ID M3BSR6_9ACTN Unreviewed; 615 AA.
AC M3BSR6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Acetyl/propionyl CoA carboxylase subunit alpha {ECO:0000313|EMBL:EMF26964.1};
GN ORFNames=H114_21513 {ECO:0000313|EMBL:EMF26964.1};
OS Streptomyces gancidicus BKS 13-15.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces pseudogriseolus group.
OX NCBI_TaxID=1284664 {ECO:0000313|EMBL:EMF26964.1, ECO:0000313|Proteomes:UP000011732};
RN [1] {ECO:0000313|EMBL:EMF26964.1, ECO:0000313|Proteomes:UP000011732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BKS 13-15 {ECO:0000313|EMBL:EMF26964.1,
RC ECO:0000313|Proteomes:UP000011732};
RX PubMed=23599292;
RA Kumar S., Kaur N., Singh N.K., Raghava G.P., Mayilraj S.;
RT "Draft Genome Sequence of Streptomyces gancidicus Strain BKS 13-15.";
RL Genome Announc. 1:E00150-13(2013).
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:EMF26964.1}.
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DR EMBL; AOHP01000089; EMF26964.1; -; Genomic_DNA.
DR RefSeq; WP_006134248.1; NZ_AOHP01000089.1.
DR AlphaFoldDB; M3BSR6; -.
DR PATRIC; fig|1284664.3.peg.4317; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000011732; 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; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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:SF126; BIOTIN CARBOXYLASE; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 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:UP000011732}.
FT DOMAIN 1..424
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 97..299
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 534..611
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 615 AA; 65685 MW; EAA3C9873ABC23F8 CRC64;
MITSLLIANR GEIACRIART CRDLGITTVA VHSDADAGAL HTRVADTAVR LPGSAPADTY
LRGDLIVKAA LAAGADAVHP GYGFLSENAD FARAVQDAGL VWIGPPPEAI EAMASKTRAK
QLMGVEPLTD VTEADLPVLV KAAAGGGGRG MRVVRRLADL DAELVAARAE AASAFGDGEV
FVEPYLENGR HVEVQVLADT HGTVWALGTR DCSLQRRHQK VIEEAPAPGL TDALTGELHT
LAVRAVRAVG YVGAGTVEFL VAGGRAHFLE MNTRLQVEHP VTEEVFGIDL VAGQIRVAEG
HALDPEPPAP RGHAIEARLY AEDPAQDWAP QTGRLHRLTV PGSVRLDTGH TDGDDIGVHY
DPMLAKVVAH APTRAEAIRK LAAALDRAVI HGPVTNRDLL VRSLRHEEFT EGRMDTGFYD
RHLPALTVPA ADPHAPLAAA LADAHGRSRF GGWRNVPSQP QIKRYAMNGE EHEVRYRHTR
TGLVADGVTV VHADASLVIL ETDGVRRRYE VSRHGDRVYV GTTSLTALPR FPSPEPEHAP
GSLLAPMPGT VVRIAEGVTE GMSVEAGRPL LWLEAMKMQH KITAPTSGTL TTLHATEGQQ
VQPGALLAVV EDNTR
//
