ID B3EI58_CHLL2 Unreviewed; 611 AA.
AC B3EI58;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Biotin/lipoyl attachment domain-containing protein {ECO:0000313|EMBL:ACD89888.1};
GN OrderedLocusNames=Clim_0808 {ECO:0000313|EMBL:ACD89888.1};
OS Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290315 {ECO:0000313|EMBL:ACD89888.1, ECO:0000313|Proteomes:UP000008841};
RN [1] {ECO:0000313|EMBL:ACD89888.1, ECO:0000313|Proteomes:UP000008841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 245 / NBRC 103803 / 6330
RC {ECO:0000313|Proteomes:UP000008841};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T., Liu Z.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium limicola DSM 245.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001097; ACD89888.1; -; Genomic_DNA.
DR RefSeq; WP_012465767.1; NC_010803.1.
DR AlphaFoldDB; B3EI58; -.
DR STRING; 290315.Clim_0808; -.
DR KEGG; cli:Clim_0808; -.
DR eggNOG; COG0511; Bacteria.
DR eggNOG; COG5016; Bacteria.
DR HOGENOM; CLU_000395_4_3_10; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000008841; Chromosome.
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 4..276
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 538..611
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 611 AA; 65736 MW; AE700870ED8436E7 CRC64;
MKKIRFMDVS FRDGFQSCYG ARVKTADFIP ALEAAVQAGT DNFEIGGGAR FQSLYFYCQE
DAFDMMDAAR RIVGPDINLQ TLSRGANVVG LVSQSRDIID LHARMFKKHG ITTIRNFDAL
MDVRNIAYSG QCIHNAGLKH QVVIALMGLP PGLKETYCHT PQFYLDKLRE ILDAGIPFDS
VAFKDASGAT TPVVVYESIK GARKMLPEGT VIEFHTHDTA GMGVACNYAA IEGGADIIDL
AMAPVSGGTA EVDILTMWHR LRGTDYTLDI DHEKYIEVEG LFMNQMEKYY MPPEAKEVNP
LIPFSPMPGG ALTANTQMMR DTNTLHLFPE VIRNMREVVA KGGFGSSVTP VSQFYFQQAF
ANTVQGPWKK ITESYGKMVL GYFGRTPAEP DPEVVRLASE QLGLQPTTED VHDINDRNPE
LGIAFNRGLL EKAGLPTTEE NIFISATCGA KGISFLKGDK PLGIRFKADV EAEAAAKAAP
KNVSSPTVST AKPAKSGMSN YIITVDGKSY NVSVAEGTGA VKSAAPTVPA AATSQAQAAG
EGTPVETSLP GTVMAIEVEV GDMVREGDDV VIIEAMKMES PVKAPKSGKV VSIDVAVGDT
VATGDALLYI A
//
