ID A0A1G1ACK0_9BACT Unreviewed; 605 AA.
AC A0A1G1ACK0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Biotin attachment protein {ECO:0000313|EMBL:OGV68169.1};
GN ORFNames=A2498_14935 {ECO:0000313|EMBL:OGV68169.1};
OS Lentisphaerae bacterium RIFOXYC12_FULL_60_16.
OC Bacteria; Lentisphaerota.
OX NCBI_TaxID=1798582 {ECO:0000313|EMBL:OGV68169.1, ECO:0000313|Proteomes:UP000178496};
RN [1] {ECO:0000313|EMBL:OGV68169.1, ECO:0000313|Proteomes:UP000178496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGV68169.1}.
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DR EMBL; MHBQ01000005; OGV68169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1ACK0; -.
DR STRING; 1798582.A2498_14935; -.
DR Proteomes; UP000178496; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR003379; Carboxylase_cons_dom.
DR InterPro; IPR000891; PYR_CT.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR45266; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR PANTHER; PTHR45266:SF3; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF02436; PYC_OADA; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 4: Predicted;
FT DOMAIN 4..274
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 527..602
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 605 AA; 64433 MW; CC0550BF8CBD57BE CRC64;
MKKIDTMITA FRDGFQSVYG ARVYTNDYLP AIEATRAAGL THFEAGGGAR FQAPVFYCNE
NPFEAMDAFR RAAGPAANLQ TLARGVNVVA LDSQSSDIVR LHAVLFKRHG MTTIRNFDAL
NDVDNLVDSG QFIHDAGLRH EICISMMALP PGCTGAHDAD FYERTMRVIL DAGIPYDSVC
FKDASGTSTP ATIFDTIQRA RRRFPAGTRI VFHTHDTAGT GIACYLAALH GGADQVDLSM
APVSGGTCQP DVISLWHALR GSEFDLDLNI DKIIEAESVL KECMKDYFMP PEAKAVEPLI
PFSPMPGGAL TANTQMMRDN GILDRYPEVI KAMGEVVRRG GFGTSVTPVS QFYFQQAFNN
VMFGPWKKIA KGYGKMVLGY FGRTPVPPDP DIVKQAAEQL KLEPTTRKVL AINDADPAKG
EAACRALLKE AGINNPGDEA IFITASCGKK GIDFLLGKAV PNGVRKRVPT AAVPAAAAAG
YTVSVNGRSY TVVINGDKAE VNGKPYDVSV VEGVSAATNG AEAVKPASTV GATLPVHAPM
PGKVVRIPVK VGDPVDLNGV LLVLEAMKME LEVKSPSAGK VAAINVSAGD QVQAGQILIS
LTDVA
//
