ID   A0A425Y447_9BACT        Unreviewed;       634 AA.
AC   A0A425Y447;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Carboxylase {ECO:0000313|EMBL:RRG23039.1};
GN   ORFNames=DWB61_06280 {ECO:0000313|EMBL:RRG23039.1};
OS   Ancylomarina euxinus.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae;
OC   Ancylomarina.
OX   NCBI_TaxID=2283627 {ECO:0000313|EMBL:RRG23039.1, ECO:0000313|Proteomes:UP000285794};
RN   [1] {ECO:0000313|EMBL:RRG23039.1, ECO:0000313|Proteomes:UP000285794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1P {ECO:0000313|EMBL:RRG23039.1,
RC   ECO:0000313|Proteomes:UP000285794};
RA   Yadav S., Villanueva L., Damste J.S.S.;
RT   "Draft genome sequence of Ancylomarina sp. M1P.";
RL   Submitted (JUL-2018) 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:RRG23039.1}.
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DR   EMBL; QQWG01000004; RRG23039.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A425Y447; -.
DR   OrthoDB; 9807469at2; -.
DR   Proteomes; UP000285794; Unassembled WGS sequence.
DR   GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProt.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
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; IPR001882; Biotin_BS.
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; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   4: Predicted;
KW   Biotin {ECO:0000256|ARBA:ARBA00023267}.
FT   DOMAIN          27..293
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   DOMAIN          556..631
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          533..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   634 AA;  70568 MW;  E9459062D959E685 CRC64;
     MIYDKHGVLQ MTQLNYGSDR PKAENPIKIN DVSLRDGHQS LFATRGRTED MLPVAEMIDE
     AGYHSVETWG GATFDTMHRF LGEDPWERLR VLKKHMPKTP FSMLLRGQNV VGYRNYADDV
     VQAFVQRSID NGMDIFRCFD ALNDFRNFET AAKVIKDNKK HLQGVVCYTL NEPRLGGEVY
     NMDYYLNKVK DLIAFGVDSV CIKDMAGLVA PYDIYNLVRE IKKFTDTPIN LHTHFTSGMG
     DLAIFKAIEA GVDIVDTCIG PYAYRTSHPA VEPMIMSLLG TNRDSGMDIN KINAIAGEME
     KYIPKYKHLD NSPKYATTDI NVLLHQTPGG MLSNLVNQLK AMDALDKLPE VYRLLPKVRK
     DLGNIPLVTP TSQIVGVQTV NNVLFDSYEG EYAQITKEVK DLCFGLYGKT THPINPEVQK
     KALKGYPRGE EPITARPGSI LEPEMEDVKT EFEGLAKDID DEVLCALYPI TGKRFLKWKY
     GLEEVPADVK AKTMAEVEKE EELVRKALSG ELTSKGKGSG RELEVTVDGE TFTVEINDPN
     GPSTPQFKGR KKKEASKDEF ATGSVVAPIP GMIIEYKVKV GDEVEVGDAL VVLEAMKMMN
     NLDAKAAGTV KEIKCETGDS VAKGDLLLVI EPKA
//