPVGLN PGFEHVHSSR ENFHTYLQSL
DVERDGLPEA FHDQLRLALR HYGVTELDRS PELEAAVFRI FLTLQNPGAS VTVITTLLRE
WLNEPTPRDE LREDIGFALD RIVAATQVRF PAIADLARGV IYAWYGQAML LRDRARVYTN
VRKHLKYLDE NPDAADRSER IADMVRSTEP LVRLLGQRIQ RDGTDNTVML EVLTRRYYGN
KGVDVIATQT ARGTTFVVAA RDGASVVSAA VPFDELASAA SGLIELARNS AAIAADIYVS
WEDQPDDFDT MAAALHEIVA ASPMPGQVQR VTFTVAGRGT AVMHHHFTFR PSATGMVEER
LIRGLHPYIA QRMRMERLRK FDLTRLPSAD DEEIYLFRAV AKENPADDRL VAFAQVRDLS
SLREHDGRLL SLPTAETVLA SCADSIRRAK RGQKRALNTN RIVMYVWPPI DASSDDLATI
ADHIRGTTAD VGLEEVQLIA RRRDRETGEL RKVSIRFSVN ATGGFDVSVG EPSTDPIEPV
DEYRQKVLSA ARRNTVYPYE LTGLLGDFRE YDLDAEQRLV PVARPKGQNT AAIVAGVVTT
PTEKYPQGIA RVVLLGDPTK SLGALSEPEC ARVIAALDLA EEMKVPLEWY ALSSGARISM
DSGTENMDWV ARALKRVVEF TQDGGEINIV VAGINVGAQP YWNAEATMLM HTKGILVMTP
ESAMVLTGKQ SLDFSGGVSA EDNFGIGGYD RVMGPNGQAQ YWAPNLGAAR DVLMAHYDHT
YVMPGEQTPR RLITSDPVDR DISDYPHVLA GSDFTTVGQI FSKEMNPDRK KPFDIRTVIR
AVADQDHQVL ERWAGMADAE TAVVSDVHLG GIPVCLLGIE SREVSRRGYT PTDGPDTYTA
GTLFPQSSKK AARAINSASG NRPLVVLANL SGFDGSPESM RKLQLEYGAE IGRAIVNFRG
PIVFCVISRY HGGAFVVFSK ALNPNMTVLA IDGSFASVLG GAPAAAVVFA GDVNKRVATD
PRVRDIEARL AQASGSDRSA LSAELADVRQ SVRAETINAV AAEFDAVHSI RRAVEVGSVD
AVIDAAELRP RIIAAIEGNA TWSHRRHEAA DPEQVDPQQI GTEQVGTSSE S
//