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Database: UniProt
Entry: A0A316C6S3_PSESE
LinkDB: A0A316C6S3_PSESE
Original site: A0A316C6S3_PSESE 
ID   A0A316C6S3_PSESE        Unreviewed;      1012 AA.
AC   A0A316C6S3;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Pyruvate carboxylase {ECO:0000313|EMBL:PWJ84973.1};
GN   ORFNames=C7441_104241 {ECO:0000313|EMBL:PWJ84973.1};
OS   Pseudaminobacter salicylatoxidans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Pseudaminobacter.
OX   NCBI_TaxID=93369 {ECO:0000313|EMBL:PWJ84973.1, ECO:0000313|Proteomes:UP000245396};
RN   [1] {ECO:0000313|EMBL:PWJ84973.1, ECO:0000313|Proteomes:UP000245396}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6986 {ECO:0000313|EMBL:PWJ84973.1,
RC   ECO:0000313|Proteomes:UP000245396};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAY-2018) 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:PWJ84973.1}.
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DR   EMBL; QGGG01000004; PWJ84973.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316C6S3; -.
DR   STRING; 1192868.GCA_000304395_02815; -.
DR   Proteomes; UP000245396; 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:InterPro.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:InterPro.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.10.600.10; pyruvate carboxylase f1077a mutant domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
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; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR000891; PYR_CT.
DR   InterPro; IPR005930; Pyruv_COase.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   NCBIfam; TIGR01235; pyruv_carbox; 1.
DR   PANTHER; PTHR43778; PYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR43778:SF2; PYRUVATE CARBOXYLASE, MITOCHONDRIAL; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF02436; PYC_OADA; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF89000; post-HMGL 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.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:PWJ84973.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245396}.
FT   DOMAIN          2..462
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          128..326
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          539..807
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   1012 AA;  111290 MW;  C462C9A5A3DFEC41 CRC64;
     MPISKILVAN RSEIAIRVFR AANELGLKTV AIWAEEDKYS LHRFKADESY QVGRGPHLTR
     DLGPIESYLS IEEVLRVAKL SGADAIHPGY GLLAESPEFA EACAEAGITF IGPRPDTMRR
     LGNKVAARNL AVEVGVPVIP ATDPLPDDVE AVKKLAADVG YPLMLKASWG GGGRGMRVIR
     SEADLAREVM EGKREAKAAF GKDEVYLEKL IERARHVEVQ VLGDTHGNAV HLFERDCSIQ
     RRNQKVVERA PAPYLDAVQR GELCDHALKI ARATDYVGAG TVEFLMDADS GKFYFIEVNP
     RIQVEHTVTE EVTGIDIVKA QIHILNGLAI GKPETGVPNQ SEIRLNGHAL QCRITTEDPE
     HNFIPDYGRI TAYRGATGFG IRLDGGTAYS GAVITRYYDP LLEKVTAWAP TPSEAIARMH
     RALREFRIRG VSTNLTFLEA IITHPSFQSN SYTTKFIDST PELFAQVKRQ DRATKLLNYL
     ADVTVNGHPE TRGRALPDPE AAAPVIPWFT GSIPDGTKQR FDALGPQKFA AWMREQKQVL
     FTDTTMRDAH QSLLATRVRT YDIARIAGTY ARALPQLLSL ECWGGATFDV AMRFLTEDPW
     ERLSKVREAA PNILLQMLLR GANGVGYTNY PDNVVQHFVK QAAAGGIDLF RVFDCLNWVE
     SMRVAMDAVL AEGKLCEAAI CYTGDMLDPN RSKYDLKYYV GLTRELEAAG AHIISLKDMG
     GLLKPAAARV LFKALREATD LPIHFHTHDT SGLGAATVLA AAEAGVDAVD AAMDAFSGNT
     SQPCLGSIVQ ALRGDPRDPG LDPEWIRRIS FYWEAVRNQY AAFESDLKGP ASEVYLHEMP
     GGQFTNLKEQ ARSLGLETRW HEVAQAYHDV NLMFGDIVKV TPSSKVVGDM ALMMVSQDLT
     VTDVENPDKD IAFPESVVAM LRGDLGQAPG GWPAALQKKA LKGEKPITVR PGSLLKPADL
     AASRKGLEEK LGRKVSEFEF ASWLMYPKVF SDFAATQETY GPVSVLPTPV YF
//
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