ID A0A0W0GI28_9CHLR Unreviewed; 667 AA.
AC A0A0W0GI28;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Pyruvate carboxylase subunit B {ECO:0000313|EMBL:KTB48231.1};
DE EC=6.4.1.1 {ECO:0000313|EMBL:KTB48231.1};
GN ORFNames=DEALK_10760 {ECO:0000313|EMBL:KTB48231.1};
OS Dehalogenimonas alkenigignens.
OC Bacteria; Chloroflexota; Dehalococcoidia; Dehalogenimonas.
OX NCBI_TaxID=1217799 {ECO:0000313|EMBL:KTB48231.1, ECO:0000313|Proteomes:UP000053947};
RN [1] {ECO:0000313|EMBL:KTB48231.1, ECO:0000313|Proteomes:UP000053947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP3-3 {ECO:0000313|EMBL:KTB48231.1,
RC ECO:0000313|Proteomes:UP000053947};
RA Key T.A., Richmond D.P., Bowman K.S., Cho Y.-J., Chun J., da Costa M.S.,
RA Rainey F.A., Moe W.M.;
RT "Genome sequence of the organohalide-respiring Dehalogenimonas
RT alkenigignens type strain (IP3-3T).";
RL Submitted (JUN-2015) 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:KTB48231.1}.
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DR EMBL; LFDV01000002; KTB48231.1; -; Genomic_DNA.
DR RefSeq; WP_058439248.1; NZ_KQ758903.1.
DR AlphaFoldDB; A0A0W0GI28; -.
DR STRING; 1217799.DEALK_10760; -.
DR PATRIC; fig|1217799.6.peg.1108; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000053947; Unassembled WGS sequence.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
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 Ligase {ECO:0000313|EMBL:KTB48231.1};
KW Pyruvate {ECO:0000313|EMBL:KTB48231.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053947}.
FT DOMAIN 6..272
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 589..666
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 543..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 667 AA; 72647 MW; DA588FEA58680B10 CRC64;
MPAQPLKITD LTLRDGHQSL FATRMRTDDI LGIIGDMDQA GFHSMEVWGG ATFDVPIRFL
NEDPWDRLRE MKKRATRTPL QMLLRGQNLV GYRNYADDVV TAFVEHAADC GVDIFRVFDA
VNDERNFETA LAAIKSRGKH AQLAISYSLT ERTMGGPVYN LDYYIEKAKK FEAMGADSFC
IKDMAGIIAP NDAYTLVKAL KKALKIPVQF HTHYTSGMAS MSMYKAVEAG ADIVDTCLAP
WALRTSHPAV EPFVAAFSGQ PRDTGLNLHQ LLKLGDYFES ITPKYRDFQD TTRMSAIDTA
VLEHQVPGGM ISNLVSQLRE AGALNRIDEV YEEIPRVRRE MGFPPLVTPT SQIVGIQAVQ
NVLFGRYKVI SAQVKDYFYG LYGRPPMPVD PEIQRLALKG YERGESPITV RPADVLKPEL
EAAKEATKGI ARDIGDVLTY ALYPQVGLRF LKWKYGLETP PADVKAKTLD DVKREDELIA
KARAGKLAEK TAEKPAAPAP SPVSVPASGL RHFNVHLDGK VYCVGVEPTA TAAPAVYAAP
PAQRSAAAPP PATAVRHEPV EGPKAVEPPK PVVTPKPVES PVAEAEAKPA AAPEPCGEDV
LAPMPGVVLR YEVKVGDKVK SGDTVVVLEA MKMAIDLPSP ADGTVAAVKF GVGDRVSRDD
VLAIIVP
//
