ID B8J4B4_DESDA Unreviewed; 484 AA.
AC B8J4B4;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Pyruvate carboxylase {ECO:0000313|EMBL:ACL48372.1};
DE EC=6.4.1.1 {ECO:0000313|EMBL:ACL48372.1};
GN OrderedLocusNames=Ddes_0460 {ECO:0000313|EMBL:ACL48372.1};
OS Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=525146 {ECO:0000313|EMBL:ACL48372.1};
RN [1] {ECO:0000313|EMBL:ACL48372.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27774 {ECO:0000313|EMBL:ACL48372.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Hazen T.C.;
RT "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT ATCC 27774.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001358; ACL48372.1; -; Genomic_DNA.
DR AlphaFoldDB; B8J4B4; -.
DR STRING; 525146.Ddes_0460; -.
DR KEGG; dds:Ddes_0460; -.
DR eggNOG; COG0439; Bacteria.
DR HOGENOM; CLU_000395_3_2_7; -.
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; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; PTHR48095:SF2; BIOTIN CARBOXYLASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 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; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ACL48372.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:ACL48372.1}.
FT DOMAIN 16..484
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 137..357
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 484 AA; 54623 MW; B3988EDA1F14831A CRC64;
MRETGLDNAQ ETIPLHKHKI LVANRGEIAM RIMRACRKLG VAFTAIFTAE DAASGHVRLA
REEGGEKSLF RVSSYHDANE LMSVADEAGC TAVHPGYGFF AEDFRFARRV TKRDRKLVFI
GPSWKIIREL GDKINTKRLA RSLGVPTVPG SDRPIYDEME AERIAKSIFE FQAQQGITRP
LVLVKASAGG GGMGIEEVYD PDQFRSVYRR IRNYALRQFK DEGVLIEQRI TDFNHLEVQV
VSDRTGINPV HFGTRNCSIQ STGLQKRIEV APGFVPEEIK YTFDAGKVLK DIVHYSLTMA
RKVGYDNVGT WEWIVTRKGE PFLMEVNTRI QVENGVSARI SKVKGQGDVD IIAEQIRIGL
GDPLGYAQDD ITFDGVGIEY RLIAEDPDSN FTPWVGRIER FQWKEQPWLT MLTHVPTQEP
YEIPTEFDPN LALAIIWGKD LEEAKARGLE FLHDLRLEGH NGAGDTLKSN VNFLAANTER
ILRF
//
