ID A0A0X3XFQ4_9ACTN Unreviewed; 467 AA.
AC A0A0X3XFQ4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Acetyl-/propionyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:KUL68107.1};
DE Flags: Fragment;
GN ORFNames=ADL34_33535 {ECO:0000313|EMBL:KUL68107.1};
OS Streptomyces sp. NRRL WC-3605.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609103 {ECO:0000313|EMBL:KUL68107.1, ECO:0000313|Proteomes:UP000052945};
RN [1] {ECO:0000313|EMBL:KUL68107.1, ECO:0000313|Proteomes:UP000052945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3605 {ECO:0000313|EMBL:KUL68107.1,
RC ECO:0000313|Proteomes:UP000052945};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KUL68107.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LLZN01000122; KUL68107.1; -; Genomic_DNA.
DR RefSeq; WP_062674824.1; NZ_LLZN01000122.1.
DR AlphaFoldDB; A0A0X3XFQ4; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000052945; 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 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; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR48095:SF2; BIOTIN CARBOXYLASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 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 PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 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:UP000052945}.
FT DOMAIN 1..443
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 467
FT /evidence="ECO:0000313|EMBL:KUL68107.1"
SQ SEQUENCE 467 AA; 49628 MW; 50E2793755CAE4B3 CRC64;
MRKVLIANRG EIAVRVARAC RDAGIASVAV YADPDRDALH VRAADEAFAL GGDTPATSYL
DIDKVLTAAR EAGADAVHPG YGFLSENAEF AQAVLDAGLI WIGPPPQAIR DLGDKVAARH
IAQRAGAPLV AGTPDPVSGA EEVVAFAKEH GLPIAIKAAF GGGGRGLKVA RTLEEVPELY
DSAVREAVAA FGRGECFVER YLDKPRHVET QCLADTHGNV VVVSTRDCSL QRRHQKLVEE
APAPFLSDAQ VEELYAASKA ILKEAGYVGA GTVEFLVGVD GTISFLEVNT RLQVEHPVTE
EVAGIDLVRE MFRIADGEEL GYGDPVLRGH SFEFRINGED PGRGFLPAPG TVTTFAPPSG
PGVRLDAGVE SGSVIGPAWD SLLAKLIVTG ATREQALQRA ARALEEFQVE GMATAIPFHR
AVVKDPAFAP ELTGSADPFT VHTRWIETEF VNDIKPFTAP TDTGTDE
//
