ID A0A0S8EUH3_9GAMM Unreviewed; 613 AA.
AC A0A0S8EUH3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Pyruvate carboxylase subunit B {ECO:0000313|EMBL:KPK51682.1};
DE EC=6.4.1.1 {ECO:0000313|EMBL:KPK51682.1};
GN ORFNames=AMS22_10515 {ECO:0000313|EMBL:KPK51682.1};
OS Thiotrichales bacterium SG8_50.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales.
OX NCBI_TaxID=1703416 {ECO:0000313|EMBL:KPK51682.1, ECO:0000313|Proteomes:UP000051903};
RN [1] {ECO:0000313|EMBL:KPK51682.1, ECO:0000313|Proteomes:UP000051903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_50 {ECO:0000313|EMBL:KPK51682.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK51682.1}.
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DR EMBL; LJTW01000138; KPK51682.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8EUH3; -.
DR PATRIC; fig|1703416.3.peg.231; -.
DR Proteomes; UP000051903; Unassembled WGS sequence.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:InterPro.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
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; IPR005776; OadA.
DR InterPro; IPR000891; PYR_CT.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR01108; oadA; 1.
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:KPK51682.1};
KW Pyruvate {ECO:0000313|EMBL:KPK51682.1}.
FT DOMAIN 8..268
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 533..613
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 523..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 613 AA; 67420 MW; 31A36563AEBCF4D7 CRC64;
MAKNKDKVLL TDLTLRDGHQ SLIATRMRTD DMVPILGKMD SVGFWSLEAW GGATYDACLR
FLKEDPWERL RKLKEGLPNT PIQMLLRGQN LLGYRHYSDD VVEAFVNKAA ENGVDVFRIF
DAMNDLRNLE TSINAVIAAG KHAQGAISYT TSPVHTIDRF VEQARQLEKM GCHSVCIKDM
AGLLTPARAA ELFGALSKAV KVPLHFHSHT TAGVANISMY EAVRNGARHV DTCMSAFSWG
TSHSPTESMV VAFGGTPYDT GLDLAALQEI GFYFHEVRKK YHQYESEFTS IDTRVQINQI
PGGMISNLSN QLKEQGALDK MGEVLNEIPR VREDLGYPPL VTPTSQIVGT QAVLNVMTGQ
RYKSITNEVK LYLHGRYGEA PGEINETVRN MAIGDEEVIT CRPADLLEPE MDRLRHEIGE
LAKNEEDVLT YAMFPEVGRI FLEERAAGKL QPEELLPAQS AGGNGGLSLA PTDFNVTLHG
ETYHIKVTGF GHKSEDERPF YVTVDGVPEE ILLESLQETV PTEGGYVDTK RASKGSKRPK
ARKEGDVNSS MPGTIVDVLV KEGDTVSAGD AVCVIEAMKM ENEVPAPISG TVKAIHIAKG
DSVNPDESLM EIE
//
