ID A0A3R7I5F8_9ACTN Unreviewed; 776 AA.
AC A0A3R7I5F8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 28-JUN-2023, entry version 16.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=DC095_013030 {ECO:0000313|EMBL:RNC73803.1}, SFRA_009115
GN {ECO:0000313|EMBL:RKM97363.1};
OS Streptomyces xinghaiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1038928 {ECO:0000313|EMBL:RKM97363.1, ECO:0000313|Proteomes:UP000028058};
RN [1] {ECO:0000313|EMBL:RKM97363.1, ECO:0000313|Proteomes:UP000028058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19609 {ECO:0000313|EMBL:RKM97363.1,
RC ECO:0000313|Proteomes:UP000028058};
RX PubMed=25477406;
RA Bekker O.B., Klimina K.M., Vatlin A.A., Zakharevich N.V., Kasianov A.S.,
RA Danilenko V.N.;
RT "Draft Genome Sequence of Streptomyces fradiae ATCC 19609, a Strain Highly
RT Sensitive to Antibiotics.";
RL Genome Announc. 2:0-0(2014).
RN [2] {ECO:0000313|EMBL:RKM97363.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 19609 {ECO:0000313|EMBL:RKM97363.1};
RA Danilenko V.N., Bekker O.B., Vatlin A.;
RT "Genome sequencing of Streptomyces fradiae ATCC 19609.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RNC73803.1, ECO:0000313|Proteomes:UP000245280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OlgR {ECO:0000313|EMBL:RNC73803.1,
RC ECO:0000313|Proteomes:UP000245280};
RA Danilenko V.N., Bekker O.B., Vatlin A.;
RT "Genome sequencing of Streptomyces xinghaiensis (fradiae) OlgR.";
RL Submitted (OCT-2018) 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:RKM97363.1}.
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DR EMBL; JNAD02000003; RKM97363.1; -; Genomic_DNA.
DR EMBL; QFBD02000005; RNC73803.1; -; Genomic_DNA.
DR RefSeq; WP_050363764.1; NZ_QFBD02000005.1.
DR AlphaFoldDB; A0A3R7I5F8; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000028058; Unassembled WGS sequence.
DR Proteomes; UP000245280; Unassembled WGS sequence.
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 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; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
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; 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; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 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 SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000028058}.
FT DOMAIN 1..454
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 670..745
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 494..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 776 AA; 78563 MW; 96240FD6B4D40FF5 CRC64;
MFESVLVANR GEIAVRVIRT LRRLGVRSVA VFSDADAEAR HVREADTAVR IGPTAAAESY
LSVERLLDAA ARSGAQAVHP GYGFLAENAA FARACEQAGL VFIGPPPGAI ELMGDKIRAK
ETVRAAGVPV VPGSSGSGLT DAELAAAARE IGMPVLLKPS AGGGGKGMRL VRSEEVLAEE
IAAARREARG SFGDDTLLVE RWIDRPRHIE IQLLADGHGH VVHLGERECS LQRRHQKIVE
EAPSPLLDEA TRAAVGEAAV QAARSCGYRG AGTVEFIVPG SDPSAYYFME MNTRLQVEHP
VTELVTGLDL VEWQLRAAAG EPLGFGQQDI RLTGHAVEAR LCAETARAAD GGRVDFLPSA
GTVRLLREPA GEGVRVDSGL SPGTEVGTAY DPMLAKIIAH GPDRATALRR LRAALAGTDV
LGVDTNAGFL RRLLAHPEVV SGEMDTGLVD RDAASLLRPS VPAEVYAAAA LLRHAALTAG
GGADAGGALG GAAGPGAPGG AAGDAAGAPG AAAGGPEGSG GRPGWTDPFS VPSGWRLGGT
PAWTPHPVGV PGHEPVTVHV RGPLHDAEIR VEEPAVTPAA TPAPAGTAPA AGPDGAGWDG
AEPDGAVRAR LVPGGDGPSA PGARLLLEYA GVTHVFHHAP DGAGGHWLGR DGDAWHATAH
DPVAAALRGG AGAGQAGALT APMPGTVTVV KAAVGDAVTA GQSLLVVEAM KMEHVIAAPH
DGTVTELDVT AGSTVAMDQV LAVVAPHEPA ATAAAADGGP AVPAAAITEE TSDAPS
//
