ID A0A1P8F812_9CHLR Unreviewed; 668 AA.
AC A0A1P8F812;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Pyruvate carboxylase subunit B {ECO:0000313|EMBL:APV44588.1};
DE EC=6.4.1.1 {ECO:0000313|EMBL:APV44588.1};
GN Name=pycB {ECO:0000313|EMBL:APV44588.1};
GN ORFNames=Dform_01260 {ECO:0000313|EMBL:APV44588.1};
OS Dehalogenimonas formicexedens.
OC Bacteria; Chloroflexota; Dehalococcoidia; Dehalogenimonas.
OX NCBI_TaxID=1839801 {ECO:0000313|EMBL:APV44588.1, ECO:0000313|Proteomes:UP000185934};
RN [1] {ECO:0000313|Proteomes:UP000185934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSZ-14 {ECO:0000313|Proteomes:UP000185934};
RA Key T.A., Bowman K.S., Lee I., Chun J., Albuquerque L., da Costa M.S.,
RA Rainey F.A., Moe W.M.;
RT "Dehalogenimonas formicexedens sp. nov., a chlorinated alkane respiring
RT bacterium isolated from contaminated groundwater.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP018258; APV44588.1; -; Genomic_DNA.
DR RefSeq; WP_076004257.1; NZ_CP018258.1.
DR AlphaFoldDB; A0A1P8F812; -.
DR STRING; 1839801.Dform_01260; -.
DR KEGG; dfo:Dform_01260; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000185934; Chromosome.
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:APV44588.1};
KW Pyruvate {ECO:0000313|EMBL:APV44588.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000185934}.
FT DOMAIN 6..272
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 585..667
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 545..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..561
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 668 AA; 72388 MW; A95624DA1E336766 CRC64;
MPAQPLKVTD LTLRDGHQSL FATRMRTDDI LGIIGEMDEV GFHSMEVWGG ATFDVPIRFL
NEDPWDRLRE MKKRAPKTPL QMLLRGQNLV GYRNYADDVV TAFVEHAADC GVDIFRVFDA
VNDERNFETA LKAIKSKGKH AQLAISYSLT ARVMGGPVYN LDYYIEKAKK FEAMGADSFC
IKDMAGIIAP NDAYNLVKAL KKAIKIPIQF HSHYTSGMAS MSMLKAVEAG ADVVDACLAP
WALRTSHPAV EPMVASLTAT SRDTGLDLHQ LLKLGEYFEA ISPKYRDFMD TTKTAVIDTA
VLEHQVPGGM ISNLVSQLRE AGALNRIDEV YEEIPRVRKE MGYPPLVTPT SQIVGIQAVQ
NVLFGRYKVI SAQVKDYFYG LYGRPPMPVD PEIQKLALKG YERGETPITV RPADVLKPEL
EAAREATEGI AKDIGDVLTY ALYPQVGLRF LKWKYGLETP PADTRARTLE DVNKEDEIIA
KAKAGKLVEK GSEKLVAQAS VSSPAPVTGL RHFNVHLDGK VYCVGVEATA AAAPAVAFVA
PPPALAQPAA PPPPPSPVEP KPAAKQVETA KPVEAPKSVE IPAAKVEAKA AAGPEPCGED
VLAPMPGVVL RYEVKVGDKV KSGDTVVVLE AMKMAIDLPS PANGTVAAIK FAVGDRVSRD
DVLAIIAA
//
