ID A0A117S1J1_9ACTN Unreviewed; 614 AA.
AC A0A117S1J1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Acety-l/propionyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:KUO20391.1};
GN ORFNames=AQJ91_14730 {ECO:0000313|EMBL:KUO20391.1};
OS Streptomyces dysideae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=909626 {ECO:0000313|EMBL:KUO20391.1, ECO:0000313|Proteomes:UP000053260};
RN [1] {ECO:0000313|EMBL:KUO20391.1, ECO:0000313|Proteomes:UP000053260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RV15 {ECO:0000313|EMBL:KUO20391.1,
RC ECO:0000313|Proteomes:UP000053260};
RA Ruckert C., Abdelmohsen U.R., Winkler A., Hentschel U., Kalinowski J.,
RA Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces sp. RV15, isolated from a marine
RT sponge.";
RL Submitted (OCT-2015) 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:KUO20391.1}.
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DR EMBL; LMXB01000038; KUO20391.1; -; Genomic_DNA.
DR RefSeq; WP_067020923.1; NZ_KQ949081.1.
DR AlphaFoldDB; A0A117S1J1; -.
DR STRING; 909626.AQJ91_14730; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000053260; 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:UP000053260}.
FT DOMAIN 1..425
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 535..612
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 614 AA; 65683 MW; E5FBDE9E4E462930 CRC64;
MITSVLVANR GEIACRVFRT CGELGIRTVA VHSDADANAR HQRVADMAVR LPGAAPSETY
LRADLVVQAA IASGADAVHP GYGFLSENPD FARAVLDAGL IWVGPPPEAI EAMASKTRAK
ELMGLAPLRE VAQGDLPVLV KASAGGGGRG MRIVRRLEEL DAALEGARTE AASAFGDGEV
FVEPYIEDGR HVEVQILADT HGTVWTLGTR DCSLQRRHQK VIEEAPAPGL NPELTATLYE
TATRAARAVA YTGAGTVEFL VTGDQAHFLE MNTRLQVEHP VTEAIHGIDL VALQIRIAEG
HALETPDPPH ARGHAVEARL YAEDPASGWT PQTGTLHHLA VPPSVRLDTG YDDGDEIGVH
YDPMLAKAVA HAPTRADAIR KLAGALERTT IHGPTTNRDL LVRSLRHKEF TTARMDTGFY
TRHLPELTTT DPDPHAPLAA ALADTQGRSR FGGWRNLPSQ PQTKRYAMAG EEHEATYRHT
RVGLSAEGVR VVHADARLVV LEVDGVRRKF EIARYGDQVH VNATTLTALP RFPDPTAQHA
PGSLLAPMPG TVIRVADGLT EGAAVQAGEP LLWLEAMKME HKITAPATGT LTALHAVPGQ
QVAVGALLAV VQPA
//
