ID A0A1W2FSE5_9PSEU Unreviewed; 1021 AA.
AC A0A1W2FSE5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 28-JAN-2026, entry version 33.
DE SubName: Full=Acetyl/propionyl-CoA carboxylase, alpha subunit {ECO:0000313|EMBL:SMD24845.1};
GN ORFNames=SAMN05660733_07926 {ECO:0000313|EMBL:SMD24845.1};
OS Lentzea albidocapillata.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=40571 {ECO:0000313|EMBL:SMD24845.1, ECO:0000313|Proteomes:UP000192840};
RN [1] {ECO:0000313|Proteomes:UP000192840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44073 {ECO:0000313|Proteomes:UP000192840};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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; FWYC01000023; SMD24845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2FSE5; -.
DR STRING; 40571.SAMN05660733_07926; -.
DR eggNOG; COG0439; Bacteria.
DR eggNOG; COG4799; Bacteria.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000192840; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 3.90.226.10; 2-enoyl-CoA Hydratase, Chain A, domain 1; 2.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR051602; ACC_Biotin_Carboxylase.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
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; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR005479; CPAse_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR48095:SF5; BLL7292 PROTEIN; 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; 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 PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000192840}.
FT DOMAIN 1..403
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 89..288
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 458..725
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 766..1005
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 724..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..740
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1021 AA; 107751 MW; D077AF95874E7950 CRC64;
MLLVANRGEV AVRVLRAAAD LGIRTVAVYA EDDASSLPVT LADRAVALRG PSPYLDIDQL
LDAAEGCQAV HPGWGFLSEN AAFARACSER GLAFVGPSAD ILELLGDKRR ARELAASLGI
PVLDAAPGKF PVMVKAVAGG GGKGMRAVLR PEDLDSAVEA CRAEALAAFG VGDVYFERLM
PSARHIEVQL VGTSVIGDRD CSLQLRHQKV VEIAPAPLLD PLLRKALHSS AMAIASAVDY
QGVGTVEFLV SGDSFAFLEV NPRLQVEHTV TEMVSGVDLV RTQLLLAWGG DVDFTPHDRG
AAVQVRVNQT SGGVLSSFGL PAGPGVRVDT HGYVGYRVGT RYDGLLAKLV VHGEDLDVAL
NRARRALREF RVEGVATNLE FLHTLLDQDI VGATTDFVAE EPVSGMRAPL AGTVVAVDPG
SVVLEAMKMQ HVVRVSGDVL VSVGDTVTEG QVLASGAGES DEDVAEVDLE HVRPDLAEVL
ARHDFDRPEA AARRHARGGR TARENIADLC TSFVEYGGLA IAAQRQRRSL EDLIERTPAD
GMVAGIGVVN GQRVVAMSYD YAVLAGTQGM RNHQKKDRLF ALAQQENLPV VLFAEGGGGR
PGDTDHSMVS GLDCGSFHAF ARLSGQVPLV GVVAGRCFAG NAVLLGTCDV IIAVEGANIG
MGGPAMIEGG GLGTFRPEDI GSLDVQVPNG VVDIAVASEE EAVAVAKKYL SYFQAPAGAQ
VSAGAQAHAG PQAHAGVPSP NAQPSPAPSG EPLKTILPDS TDNFGSWNCA DQRLLRHAIP
ENRLRAYDIR ALITTLADTG SVLELRQGFG KAIVTALVRI EGRPIALIAN DPNVLGGAID
ADAADKCARF LQLADAFDIP VVSLCDTPGF MVGPDAERTA TVRHLTRMVV TGANLTVPFG
LVILRKAYGL GAQAMAAGSL KVPQFAISWP TGEFGPMGLE GAIKLGFRKE LDAIADPDER
RQRYDQMVAM AYEHGKALNV ASVFEIDDVI DPADTRRWIA TALAPATSRS QGKKRPFIDT
W
//
