ID A0A2T0ZVY5_9ACTN Unreviewed; 1100 AA.
AC A0A2T0ZVY5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Biotin-dependent enzyme {ECO:0000313|EMBL:PRZ40525.1};
GN ORFNames=CLV47_11658 {ECO:0000313|EMBL:PRZ40525.1};
OS Antricoccus suffuscus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Antricoccaceae; Antricoccus.
OX NCBI_TaxID=1629062 {ECO:0000313|EMBL:PRZ40525.1, ECO:0000313|Proteomes:UP000237752};
RN [1] {ECO:0000313|EMBL:PRZ40525.1, ECO:0000313|Proteomes:UP000237752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100065 {ECO:0000313|EMBL:PRZ40525.1,
RC ECO:0000313|Proteomes:UP000237752};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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:PRZ40525.1}.
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DR EMBL; PVUE01000016; PRZ40525.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0ZVY5; -.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000237752; 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; IPR034733; AcCoA_carboxyl_beta.
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; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_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; PF00364; Biotin_lipoyl; 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 SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50989; COA_CT_CTER; 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:UP000237752}.
FT DOMAIN 3..461
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..324
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 485..563
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 841..1082
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 1100 AA; 118511 MW; B2013DBE189079FB CRC64;
MTSISKVLIA NRGEVATRVA RAVAGLGLRS VGIHSADDGD SLHLRHCDEI VALDGSGPSA
YLDGEQIVRR AVEIGASHIH PGYGFLSENA DFARACEKHG IVFVGPAADV LEEFGDKSKA
RALALAHDVP ILPGTPHAAT KEQMRDFIDG LGAAFTEGKV AALIKAVAGG GGRGMRIVRR
LDELEAAYDL CAAEAQGAFG SPDVYIEQLL PSAQHIEVQL IGDGTGAVSH IWDRDCSIQR
RNQKLIEIAP SRIVDAELRQ RILYAAKRLA GALNYRGLAT VEFLVGEDGD YYFMETNPRL
QVEHTVTEEV TGLDLVRAQI QVCCGLTLDD LGLEQEQIPE PRGYAVQVRL NAEIMQQDGT
TIPQTGRISA FHLASGRGIR ADANAYAGYS VNPRFDSLLA KLIVHSNLDD FESVAAIADR
ALAESQISGV ETNISLQRAI LRSAEFRSGT ARTNFVDSNI QTLLEAVPVA PALFADHAAT
GQVTHAAVAV PEGVIGVESP MSGAVVSVDV APGDTVRAGQ TLLVLESMKM QHVIAAPEAG
EVREIYTSTG DVVDANAIVV AYEPRNASGG DTAEQRQIDP DYIRPDLNAL IERKKFLWDE
NRPRAVEKRH KLGKRTVREN VERLVDPGTF VEYNSLVIAA QRKRRSLDDL IENTPADGLV
TGLARVGEAT FGREKSMCAV FAYDYTVLAG TQGYWNHKKT DRIFDVAYRQ QHPVILFCEG
GGGRPGDVDP DKVSGLSNPS WLWLGKLSGT VPFVGITSGR CFAGNAAMLG VCDVVIATSD
SNIGMGGPAM IEGGGLGVFA PEEIGPIDVQ THNGVVDIEV EDEDEAVDVA KKYLSYFQGD
LPDFQAHDQR LLRHVIPENR KRVYDVRQAI ELLFDVDSVL ELRPKFGTTI VTALARLEGR
AVGVIANNPK VLGGAIDSDG SDKAARFIQL CDVFGIPIVS LCDTPGFMVG PDSEKTASVR
HMSRMFLRGG NASVPIAMVV LRKCYGLGGM AMGGASTFVP MIGLAWPTSE FGGMGLEGAV
RLGFRKELEA IDDPGERETR YQELVDGMYE WGGGINTATH LEIDDVIDPA DTRRLLTLSL
GDVEKGKWTN SHSNPLIDAW
//
