ID A0A1B4XFT7_9GAMM Unreviewed; 613 AA.
AC A0A1B4XFT7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Pyruvate carboxylase subunit B {ECO:0000313|EMBL:BAV33674.1};
GN ORFNames=SCL_1363 {ECO:0000313|EMBL:BAV33674.1};
OS Sulfuricaulis limicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Acidiferrobacterales;
OC Acidiferrobacteraceae; Sulfuricaulis.
OX NCBI_TaxID=1620215 {ECO:0000313|EMBL:BAV33674.1, ECO:0000313|Proteomes:UP000243180};
RN [1] {ECO:0000313|EMBL:BAV33674.1, ECO:0000313|Proteomes:UP000243180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HA5 {ECO:0000313|EMBL:BAV33674.1,
RC ECO:0000313|Proteomes:UP000243180};
RA Miura A., Kojima H., Fukui M.;
RT "Complete genome sequence of a sulfur-oxidizing gammaproteobacterium strain
RT HA5.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; AP014879; BAV33674.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B4XFT7; -.
DR KEGG; slim:SCL_1363; -.
DR InParanoid; A0A1B4XFT7; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000243180; Chromosome.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:InterPro.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProt.
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 Pyruvate {ECO:0000313|EMBL:BAV33674.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000243180}.
FT DOMAIN 8..268
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 536..613
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 530..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 613 AA; 67903 MW; 4DDDEFB3F0317FC9 CRC64;
MASSSKKVMV TDLVLRDAHQ SLLATRMRTE DMLPICDKLD KVGYWSLEAW GGATFDTCLR
FLKEDPWERL RKLKQALPKT PLQMLLRGQN LLGYRHYSDD VVEAFVKKSA ECGVDVFRIF
DAMNDMRNIE VSVKAVLKAG KHAQGAICYT TSPVHTIEHF VEIAREMEKM GCQTIAIKDM
AGLITPARTV ELYQALSKAV KVPLAFHSHT TVGVANICMY LAVEHGARHI DTAISSLSWG
TSHSPTESMV VALRETPYDT GLNLEQLQEI GFYFREVRKK YHQFESEYAE IDTRVQVSQV
PGGMISNLSN QLKEQGALNR MNEVLAEIPR VREDLGFPPL VTPTSQIVGT QAVLNVLTGK
RYKSITNEVK LYLQGRYGKA PGKINETVRS MAIGNEEVIT CRPADKLKPE MHRLRDEIGE
LARSEEDVLT YAMFPEIGRK FLEERAAGTL KPEELKPPKS AEATALPAYA PTDFNVTMHG
ETYHIRVTGA GHKSEEQRPF FVSVDGVPEQ ILIETLTETV PTEAGMVDTR RASRGSKRPK
ASKEGHVTSS MPGTIVDILV KAGVKVKAGD PVLVVEAMKM ENEVPAPVAG TVKAVNVTKG
DSVNPDEALV EIE
//
