ID A0A222SI27_9CHLB Unreviewed; 612 AA.
AC A0A222SI27;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Biotin attachment protein {ECO:0000313|EMBL:ASQ90648.1};
GN ORFNames=CHL67_06655 {ECO:0000313|EMBL:ASQ90648.1};
OS Prosthecochloris sp. GSB1.
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Prosthecochloris.
OX NCBI_TaxID=281093 {ECO:0000313|EMBL:ASQ90648.1, ECO:0000313|Proteomes:UP000201322};
RN [1] {ECO:0000313|Proteomes:UP000201322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TY Vent \ GSB1 \ Ty-1 {ECO:0000313|Proteomes:UP000201322};
RA Bryant D.A., Liu Z., Li T., Zhao F., Garcia Costas A.M.;
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP022571; ASQ90648.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A222SI27; -.
DR KEGG; pros:CHL67_06655; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000201322; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000201322}.
FT DOMAIN 4..276
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 537..612
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 477..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 612 AA; 65603 MW; 006B62738ECBAD1C CRC64;
MKKIRFMDVS FRDGFQSCYG ARVKTDDFLP VLEAAVAAGT DNFEIGGGAR FQSLYFYCQE
DAFDMMDAAR KVVGPDINLQ TLARGANVVG LVSQSRDIID LHARMFRKHG ISTIRNFDAL
MDVRNIAYSG QCIHNAGLKH QVVIALMGLP PGLNEKYCHT PQFYIDKLKE IIDAGVPFDS
VAFKDASGTT TPAIVYEAIK GARKMLPSDT VIQFHTHDTA GMGVACNFAA IEAGADIIDL
AMAPVSGGTA EVDILTMWHR LRGTGYTLDI DHEKIIEVEA MFIDHMDKYY MPPEAKEVNP
LIPFSPMPGG ALTANTQMMR DNNSLHLFPE VIRNMREVVA KGGFGSSVTP VSQFYFQQAF
ANTVQGKWKK ITESYGKMVL GYFGKTPAEP DPEIVSLASG QLGLQPTKED VHDINDRNPE
LGIDYNRTLL EKEGLPTTEE NIFIAATCGA KGIAFLKGDA PLGIRYKADV EAETAAKVAP
KSGPKSDAVS SMPRSSSGNY TVTVDGRAYN VTVAEGSGAV QSVSPAPSAA APAQAAAETQ
GDGSPVEAAM PGSVVAIEVE VGDSVSEGDD VMIIEAMKME SPVKAPKSGK VVSIEVAPGD
TVATGDVLMY IA
//
