ID U5WBM6_9ACTN Unreviewed; 668 AA.
AC U5WBM6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Propionyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:AGZ46578.1};
GN ORFNames=AFR_41620 {ECO:0000313|EMBL:AGZ46578.1};
OS Actinoplanes friuliensis DSM 7358.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ46578.1, ECO:0000313|Proteomes:UP000017746};
RN [1] {ECO:0000313|EMBL:AGZ46578.1, ECO:0000313|Proteomes:UP000017746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ46578.1,
RC ECO:0000313|Proteomes:UP000017746};
RX PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL J. Biotechnol. 178:41-42(2014).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CP006272; AGZ46578.1; -; Genomic_DNA.
DR RefSeq; WP_023562910.1; NC_022657.1.
DR AlphaFoldDB; U5WBM6; -.
DR STRING; 1246995.AFR_41620; -.
DR KEGG; afs:AFR_41620; -.
DR PATRIC; fig|1246995.3.peg.8423; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_1_11; -.
DR OrthoDB; 249215at2; -.
DR Proteomes; UP000017746; Chromosome.
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: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; PS00866; CPSASE_1; 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:UP000017746}.
FT DOMAIN 1..439
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 115..302
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 594..666
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 668 AA; 70737 MW; AE40A387029ED10C CRC64;
MIRRLLVANR GEIARRVFAT CRLVGIETVA VYSDADSDAP HVTEADYAVH LSGGTAASTY
LRGDLIIAAA KRAGVNAIHP GDGLLAEDPD FAAEVADAGM IWVGPPAKTL GLLHSKIETK
AVVAEAGVPV LPTMTDPETI TDFPVLIKPS GGQGGQGMRV VRDPVTLAEA MASTRQETGD
QVFCEPYVEN VRHIEVPIIA DAHGAVVPFG ERECSVQRRY QKIIEETPSP AVDPALREEL
CRAAIIAVRA IGYVGAGAVE FLLDEQGDFW FLELTPSLQV EHAVTECVSG YDLVRLQLLV
SEGGHLPMPG PPPIRGHAIE VRICAEDPAY AWLPASGTLH RFAVPDVAGS FRPLPQPGLR
LDAGVVDGSV VGLQGDSMLA KLVAWAPTRQ EAARMLASAL TRAQLHGVVA NRDLLVRVLR
HQAFRAGDVD TGFLDRHPEV FAPLLSSVDA VRISCLAAAL AGAAARRATA PVLASLPSGW
RNVPSGSQTA VYDGPAGPVE VGYRMNRHGE LAGWWVRSVD PEELDLAGLG QAPTLDDHPP
TVVVHADGGR VDLDVNGIRL SLKVHRVGDI SYVDSPEGSV TLRELSRFPL PAPEATEGSL
IAPLPGAVRR VLVVPGQRVR AGELLLTLEA MKLEHPVHAP SAGVVASLPV HPGAEVDTGE
LLAVLDPE
//
