ID Q08MD5_STIAD Unreviewed; 484 AA.
AC Q08MD5;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE SubName: Full=Pyruvate carboxylase subunit A {ECO:0000313|EMBL:EAU61643.1};
DE EC=6.4.1.1 {ECO:0000313|EMBL:EAU61643.1};
GN ORFNames=STIAU_2385 {ECO:0000313|EMBL:EAU61643.1};
OS Stigmatella aurantiaca (strain DW4/3-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=378806 {ECO:0000313|EMBL:EAU61643.1, ECO:0000313|Proteomes:UP000032702};
RN [1] {ECO:0000313|EMBL:EAU61643.1, ECO:0000313|Proteomes:UP000032702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:EAU61643.1,
RC ECO:0000313|Proteomes:UP000032702};
RA Nierman W.C.;
RL Submitted (APR-2006) 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:EAU61643.1}.
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DR EMBL; AAMD01000380; EAU61643.1; -; Genomic_DNA.
DR AlphaFoldDB; Q08MD5; -.
DR PATRIC; fig|378806.16.peg.320; -.
DR Proteomes; UP000032702; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EAU61643.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:EAU61643.1}.
FT DOMAIN 1..428
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 103..300
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 455..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 484 AA; 53076 MW; 76D5FD51025AEAA3 CRC64;
MRTCKELGIP TVAVYSEADR SALHVRMADQ AYFVGPPPSR ESYLVQERIL EVARHAGADA
IHPGYGFLSE NASFVRACEK AGITFIGPPA SAMDAMGEKT RARQNMIQAG VPVVPGTTEP
IATQEEALAY AQKIGFPVML KAAGGGGGKG MRKVEKTEEF DSAWRSAKSE ALNAFGNDAV
YIEKYLDKPH HVEIQVFADQ YGTTVHLGER ECSAQRRHQK VVEETPSPIL TPELRAQMGE
VAVKAAKAVN YVGAGTVEFL VDAHRNFYFL EMNTRLQVEH PVTEWVTGLD LVALQIKVAE
GEKLPFTSTV PPRGHSIEVR IYAEDPARNF MPSPGKIQYL RVPGGPNVRD DSGVFAGFTV
PNFYDPMISK LSVWAPTRAE AIARAQRALS EYVVKGITTN TRYLKAILAH PEFAGGDYDT
SFLTREHTVL LGGEDPKLNE VALLASAVFA HQRDQKRAKT LPQKASPGTG GLSAWRMSLR
TRRR
//
