ID C5S1G1_9PAST Unreviewed; 603 AA.
AC C5S1G1;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE SubName: Full=Pyruvate carboxylase subunit B {ECO:0000313|EMBL:EER47392.1};
DE EC=4.1.1.3 {ECO:0000313|EMBL:EER47392.1};
GN ORFNames=AM305_08694 {ECO:0000313|EMBL:EER47392.1};
OS Actinobacillus minor NM305.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=637911 {ECO:0000313|EMBL:EER47392.1, ECO:0000313|Proteomes:UP000005532};
RN [1] {ECO:0000313|EMBL:EER47392.1, ECO:0000313|Proteomes:UP000005532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM305 {ECO:0000313|EMBL:EER47392.1,
RC ECO:0000313|Proteomes:UP000005532};
RX PubMed=19819087; DOI=10.1016/j.vetmic.2009.09.030;
RA Arya G., Niven D.F.;
RT "Production of haemolysins by strains of the Actinobacillus
RT minor/"porcitonsillarum" complex.";
RL Vet. Microbiol. 141:332-341(2010).
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:EER47392.1}.
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DR EMBL; ACQL01000085; EER47392.1; -; Genomic_DNA.
DR RefSeq; WP_005823629.1; NZ_ACQL01000085.1.
DR AlphaFoldDB; C5S1G1; -.
DR eggNOG; COG0511; Bacteria.
DR eggNOG; COG5016; Bacteria.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000005532; Unassembled WGS sequence.
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 Lyase {ECO:0000313|EMBL:EER47392.1};
KW Pyruvate {ECO:0000313|EMBL:EER47392.1}.
FT DOMAIN 8..268
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 525..603
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 459..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 603 AA; 65055 MW; 86AAA69BA65FF985 CRC64;
MTTQTKKIAI TDVVLRDAHQ SLFATRLRLD DMLPIAAELD KIGYWSLEAW GGATFDSCIR
FLGEDPWVRL RELKKAMPKT PLQMLLRGQN LLGYRHYADD VVDKFVERSV ANGMSVFRVF
DALNDPRNMK QALQAVKKQG GHAQGTLSYT TSPVHTLQTW LDVTEQLLEI GIDSLVIKDM
SGILTPMAAH ELVIEIKKRY DVELHLHCHS TTGMAEMALL KAIEAGVDGV DTSISSMSGT
YGHPATESIV ATLQGTPYDT GLSIPELEKI AAYFRNVRKK YAKFEGQLRG IDSRILVAQV
PGGMLTNLES QLKQQNASDK LDLVLQEIPK VREDLGNIPL VTPTSQIVGT QAVMNVLMGE
RYKTIAKETA GILKGEYGRT PAPVNAALQA RVLEGAAPIT DRPADHIAPE MDKIVAEVVA
TAKEKGIALS ENTVDDALIV ALFQQVGWKF LENRNNPSAF EPVPNGEEAK PTTAAQPKAQ
PQTGPAVYTI EVEGKAYVVK VSEGGDITNI APTTAAPAPA APQAVTSVPN SANAEPVKAP
MAGNILKVEV SEGQQVAEGD VLLILEAMKM ETQICAAKAG VVQGISTKQG DVVAVDQVLM
SIA
//
