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Database: UniProt
Entry: H5U2E0_9ACTN
LinkDB: H5U2E0_9ACTN
Original site: H5U2E0_9ACTN 
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
//
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